Input: What are the treatments for congenital generalized lipodystrophy ?

Output: These resources address the diagnosis or management of congenital generalized lipodystrophy:  - Gene Review: Gene Review: Berardinelli-Seip Congenital Lipodystrophy  - Genetic Testing Registry: Berardinelli-Seip congenital lipodystrophy  - MedlinePlus Encyclopedia: Hypertrophic Cardiomypathy  - University of Texas Southwestern Medical Center: Lipodystrophy   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) myoclonic epilepsy with ragged-red fibers ?

Output: Myoclonic epilepsy with ragged-red fibers (MERRF) is a disorder that affects many parts of the body, particularly the muscles and nervous system. In most cases, the signs and symptoms of this disorder appear during childhood or adolescence. The features of MERRF vary widely among affected individuals, even among members of the same family.  MERRF is characterized by muscle twitches (myoclonus), weakness (myopathy), and progressive stiffness (spasticity). When the muscle cells of affected individuals are stained and viewed under a microscope, these cells usually appear abnormal. These abnormal muscle cells are called ragged-red fibers. Other features of MERRF include recurrent seizures (epilepsy), difficulty coordinating movements (ataxia), a loss of sensation in the extremities (peripheral neuropathy), and slow deterioration of intellectual function (dementia). People with this condition may also develop hearing loss or optic atrophy, which is the degeneration (atrophy) of nerve cells that carry visual information from the eyes to the brain. Affected individuals sometimes have short stature and a form of heart disease known as cardiomyopathy. Less commonly, people with MERRF develop fatty tumors, called lipomas, just under the surface of the skin. </s>


Input: How many people are affected by myoclonic epilepsy with ragged-red fibers ?

Output: MERRF is a rare condition; its prevalence is unknown. MERRF is part of a group of conditions known as mitochondrial disorders, which affect an estimated 1 in 5,000 people worldwide. </s>


Input: What are the genetic changes related to myoclonic epilepsy with ragged-red fibers ?

Output: Mutations in the MT-TK gene are the most common cause of MERRF, occurring in more than 80 percent of all cases. Less frequently, mutations in the MT-TL1, MT-TH, and MT-TS1 genes have been reported to cause the signs and symptoms of MERRF. People with mutations in the MT-TL1, MT-TH, or MT-TS1 gene typically have signs and symptoms of other mitochondrial disorders as well as those of MERRF.  The MT-TK, MT-TL1, MT-TH, and MT-TS1 genes are contained in mitochondrial DNA (mtDNA). Mitochondria are structures within cells that use oxygen to convert the energy from food into a form cells can use through a process called oxidative phosphorylation. Although most DNA is packaged in chromosomes within the nucleus, mitochondria also have a small amount of their own DNA. The genes associated with MERRF provide instructions for making molecules called transfer RNAs, which are chemical cousins of DNA. These molecules help assemble protein building blocks called amino acids into full-length, functioning proteins within mitochondria. These proteins perform the steps of oxidative phosphorylation.  Mutations that cause MERRF impair the ability of mitochondria to make proteins, use oxygen, and produce energy. These mutations particularly affect organs and tissues with high energy requirements, such as the brain and muscles. Researchers have not determined how changes in mtDNA lead to the specific signs and symptoms of MERRF.  A small percentage of MERRF cases are caused by mutations in other mitochondrial genes, and in some cases the cause of the condition is unknown. </s>


Input: Is myoclonic epilepsy with ragged-red fibers inherited ?

Output: MERRF is inherited in a mitochondrial pattern, which is also known as maternal inheritance. This pattern of inheritance applies to genes contained in mtDNA. Because egg cells, but not sperm cells, contribute mitochondria to the developing embryo, children can only inherit disorders resulting from mtDNA mutations from their mother. These disorders can appear in every generation of a family and can affect both males and females, but fathers do not pass traits associated with changes in mtDNA to their children.  In most cases, people with MERRF inherit an altered mitochondrial gene from their mother, who may or may not show symptoms of the disorder. Less commonly, the disorder results from a new mutation in a mitochondrial gene and occurs in people with no family history of MERRF. </s>


Input: What are the treatments for myoclonic epilepsy with ragged-red fibers ?

Output: These resources address the diagnosis or management of MERRF:  - Gene Review: Gene Review: MERRF  - Genetic Testing Registry: Myoclonus with epilepsy with ragged red fibers  - Kennedy Krieger Institute: Mitochondrial Disorders  - MedlinePlus Encyclopedia: Lipoma  - MedlinePlus Encyclopedia: Optic nerve atrophy  - MedlinePlus Encyclopedia: Peripheral Neuropathy  - MitoAction: Tips and Tools for Living with Mito  - United Mitochondrial Disease Foundation: Treatments and Therapies   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) multiminicore disease ?

Output: Multiminicore disease is a disorder that primarily affects muscles used for movement (skeletal muscles). This condition causes muscle weakness and related health problems that range from mild to life-threatening.  Researchers have identified at least four forms of multiminicore disease, which can be distinguished by their characteristic signs and symptoms. The most common form, called the classic form, causes muscle weakness beginning in infancy or early childhood. This weakness is most noticeable in muscles of the trunk and neck (axial muscles) and is less severe in the arm and leg muscles. Muscle weakness causes affected infants to appear "floppy" (hypotonic) and can delay the development of motor skills such as sitting, standing, and walking. The disease causes muscles of the ribcage and spine to stiffen. When combined with weakness of the muscles needed for breathing, this stiffness leads to severe or life-threatening respiratory problems. Almost all children with multiminicore disease develop an abnormal curvature of the spine (scoliosis), which appears during childhood and steadily worsens over time.  Other forms of multiminicore disease have different patterns of signs and symptoms. They are less common than the classic form, together accounting for about 25 percent of all cases. The atypical forms of the condition tend to be milder and cause few or no problems with breathing. The moderate form with hand involvement causes muscle weakness and looseness of the joints, particularly in the arms and hands. Another form of multiminicore disease, known as the antenatal form with arthrogryposis, is characterized by stiff, rigid joints throughout the body (arthrogryposis), distinctive facial features, and other birth defects. Paralysis of the eye muscles (external ophthalmoplegia) is a primary feature of another atypical form of multiminicore disease. This form of the condition also causes general muscle weakness and feeding difficulties that appear in the first year of life.  Many people with multiminicore disease also have an increased risk of a developing a severe reaction to certain drugs used during surgery and other invasive procedures. This reaction is called malignant hyperthermia. Malignant hyperthermia occurs in response to some anesthetic gases, which are used to block the sensation of pain, and with a particular type of muscle relaxant. If given these drugs, people at risk for malignant hyperthermia may experience muscle rigidity, breakdown of muscle fibers (rhabdomyolysis), a high fever, increased acid levels in the blood and other tissues (acidosis), and a rapid heart rate. The complications of malignant hyperthermia can be life-threatening unless they are treated promptly.  Multiminicore disease gets its name from small, disorganized areas called minicores, which are found in muscle fibers of many affected individuals. These abnormal regions can only be seen under a microscope. Although the presence of minicores can help doctors diagnose multiminicore disease, it is unclear how they are related to muscle weakness and the other features of this condition. </s>


Input: How many people are affected by multiminicore disease ?

Output: Multiminicore disease is thought to be a rare disorder, although its incidence is unknown. </s>


Input: What are the genetic changes related to multiminicore disease ?

Output: Mutations in the RYR1 and SEPN1 genes cause multiminicore disease.  The severe, classic form of multiminicore disease is usually caused by mutations in the SEPN1 gene. This gene provides instructions for making a protein called selenoprotein N. Although its function is unknown, researchers suspect that this protein may play a role in the formation of muscle tissue before birth. It may also be important for normal muscle function after birth. It is unclear, however, how mutations in the SEPN1 gene lead to muscle weakness and the other features of multiminicore disease.  Atypical forms of multiminicore disease often result from mutations in the RYR1 gene. RYR1 mutations are also associated with an increased risk of malignant hyperthermia. This gene provides instructions for making a protein called ryanodine receptor 1, which plays an essential role in skeletal muscles. For the body to move normally, these muscles must tense (contract) and relax in a coordinated way. Muscle contractions are triggered by the flow of charged atoms (ions) into muscle cells. In response to certain signals, the ryanodine receptor 1 protein forms a channel that releases stored calcium ions within muscle cells. The resulting increase in calcium ion concentration inside muscle cells stimulates muscle fibers to contract.  Mutations in the RYR1 gene change the structure and function of the ryanodine receptor 1 protein. Some mutations may lead to problems with regulation of the RYR1 channel, while other mutations appear to change the shape of the channel in such a way that calcium ions cannot flow through properly. A disruption in calcium ion transport prevents muscles from contracting normally, leading to the muscle weakness characteristic of multiminicore disease.  In some affected families, the genetic cause of the disorder has not been found. Mutations in genes other than SEPN1 and RYR1 may underlie the condition in these families. </s>


Input: Is multiminicore disease inherited ?

Output: This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. </s>


Input: What are the treatments for multiminicore disease ?

Output: These resources address the diagnosis or management of multiminicore disease:  - Gene Review: Gene Review: Multiminicore Disease  - Genetic Testing Registry: Minicore myopathy with external ophthalmoplegia  - Genetic Testing Registry: Minicore myopathy, antenatal onset, with arthrogryposis  - Genetic Testing Registry: Multiminicore Disease  - MedlinePlus Encyclopedia: Malignant Hyperthermia   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) episodic ataxia ?

Output: Episodic ataxia is a group of related conditions that affect the nervous system and cause problems with movement. People with episodic ataxia have recurrent episodes of poor coordination and balance (ataxia). During these episodes, many people also experience dizziness (vertigo), nausea and vomiting, migraine headaches, blurred or double vision, slurred speech, and ringing in the ears (tinnitus). Seizures, muscle weakness, and paralysis affecting one side of the body (hemiplegia) may also occur during attacks. Additionally, some affected individuals have a muscle abnormality called myokymia during or between episodes. This abnormality can cause muscle cramping, stiffness, and continuous, fine muscle twitching that appears as rippling under the skin.  Episodes of ataxia and other symptoms can begin anytime from early childhood to adulthood. They can be triggered by environmental factors such as emotional stress, caffeine, alcohol, certain medications, physical activity, and illness. The frequency of attacks ranges from several per day to one or two per year. Between episodes, some affected individuals continue to experience ataxia, which may worsen over time, as well as involuntary eye movements called nystagmus.  Researchers have identified at least seven types of episodic ataxia, designated type 1 through type 7. The types are distinguished by their pattern of signs and symptoms, age of onset, length of attacks, and, when known, genetic cause. </s>


Input: How many people are affected by episodic ataxia ?

Output: Episodic ataxia is uncommon, affecting less than 1 in 100,000 people. Only types 1 and 2 have been identified in more than one family, and type 2 is by far the most common form of the condition. </s>


Input: What are the genetic changes related to episodic ataxia ?

Output: Episodic ataxia can be caused by mutations in several genes that play important roles in the nervous system. Three of these genes, KCNA1, CACNA1A, and CACNB4, provide instructions for making proteins that are involved in the transport of charged atoms (ions) across cell membranes. The movement of these ions is critical for normal signaling between nerve cells (neurons) in the brain and other parts of the nervous system. Mutations in the KCNA1, CACNA1A, and CACNB4 genes are responsible for episodic ataxia types 1, 2, and 5, respectively.  Mutations in the SLC1A3 gene have been found to cause episodic ataxia type 6. This gene provides instructions for making a protein that transports a brain chemical (neurotransmitter) called glutamate. Neurotransmitters, including glutamate, allow neurons to communicate by relaying chemical signals from one neuron to another.  Researchers believe that mutations in the KCNA1, CACNA1A, CACNB4, and SLC1A3 genes alter the transport of ions and glutamate in the brain, which causes certain neurons to become overexcited and disrupts normal communication between these cells. Although changes in chemical signaling in the brain underlie the recurrent attacks seen in people with episodic ataxia, it is unclear how mutations in these genes cause the specific features of the disorder.  The genetic causes of episodic ataxia types 3, 4, and 7 have not been identified. Researchers are looking for additional genes that can cause episodic ataxia. </s>


Input: Is episodic ataxia inherited ?

Output: This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder.  In some cases, an affected person inherits the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. </s>


Input: What are the treatments for episodic ataxia ?

Output: These resources address the diagnosis or management of episodic ataxia:  - Consortium for Clinical Investigations of Neurological Channelopathies (CINCH)  - Gene Review: Gene Review: Episodic Ataxia Type 1  - Gene Review: Gene Review: Episodic Ataxia Type 2  - Genetic Testing Registry: Episodic ataxia type 1  - Genetic Testing Registry: Episodic ataxia type 2  - Genetic Testing Registry: Episodic ataxia, type 3  - Genetic Testing Registry: Episodic ataxia, type 4  - Genetic Testing Registry: Episodic ataxia, type 7  - MedlinePlus Encyclopedia: Movement - uncoordinated  - MedlinePlus Encyclopedia: Vertigo-associated disorders   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) pyruvate dehydrogenase deficiency ?

Output: Pyruvate dehydrogenase deficiency is characterized by the buildup of a chemical called lactic acid in the body and a variety of neurological problems. Signs and symptoms of this condition usually first appear shortly after birth, and they can vary widely among affected individuals. The most common feature is a potentially life-threatening buildup of lactic acid (lactic acidosis), which can cause nausea, vomiting, severe breathing problems, and an abnormal heartbeat. People with pyruvate dehydrogenase deficiency usually have neurological problems as well. Most have delayed development of mental abilities and motor skills such as sitting and walking. Other neurological problems can include intellectual disability, seizures, weak muscle tone (hypotonia), poor coordination, and difficulty walking. Some affected individuals have abnormal brain structures, such as underdevelopment of the tissue connecting the left and right halves of the brain (corpus callosum), wasting away (atrophy) of the exterior part of the brain known as the cerebral cortex, or patches of damaged tissue (lesions) on some parts of the brain. Because of the severe health effects, many individuals with pyruvate dehydrogenase deficiency do not survive past childhood, although some may live into adolescence or adulthood. </s>


Input: How many people are affected by pyruvate dehydrogenase deficiency ?

Output: Pyruvate dehydrogenase deficiency is believed to be a rare condition; however, its prevalence is unknown. </s>


Input: What are the genetic changes related to pyruvate dehydrogenase deficiency ?

Output: The genes involved in pyruvate dehydrogenase deficiency each provide instructions for making a protein that is a component of a group of proteins called the pyruvate dehydrogenase complex. This complex plays an important role in the pathways that convert the energy from food into a form that cells can use. The pyruvate dehydrogenase complex converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. This conversion is essential to begin the series of chemical reactions that produce energy for cells.  The pyruvate dehydrogenase complex is made up of multiple copies of several enzymes called E1, E2, and E3, each of which performs part of the chemical reaction that converts pyruvate to acetyl-CoA. In addition, other proteins included in the complex ensure its proper function. One of these proteins, E3 binding protein, attaches E3 to the complex and provides the correct structure for the complex to perform its function. Other associated proteins control the activity of the complex: pyruvate dehydrogenase phosphatase turns on (activates) the complex, while pyruvate dehydrogenase kinase turns off (inhibits) the complex.  The E1 enzyme, also called pyruvate dehydrogenase, is composed of four parts (subunits): two alpha subunits (called E1 alpha) and two beta subunits (called E1 beta). Mutations in the gene that provides instructions for making E1 alpha, the PDHA1 gene, are the most common cause of pyruvate dehydrogenase deficiency, accounting for approximately 80 percent of cases. These mutations lead to a shortage of E1 alpha protein or result in an abnormal protein that cannot function properly. A decrease in functional E1 alpha leads to reduced activity of the pyruvate dehydrogenase complex.  Other components of the pyruvate dehydrogenase complex are also involved in pyruvate dehydrogenase deficiency. Mutations in the genes that provide instructions for E1 beta (the PDHB gene), the E2 enzyme (the DLAT gene), E3 binding protein (the PDHX gene), and pyruvate dehydrogenase phosphatase (the PDP1 gene) have been identified in people with this condition. Although it is unclear how mutations in each of these genes affect the complex, reduced functioning of one component of the complex appears to impair the activity of the whole complex. As with PDHA1 gene mutations, changes in these other genes lead to a reduction of pyruvate dehydrogenase complex activity.  With decreased function of this complex, pyruvate builds up and is converted in another chemical reaction to lactic acid. The excess lactic acid causes lactic acidosis in affected individuals. In addition, the production of cellular energy is diminished. The brain, which requires especially large amounts of energy, is severely affected, resulting in the neurological problems associated with pyruvate dehydrogenase deficiency. </s>


Input: Is pyruvate dehydrogenase deficiency inherited ?

Output: Pyruvate dehydrogenase deficiency can have different inheritance patterns. When the condition is caused by mutations in the PDHA1 gene, it is inherited in an X-linked recessive pattern. The PDHA1 gene is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would usually have to occur in both copies of the gene to cause the disorder. However, in pyruvate dehydrogenase deficiency, one altered copy of the PDHA1 gene is sufficient to cause the disorder, because the X chromosome with the normal copy of the PDHA1 gene is turned off through a process called X-inactivation.  Early in embryonic development in females, one of the two X chromosomes is permanently inactivated in somatic cells (cells other than egg and sperm cells). X-inactivation ensures that females, like males, have only one active copy of the X chromosome in each body cell. Usually X-inactivation occurs randomly, such that each X chromosome is active in about half of the body cells. Sometimes X-inactivation is not random, and one X chromosome is active in more than half of cells. When X-inactivation does not occur randomly, it is called skewed X-inactivation.  Research shows that females with pyruvate dehydrogenase deficiency caused by mutation of the PDHA1 gene have skewed X-inactivation, which results in the inactivation of the X chromosome with the normal copy of the PDHA1 gene in most cells of the body. This skewed X-inactivation causes the chromosome with the mutated PDHA1 gene to be expressed in more than half of cells.  When caused by mutations in the other associated genes, pyruvate dehydrogenase deficiency is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. </s>


Input: What are the treatments for pyruvate dehydrogenase deficiency ?

Output: These resources address the diagnosis or management of pyruvate dehydrogenase deficiency:  - Genetic Testing Registry: Pyruvate dehydrogenase E1-beta deficiency  - Genetic Testing Registry: Pyruvate dehydrogenase E2 deficiency  - Genetic Testing Registry: Pyruvate dehydrogenase E3-binding protein deficiency  - Genetic Testing Registry: Pyruvate dehydrogenase complex deficiency  - Genetic Testing Registry: Pyruvate dehydrogenase phosphatase deficiency   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) phosphoglycerate mutase deficiency ?

Output: Phosphoglycerate mutase deficiency is a disorder that primarily affects muscles used for movement (skeletal muscles). Beginning in childhood or adolescence, affected individuals experience muscle aches or cramping following strenuous physical activity. Some people with this condition also have recurrent episodes of myoglobinuria. Myoglobinuria occurs when muscle tissue breaks down abnormally and releases a protein called myoglobin, which is processed by the kidneys and released in the urine. If untreated, myoglobinuria can lead to kidney failure.  In some cases of phosphoglycerate mutase deficiency, microscopic tube-shaped structures called tubular aggregates are seen in muscle fibers. It is unclear how tubular aggregates are associated with the signs and symptoms of the disorder. </s>


Input: How many people are affected by phosphoglycerate mutase deficiency ?

Output: Phosphoglycerate mutase deficiency is a rare condition; about 15 affected people have been reported in the medical literature. Most affected individuals have been African American. </s>


Input: What are the genetic changes related to phosphoglycerate mutase deficiency ?

Output: Phosphoglycerate mutase deficiency is caused by mutations in the PGAM2 gene. This gene provides instructions for making an enzyme called phosphoglycerate mutase, which is involved in a critical energy-producing process in cells known as glycolysis. During glycolysis, the simple sugar glucose is broken down to produce energy.  The version of phosphoglycerate mutase produced from the PGAM2 gene is found primarily in skeletal muscle cells. Mutations in the PGAM2 gene greatly reduce the activity of phosphoglycerate mutase, which disrupts energy production in these cells. This defect underlies the muscle cramping and myoglobinuria that occur after strenuous exercise in affected individuals. </s>


Input: Is phosphoglycerate mutase deficiency inherited ?

Output: This condition is inherited in an autosomal recessive pattern, which means both copies of the PGAM2 gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. However, people who carry one altered copy of the PGAM2 gene may have some features of phosphoglycerate mutase deficiency, including episodes of exercise-induced muscle cramping and myoglobinuria. </s>


Input: What are the treatments for phosphoglycerate mutase deficiency ?

Output: These resources address the diagnosis or management of phosphoglycerate mutase deficiency:  - Genetic Testing Registry: Glycogen storage disease type X   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) Lenz microphthalmia syndrome ?

Output: Lenz microphthalmia syndrome is a condition characterized by abnormal development of the eyes and several other parts of the body. It occurs almost exclusively in males.  The eye abnormalities associated with Lenz microphthalmia syndrome can affect one or both eyes. People with this condition are born with eyeballs that are abnormally small (microphthalmia) or absent (anophthalmia), leading to vision loss or blindness. Other eye problems can include clouding of the lens (cataract), involuntary eye movements (nystagmus), a gap or split in structures that make up the eye (coloboma), and a higher risk of an eye disease called glaucoma.  Abnormalities of the ears, teeth, hands, skeleton, and urinary system are also frequently seen in Lenz microphthalmia syndrome. Less commonly, heart defects have been reported in affected individuals. Many people with this condition have delayed development or intellectual disability ranging from mild to severe. </s>


Input: How many people are affected by Lenz microphthalmia syndrome ?

Output: Lenz microphthalmia syndrome is a very rare condition; its incidence is unknown. It has been identified in only a few families worldwide. </s>


Input: What are the genetic changes related to Lenz microphthalmia syndrome ?

Output: Mutations in at least two genes on the X chromosome are thought to be responsible for Lenz microphthalmia syndrome. Only one of these genes, BCOR, has been identified.  The BCOR gene provides instructions for making a protein called the BCL6 corepressor. This protein helps regulate the activity of other genes. Little is known about the protein's function, although it appears to play an important role in early embryonic development. A mutation in the BCOR gene has been found in one family with Lenz microphthalmia syndrome. This mutation changes the structure of the BCL6 corepressor protein, which disrupts the normal development of the eyes and several other organs and tissues before birth.  Researchers are working to determine whether Lenz microphthalmia syndrome is a single disorder with different genetic causes or two very similar disorders, each caused by mutations in a different gene. They are searching for a second gene on the X chromosome that may underlie additional cases of the disorder. </s>


Input: Is Lenz microphthalmia syndrome inherited ?

Output: This condition is inherited in an X-linked recessive pattern. The gene associated with this condition is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. </s>


Input: What are the treatments for Lenz microphthalmia syndrome ?

Output: These resources address the diagnosis or management of Lenz microphthalmia syndrome:  - Gene Review: Gene Review: Lenz Microphthalmia Syndrome  - Genetic Testing Registry: Lenz microphthalmia syndrome   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) Prader-Willi syndrome ?

Output: Prader-Willi syndrome is a complex genetic condition that affects many parts of the body. In infancy, this condition is characterized by weak muscle tone (hypotonia), feeding difficulties, poor growth, and delayed development. Beginning in childhood, affected individuals develop an insatiable appetite, which leads to chronic overeating (hyperphagia) and obesity. Some people with Prader-Willi syndrome, particularly those with obesity, also develop type 2 diabetes mellitus (the most common form of diabetes).  People with Prader-Willi syndrome typically have mild to moderate intellectual impairment and learning disabilities. Behavioral problems are common, including temper outbursts, stubbornness, and compulsive behavior such as picking at the skin. Sleep abnormalities can also occur. Additional features of this condition include distinctive facial features such as a narrow forehead, almond-shaped eyes, and a triangular mouth; short stature; and small hands and feet. Some people with Prader-Willi syndrome have unusually fair skin and light-colored hair. Both affected males and affected females have underdeveloped genitals. Puberty is delayed or incomplete, and most affected individuals are unable to have children (infertile). </s>


Input: How many people are affected by Prader-Willi syndrome ?

Output: Prader-Willi syndrome affects an estimated 1 in 10,000 to 30,000 people worldwide. </s>


Input: What are the genetic changes related to Prader-Willi syndrome ?

Output: Prader-Willi syndrome is caused by the loss of function of genes in a particular region of chromosome 15. People normally inherit one copy of this chromosome from each parent. Some genes are turned on (active) only on the copy that is inherited from a person's father (the paternal copy). This parent-specific gene activation is caused by a phenomenon called genomic imprinting.  Most cases of Prader-Willi syndrome (about 70 percent) occur when a segment of the paternal chromosome 15 is deleted in each cell. People with this chromosomal change are missing certain critical genes in this region because the genes on the paternal copy have been deleted, and the genes on the maternal copy are turned off (inactive). In another 25 percent of cases, a person with Prader-Willi syndrome has two copies of chromosome 15 inherited from his or her mother (maternal copies) instead of one copy from each parent. This phenomenon is called maternal uniparental disomy. Rarely, Prader-Willi syndrome can also be caused by a chromosomal rearrangement called a translocation, or by a mutation or other defect that abnormally turns off (inactivates) genes on the paternal chromosome 15.  It appears likely that the characteristic features of Prader-Willi syndrome result from the loss of function of several genes on chromosome 15. Among these are genes that provide instructions for making molecules called small nucleolar RNAs (snoRNAs). These molecules have a variety of functions, including helping to regulate other types of RNA molecules. (RNA molecules play essential roles in producing proteins and in other cell activities.) Studies suggest that the loss of a particular group of snoRNA genes, known as the SNORD116 cluster, may play a major role in causing the signs and symptoms of Prader-Willi syndrome. However, it is unknown how a missing SNORD116 cluster could contribute to intellectual disability, behavioral problems, and the physical features of the disorder.  In some people with Prader-Willi syndrome, the loss of a gene called OCA2 is associated with unusually fair skin and light-colored hair. The OCA2 gene is located on the segment of chromosome 15 that is often deleted in people with this disorder. However, loss of the OCA2 gene does not cause the other signs and symptoms of Prader-Willi syndrome. The protein produced from this gene helps determine the coloring (pigmentation) of the skin, hair, and eyes.  Researchers are studying other genes on chromosome 15 that may also be related to the major signs and symptoms of this condition. </s>


Input: Is Prader-Willi syndrome inherited ?

Output: Most cases of Prader-Willi syndrome are not inherited, particularly those caused by a deletion in the paternal chromosome 15 or by maternal uniparental disomy. These genetic changes occur as random events during the formation of reproductive cells (eggs and sperm) or in early embryonic development. Affected people typically have no history of the disorder in their family.  Rarely, a genetic change responsible for Prader-Willi syndrome can be inherited. For example, it is possible for a genetic change that abnormally inactivates genes on the paternal chromosome 15 to be passed from one generation to the next. </s>


Input: What are the treatments for Prader-Willi syndrome ?

Output: These resources address the diagnosis or management of Prader-Willi syndrome:  - Gene Review: Gene Review: Prader-Willi Syndrome  - Genetic Testing Registry: Prader-Willi syndrome  - MedlinePlus Encyclopedia: Hypotonia  - MedlinePlus Encyclopedia: Prader-Willi Syndrome   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) Parkinson disease ?

Output: Parkinson disease is a progressive disorder of the nervous system. The disorder affects several regions of the brain, especially an area called the substantia nigra that controls balance and movement.  Often the first symptom of Parkinson disease is trembling or shaking (tremor) of a limb, especially when the body is at rest. Typically, the tremor begins on one side of the body, usually in one hand. Tremors can also affect the arms, legs, feet, and face. Other characteristic symptoms of Parkinson disease include rigidity or stiffness of the limbs and torso, slow movement (bradykinesia) or an inability to move (akinesia), and impaired balance and coordination (postural instability). These symptoms worsen slowly over time.  Parkinson disease can also affect emotions and thinking ability (cognition). Some affected individuals develop psychiatric conditions such as depression and visual hallucinations. People with Parkinson disease also have an increased risk of developing dementia, which is a decline in intellectual functions including judgment and memory.  Generally, Parkinson disease that begins after age 50 is called late-onset disease. The condition is described as early-onset disease if signs and symptoms begin before age 50. Early-onset cases that begin before age 20 are sometimes referred to as juvenile-onset Parkinson disease. </s>


Input: How many people are affected by Parkinson disease ?

Output: Parkinson disease affects more than 1 million people in North America and more than 4 million people worldwide. In the United States, Parkinson disease occurs in approximately 13 per 100,000 people, and about 60,000 new cases are identified each year.  The late-onset form is the most common type of Parkinson disease, and the risk of developing this condition increases with age. Because more people are living longer, the number of people with this disease is expected to increase in coming decades. </s>


Input: What are the genetic changes related to Parkinson disease ?

Output: Most cases of Parkinson disease probably result from a complex interaction of environmental and genetic factors. These cases are classified as sporadic and occur in people with no apparent history of the disorder in their family. The cause of these sporadic cases remains unclear.  Approximately 15 percent of people with Parkinson disease have a family history of this disorder. Familial cases of Parkinson disease can be caused by mutations in the LRRK2, PARK2, PARK7, PINK1, or SNCA gene, or by alterations in genes that have not been identified. Mutations in some of these genes may also play a role in cases that appear to be sporadic (not inherited).  Alterations in certain genes, including GBA and UCHL1, do not cause Parkinson disease but appear to modify the risk of developing the condition in some families. Variations in other genes that have not been identified probably also contribute to Parkinson disease risk.  It is not fully understood how genetic changes cause Parkinson disease or influence the risk of developing the disorder. Many Parkinson disease symptoms occur when nerve cells (neurons) in the substantia nigra die or become impaired. Normally, these cells produce a chemical messenger called dopamine, which transmits signals within the brain to produce smooth physical movements. When these dopamine-producing neurons are damaged or die, communication between the brain and muscles weakens. Eventually, the brain becomes unable to control muscle movement.  Some gene mutations appear to disturb the cell machinery that breaks down (degrades) unwanted proteins in dopamine-producing neurons. As a result, undegraded proteins accumulate, leading to the impairment or death of these cells. Other mutations may affect the function of mitochondria, the energy-producing structures within cells. As a byproduct of energy production, mitochondria make unstable molecules called free radicals that can damage cells. Cells normally counteract the effects of free radicals before they cause damage, but mutations can disrupt this process. As a result, free radicals may accumulate and impair or kill dopamine-producing neurons.  In most cases of Parkinson disease, protein deposits called Lewy bodies appear in dead or dying dopamine-producing neurons. (When Lewy bodies are not present, the condition is sometimes referred to as parkinsonism.) It is unclear whether Lewy bodies play a role in killing nerve cells or if they are part of the cells' response to the disease. </s>


Input: Is Parkinson disease inherited ?

Output: Most cases of Parkinson disease occur in people with no apparent family history of the disorder. These sporadic cases may not be inherited, or they may have an inheritance pattern that is unknown.  Among familial cases of Parkinson disease, the inheritance pattern differs depending on the gene that is altered. If the LRRK2 or SNCA gene is involved, the disorder is inherited in an autosomal dominant pattern, which means one copy of an altered gene in each cell is sufficient to cause the disorder. In most cases, an affected person has one parent with the condition.  If the PARK2, PARK7, or PINK1 gene is involved, Parkinson disease is inherited in an autosomal recessive pattern. This type of inheritance means that two copies of the gene in each cell are altered. Most often, the parents of an individual with autosomal recessive Parkinson disease each carry one copy of the altered gene but do not show signs and symptoms of the disorder.  When genetic alterations modify the risk of developing Parkinson disease, the inheritance pattern is usually unknown. </s>


Input: What are the treatments for Parkinson disease ?

Output: These resources address the diagnosis or management of Parkinson disease:  - Gene Review: Gene Review: Parkinson Disease Overview  - Genetic Testing Registry: Parkinson disease 1  - Genetic Testing Registry: Parkinson disease 10  - Genetic Testing Registry: Parkinson disease 11  - Genetic Testing Registry: Parkinson disease 12  - Genetic Testing Registry: Parkinson disease 13  - Genetic Testing Registry: Parkinson disease 14  - Genetic Testing Registry: Parkinson disease 15  - Genetic Testing Registry: Parkinson disease 16  - Genetic Testing Registry: Parkinson disease 17  - Genetic Testing Registry: Parkinson disease 18  - Genetic Testing Registry: Parkinson disease 2  - Genetic Testing Registry: Parkinson disease 3  - Genetic Testing Registry: Parkinson disease 4  - Genetic Testing Registry: Parkinson disease 5  - Genetic Testing Registry: Parkinson disease 6, autosomal recessive early-onset  - Genetic Testing Registry: Parkinson disease 7  - Genetic Testing Registry: Parkinson disease 8, autosomal dominant  - Genetic Testing Registry: Parkinson disease, late-onset  - Genetic Testing Registry: Parkinson disease, mitochondrial  - MedlinePlus Encyclopedia: Parkinson's Disease  - Michael J. Fox Foundation for Parkinson's Research: What Drugs Are Used to Treat Parkinson's Disease and How Do They Work?  - National Institute of Neurological Disorders and Stroke: Deep Brain Stimulation for Parkinson's Disease  - Parkinson's Disease Foundation: Diagnosis  - Parkinson's Disease Foundation: Medications & Treatments   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) alpha thalassemia X-linked intellectual disability syndrome ?

Output: Alpha thalassemia X-linked intellectual disability syndrome is an inherited disorder that affects many parts of the body. This condition occurs almost exclusively in males.  Males with alpha thalassemia X-linked intellectual disability syndrome have intellectual disability and delayed development. Their speech is significantly delayed, and most never speak or sign more than a few words. Most affected children have weak muscle tone (hypotonia), which delays motor skills such as sitting, standing, and walking. Some people with this disorder are never able to walk independently.  Almost everyone with alpha thalassemia X-linked intellectual disability syndrome has distinctive facial features, including widely spaced eyes, a small nose with upturned nostrils, and low-set ears. The upper lip is shaped like an upside-down "V," and the lower lip tends to be prominent. These facial characteristics are most apparent in early childhood. Over time, the facial features become coarser, including a flatter face with a shortened nose.  Most affected individuals have mild signs of a blood disorder called alpha thalassemia. This disorder reduces the production of hemoglobin, which is the protein in red blood cells that carries oxygen to cells throughout the body. A reduction in the amount of hemoglobin prevents enough oxygen from reaching the body's tissues. Rarely, affected individuals also have a shortage of red blood cells (anemia), which can cause pale skin, weakness, and fatigue.  Additional features of alpha thalassemia X-linked intellectual disability syndrome include an unusually small head size (microcephaly), short stature, and skeletal abnormalities. Many affected individuals have problems with the digestive system, such as a backflow of stomach acids into the esophagus (gastroesophageal reflux) and chronic constipation. Genital abnormalities are also common; affected males may have undescended testes and the opening of the urethra on the underside of the penis (hypospadias). In more severe cases, the external genitalia do not look clearly male or female (ambiguous genitalia). </s>


Input: How many people are affected by alpha thalassemia X-linked intellectual disability syndrome ?

Output: Alpha thalassemia X-linked intellectual disability syndrome appears to be a rare condition, although its exact prevalence is unknown. More than 200 affected individuals have been reported. </s>


Input: What are the genetic changes related to alpha thalassemia X-linked intellectual disability syndrome ?

Output: Alpha thalassemia X-linked intellectual disability syndrome results from mutations in the ATRX gene. This gene provides instructions for making a protein that plays an essential role in normal development. Although the exact function of the ATRX protein is unknown, studies suggest that it helps regulate the activity (expression) of other genes. Among these genes are HBA1 and HBA2, which are necessary for normal hemoglobin production.  Mutations in the ATRX gene change the structure of the ATRX protein, which likely prevents it from effectively regulating gene expression. Reduced activity of the HBA1 and HBA2 genes causes alpha thalassemia. Abnormal expression of other genes, which have not been identified, probably causes developmental delay, distinctive facial features, and the other signs and symptoms of alpha thalassemia X-linked intellectual disability syndrome. </s>


Input: Is alpha thalassemia X-linked intellectual disability syndrome inherited ?

Output: This condition is inherited in an X-linked recessive pattern. The ATRX gene is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), one working copy of the ATRX gene can usually compensate for the mutated copy. Therefore, females who carry a single mutated ATRX gene almost never have signs of alpha thalassemia X-linked intellectual disability syndrome.  A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. </s>


Input: What are the treatments for alpha thalassemia X-linked intellectual disability syndrome ?

Output: These resources address the diagnosis or management of alpha thalassemia X-linked intellectual disability syndrome:  - Gene Review: Gene Review: Alpha-Thalassemia X-Linked Intellectual Disability Syndrome  - Genetic Testing Registry: ATR-X syndrome  - MedlinePlus Encyclopedia: Ambiguous Genitalia  - MedlinePlus Encyclopedia: Hypospadias   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) atypical hemolytic-uremic syndrome ?

Output: Atypical hemolytic-uremic syndrome is a disease that primarily affects kidney function. This condition, which can occur at any age, causes abnormal blood clots (thrombi) to form in small blood vessels in the kidneys. These clots can cause serious medical problems if they restrict or block blood flow. Atypical hemolytic-uremic syndrome is characterized by three major features related to abnormal clotting: hemolytic anemia, thrombocytopenia, and kidney failure.  Hemolytic anemia occurs when red blood cells break down (undergo hemolysis) prematurely. In atypical hemolytic-uremic syndrome, red blood cells can break apart as they squeeze past clots within small blood vessels. Anemia results if these cells are destroyed faster than the body can replace them. This condition can lead to unusually pale skin (pallor), yellowing of the eyes and skin (jaundice), fatigue, shortness of breath, and a rapid heart rate.  Thrombocytopenia is a reduced level of circulating platelets, which are cell fragments that normally assist with blood clotting. In people with atypical hemolytic-uremic syndrome, fewer platelets are available in the bloodstream because a large number of platelets are used to make abnormal clots. Thrombocytopenia can cause easy bruising and abnormal bleeding.  As a result of clot formation in small blood vessels, people with atypical hemolytic-uremic syndrome experience kidney damage and acute kidney failure that lead to end-stage renal disease (ESRD) in about half of all cases. These life-threatening complications prevent the kidneys from filtering fluids and waste products from the body effectively.  Atypical hemolytic-uremic syndrome should be distinguished from a more common condition called typical hemolytic-uremic syndrome. The two disorders have different causes and different signs and symptoms. Unlike the atypical form, the typical form is caused by infection with certain strains of Escherichia coli bacteria that produce toxic substances called Shiga-like toxins. The typical form is characterized by severe diarrhea and most often affects children younger than 10. The typical form is less likely than the atypical form to involve recurrent attacks of kidney damage that lead to ESRD. </s>


Input: How many people are affected by atypical hemolytic-uremic syndrome ?

Output: The incidence of atypical hemolytic-uremic syndrome is estimated to be 1 in 500,000 people per year in the United States. The atypical form is probably about 10 times less common than the typical form. </s>


Input: What are the genetic changes related to atypical hemolytic-uremic syndrome ?

Output: Atypical hemolytic-uremic syndrome often results from a combination of environmental and genetic factors. Mutations in at least seven genes appear to increase the risk of developing the disorder. Mutations in a gene called CFH are most common; they have been found in about 30 percent of all cases of atypical hemolytic-uremic syndrome. Mutations in the other genes have each been identified in a smaller percentage of cases.  The genes associated with atypical hemolytic-uremic syndrome provide instructions for making proteins involved in a part of the body's immune response known as the complement system. This system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger inflammation, and remove debris from cells and tissues. The complement system must be carefully regulated so it targets only unwanted materials and does not attack the body's healthy cells. The regulatory proteins associated with atypical hemolytic-uremic syndrome protect healthy cells by preventing activation of the complement system when it is not needed.  Mutations in the genes associated with atypical hemolytic-uremic syndrome lead to uncontrolled activation of the complement system. The overactive system attacks cells that line blood vessels in the kidneys, causing inflammation and the formation of abnormal clots. These abnormalities lead to kidney damage and, in many cases, kidney failure and ESRD.  Although gene mutations increase the risk of atypical hemolytic-uremic syndrome, studies suggest that they are often not sufficient to cause the disease. In people with certain genetic changes, the signs and symptoms of the disorder may be triggered by factors including certain medications (such as anticancer drugs), chronic diseases, viral or bacterial infections, cancers, organ transplantation, or pregnancy.  Some people with atypical hemolytic-uremic syndrome do not have any known genetic changes or environmental triggers for the disease. In these cases, the disorder is described as idiopathic. </s>


Input: Is atypical hemolytic-uremic syndrome inherited ?

Output: Most cases of atypical hemolytic-uremic syndrome are sporadic, which means that they occur in people with no apparent history of the disorder in their family. Less than 20 percent of all cases have been reported to run in families. When the disorder is familial, it can have an autosomal dominant or an autosomal recessive pattern of inheritance.  Autosomal dominant inheritance means one copy of an altered gene in each cell is sufficient to increase the risk of the disorder. In some cases, an affected person inherits the mutation from one affected parent. However, most people with the autosomal dominant form of atypical hemolytic-uremic syndrome have no history of the disorder in their family. Because not everyone who inherits a gene mutation will develop the signs and symptoms of the disease, an affected individual may have unaffected relatives who carry a copy of the mutation.  Autosomal recessive inheritance means both copies of a gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. </s>


Input: What are the treatments for atypical hemolytic-uremic syndrome ?

Output: These resources address the diagnosis or management of atypical hemolytic-uremic syndrome:  - Gene Review: Gene Review: Atypical Hemolytic-Uremic Syndrome  - Genetic Testing Registry: Atypical hemolytic uremic syndrome  - Genetic Testing Registry: Atypical hemolytic-uremic syndrome 1  - Genetic Testing Registry: Atypical hemolytic-uremic syndrome 2  - Genetic Testing Registry: Atypical hemolytic-uremic syndrome 3  - Genetic Testing Registry: Atypical hemolytic-uremic syndrome 4  - Genetic Testing Registry: Atypical hemolytic-uremic syndrome 5  - Genetic Testing Registry: Atypical hemolytic-uremic syndrome 6  - MedlinePlus Encyclopedia: Hemolytic Anemia  - MedlinePlus Encyclopedia: Hemolytic-Uremic Syndrome  - MedlinePlus Encyclopedia: Thrombocytopenia  - National Institute of Diabetes and Digestive and Kidney Diseases: Kidney Failure: Choosing a Treatment That's Right for You   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) ALG1-congenital disorder of glycosylation ?

Output: ALG1-congenital disorder of glycosylation (ALG1-CDG, also known as congenital disorder of glycosylation type Ik) is an inherited disorder with varying signs and symptoms that typically develop during infancy and can affect several body systems.  Individuals with ALG1-CDG often have intellectual disability, delayed development, and weak muscle tone (hypotonia). Many affected individuals develop seizures that can be difficult to treat. Individuals with ALG1-CDG may also have movement problems such as involuntary rhythmic shaking (tremor) or difficulties with movement and balance (ataxia).  People with ALG1-CDG often have problems with blood clotting, which can lead to abnormal clotting or bleeding episodes. Additionally, affected individuals may produce abnormally low levels of proteins called antibodies (or immunoglobulins), particularly immunoglobulin G (IgG). Antibodies help protect the body against infection by foreign particles and germs. A reduction in antibodies can make it difficult for affected individuals to fight infections.  Some people with ALG1-CDG have physical abnormalities such as a small head size (microcephaly); unusual facial features; joint deformities called contractures; long, slender fingers and toes (arachnodactyly); or unusually fleshy pads at the tips of the fingers and toes. Eye problems that may occur in people with this condition include eyes that do not point in the same direction (strabismus) or involuntary eye movements (nystagmus). Rarely, affected individuals develop vision loss.  Less common abnormalities that occur in people with ALG1-CDG include respiratory problems, reduced sensation in their arms and legs (peripheral neuropathy), swelling (edema), and gastrointestinal difficulties.  The signs and symptoms of ALG1-CDG are often severe, with affected individuals surviving only into infancy or childhood. However, some people with this condition are more mildly affected and survive into adulthood. </s>


Input: How many people are affected by ALG1-congenital disorder of glycosylation ?

Output: ALG1-CDG appears to be a rare disorder; fewer than 30 affected individuals have been described in the scientific literature. </s>


Input: What are the genetic changes related to ALG1-congenital disorder of glycosylation ?

Output: Mutations in the ALG1 gene cause ALG1-CDG. This gene provides instructions for making an enzyme that is involved in a process called glycosylation. During this process, complex chains of sugar molecules (oligosaccharides) are added to proteins and fats (lipids). Glycosylation modifies proteins and lipids so they can fully perform their functions. The enzyme produced from the ALG1 gene transfers a simple sugar called mannose to growing oligosaccharides at a particular step in the formation of the sugar chain. Once the correct number of sugar molecules are linked together, the oligosaccharide is attached to a protein or lipid.  ALG1 gene mutations lead to the production of an abnormal enzyme with reduced activity. The poorly functioning enzyme cannot add mannose to sugar chains efficiently, and the resulting oligosaccharides are often incomplete. Although the short oligosaccharides can be transferred to proteins and fats, the process is not as efficient as with the full-length oligosaccharide. The wide variety of signs and symptoms in ALG1-CDG are likely due to impaired glycosylation of proteins and lipids that are needed for normal function of many organs and tissues. </s>


Input: Is ALG1-congenital disorder of glycosylation inherited ?

Output: This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. </s>


Input: What are the treatments for ALG1-congenital disorder of glycosylation ?

Output: These resources address the diagnosis or management of ALG1-congenital disorder of glycosylation:  - Gene Review: Gene Review: Congenital Disorders of N-Linked Glycosylation Pathway Overview  - Genetic Testing Registry: Congenital disorder of glycosylation type 1K   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) intestinal pseudo-obstruction ?

Output: Intestinal pseudo-obstruction is a condition characterized by impairment of the muscle contractions that move food through the digestive tract. The condition may arise from abnormalities of the gastrointestinal muscles themselves (myogenic) or from problems with the nerves that control the muscle contractions (neurogenic).  When intestinal pseudo-obstruction occurs by itself, it is called primary or idiopathic intestinal pseudo-obstruction. The disorder can also develop as a complication of another medical condition; in these cases, it is called secondary intestinal pseudo-obstruction.  Intestinal pseudo-obstruction leads to a buildup of partially digested food in the intestines. This buildup can cause abdominal swelling (distention) and pain, nausea, vomiting, and constipation or diarrhea. Affected individuals experience loss of appetite and impaired ability to absorb nutrients, which may lead to malnutrition. These symptoms resemble those of an intestinal blockage (obstruction), but in intestinal pseudo-obstruction no blockage is found.  Some people with intestinal pseudo-obstruction have bladder dysfunction such as an inability to pass urine. Other features of this condition may include decreased muscle tone (hypotonia) or stiffness (spasticity), weakness in the muscles that control eye movement (ophthalmoplegia), intellectual disability, seizures, unusual facial features, or recurrent infections.  Intestinal pseudo-obstruction can occur at any time of life. Its symptoms may range from mild to severe. Some affected individuals may require nutritional support. Depending on the severity of the condition, such support may include nutritional supplements, a feeding tube, or intravenous feedings (parenteral nutrition). </s>


Input: How many people are affected by intestinal pseudo-obstruction ?

Output: Primary intestinal pseudo-obstruction is a rare disorder. Its prevalence is unknown. The prevalence of secondary intestinal pseudo-obstruction is also unknown, but it is believed to be more common than the primary form. </s>


Input: What are the genetic changes related to intestinal pseudo-obstruction ?

Output: In some individuals with primary intestinal pseudo-obstruction, the condition is caused by mutations in the FLNA gene. This gene provides instructions for producing the protein filamin A, which helps build the network of protein filaments (cytoskeleton) that gives structure to cells and allows them to change shape and move. Filamin A attaches (binds) to another protein called actin and helps it form the branching network of filaments that make up the cytoskeleton.  Some individuals with primary intestinal pseudo-obstruction have FLNA gene mutations that result in an abnormally short filamin A protein. Others have duplications or deletions of genetic material in the FLNA gene. Researchers believe that these genetic changes may impair the function of the filamin A protein, causing abnormalities in the cytoskeleton of nerve cells (neurons) in the gastrointestinal tract. These abnormalities interfere with the nerves' ability to produce the coordinated waves of muscle contractions (peristalsis) that move food through the digestive tract.  Deletions or duplications of genetic material that affect the FLNA gene can also include adjacent genes on the X chromosome. Changes in adjacent genes may account for some of the other signs and symptoms that can occur with intestinal pseudo-obstruction.  Secondary intestinal pseudo-obstruction may result from other disorders that damage muscles or nerves, such as Parkinson disease, diabetes, or muscular dystrophy. Additionally, the condition is a feature of an inherited disease called mitochondrial neurogastrointestinal encephalopathy disease (MNGIE disease) that affects the energy-producing centers of cells (mitochondria). Infections, surgery, or certain drugs can also cause secondary intestinal pseudo-obstruction.  In some affected individuals, the cause of intestinal pseudo-obstruction is unknown. Studies suggest that in some cases the condition may result from mutations in other genes that have not been identified. </s>


Input: Is intestinal pseudo-obstruction inherited ?

Output: Intestinal pseudo-obstruction is often not inherited. When it does run in families, it can have different inheritance patterns.  Intestinal pseudo-obstruction caused by FLNA gene mutations is inherited in an X-linked recessive pattern. The FLNA gene is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons.  Intestinal pseudo-obstruction can also be inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. In other families it is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. When intestinal pseudo-obstruction is inherited in an autosomal dominant or autosomal recessive pattern, the genetic cause of the disorder is unknown.  When intestinal pseudo-obstruction is a feature of MNGIE disease, it is inherited in a mitochondrial pattern, which is also known as maternal inheritance. This pattern of inheritance applies to genes contained in mitochondrial DNA (mtDNA). Because egg cells, but not sperm cells, contribute mitochondria to the developing embryo, children can only inherit disorders resulting from mtDNA mutations from their mother. These disorders can appear in every generation of a family and can affect both males and females, but fathers do not pass traits associated with changes in mtDNA to their children.  In some cases, the inheritance pattern is unknown. </s>


Input: What are the treatments for intestinal pseudo-obstruction ?

Output: These resources address the diagnosis or management of intestinal pseudo-obstruction:  - Children's Hospital of Pittsburgh  - Genetic Testing Registry: Intestinal pseudoobstruction neuronal chronic idiopathic X-linked  - Genetic Testing Registry: Natal teeth, intestinal pseudoobstruction and patent ductus  - Genetic Testing Registry: Visceral myopathy familial with external ophthalmoplegia  - Genetic Testing Registry: Visceral neuropathy familial  - Genetic Testing Registry: Visceral neuropathy, familial, autosomal dominant   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) autosomal recessive axonal neuropathy with neuromyotonia ?

Output: Autosomal recessive axonal neuropathy with neuromyotonia is a disorder that affects the peripheral nerves. Peripheral nerves connect the brain and spinal cord to muscles and to sensory cells that detect sensations such as touch, pain, heat, and sound.  Axonal neuropathy, a characteristic feature of this condition, is caused by damage to a particular part of peripheral nerves called axons, which are the extensions of nerve cells (neurons) that transmit nerve impulses. In people with autosomal recessive axonal neuropathy with neuromyotonia, the damage primarily causes progressive weakness and wasting (atrophy) of muscles in the feet, legs, and hands. Muscle weakness may be especially apparent during exercise (exercise intolerance) and can lead to an unusual walking style (gait), frequent falls, and joint deformities (contractures) in the hands and feet. In some affected individuals, axonal neuropathy also causes decreased sensitivity to touch, heat, or cold, particularly in the lower arms or legs.  Another feature of this condition is neuromyotonia (also known as Isaac syndrome). Neuromyotonia results from overactivation (hyperexcitability) of peripheral nerves, which leads to delayed relaxation of muscles after voluntary tensing (contraction), muscle cramps, and involuntary rippling movement of the muscles (myokymia). </s>


Input: How many people are affected by autosomal recessive axonal neuropathy with neuromyotonia ?

Output: Autosomal recessive axonal neuropathy with neuromyotonia is a rare form of inherited peripheral neuropathy. This group of conditions affects an estimated 1 in 2,500 people. The prevalence of autosomal recessive axonal neuropathy with neuromyotonia is unknown. </s>


Input: What are the genetic changes related to autosomal recessive axonal neuropathy with neuromyotonia ?

Output: Autosomal recessive axonal neuropathy with neuromyotonia is caused by mutations in the HINT1 gene. This gene provides instructions for making a protein that is involved in the function of the nervous system; however its specific role is not well understood. Laboratory studies show that the HINT1 protein has the ability to carry out a chemical reaction called hydrolysis that breaks down certain molecules; however, it is not known what effects the reaction has in the body.  HINT1 gene mutations that cause autosomal recessive axonal neuropathy with neuromyotonia lead to production of a HINT1 protein with little or no function. Sometimes the abnormal protein is broken down prematurely. Researchers are working to determine how loss of functional HINT1 protein affects the peripheral nerves and leads to the signs and symptoms of this condition. </s>


Input: Is autosomal recessive axonal neuropathy with neuromyotonia inherited ?

Output: This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. </s>


Input: What are the treatments for autosomal recessive axonal neuropathy with neuromyotonia ?

Output: These resources address the diagnosis or management of autosomal recessive axonal neuropathy with neuromyotonia:  - Genetic Testing Registry: Gamstorp-Wohlfart syndrome   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) ataxia-telangiectasia ?

Output: Ataxia-telangiectasia is a rare inherited disorder that affects the nervous system, immune system, and other body systems. This disorder is characterized by progressive difficulty with coordinating movements (ataxia) beginning in early childhood, usually before age 5. Affected children typically develop difficulty walking, problems with balance and hand coordination, involuntary jerking movements (chorea), muscle twitches (myoclonus), and disturbances in nerve function (neuropathy). The movement problems typically cause people to require wheelchair assistance by adolescence. People with this disorder also have slurred speech and trouble moving their eyes to look side-to-side (oculomotor apraxia). Small clusters of enlarged blood vessels called telangiectases, which occur in the eyes and on the surface of the skin, are also characteristic of this condition.  Affected individuals tend to have high amounts of a protein called alpha-fetoprotein (AFP) in their blood. The level of this protein is normally increased in the bloodstream of pregnant women, but it is unknown why individuals with ataxia-telangiectasia have elevated AFP or what effects it has in these individuals.  People with ataxia-telangiectasia often have a weakened immune system, and many develop chronic lung infections. They also have an increased risk of developing cancer, particularly cancer of blood-forming cells (leukemia) and cancer of immune system cells (lymphoma). Affected individuals are very sensitive to the effects of radiation exposure, including medical x-rays. The life expectancy of people with ataxia-telangiectasia varies greatly, but affected individuals typically live into early adulthood. </s>


Input: How many people are affected by ataxia-telangiectasia ?

Output: Ataxia-telangiectasia occurs in 1 in 40,000 to 100,000 people worldwide. </s>


Input: What are the genetic changes related to ataxia-telangiectasia ?

Output: Mutations in the ATM gene cause ataxia-telangiectasia. The ATM gene provides instructions for making a protein that helps control cell division and is involved in DNA repair. This protein plays an important role in the normal development and activity of several body systems, including the nervous system and immune system. The ATM protein assists cells in recognizing damaged or broken DNA strands and coordinates DNA repair by activating enzymes that fix the broken strands. Efficient repair of damaged DNA strands helps maintain the stability of the cell's genetic information.  Mutations in the ATM gene reduce or eliminate the function of the ATM protein. Without this protein, cells become unstable and die. Cells in the part of the brain involved in coordinating movements (the cerebellum) are particularly affected by loss of the ATM protein. The loss of these brain cells causes some of the movement problems characteristic of ataxia-telangiectasia. Mutations in the ATM gene also prevent cells from responding correctly to DNA damage, which allows breaks in DNA strands to accumulate and can lead to the formation of cancerous tumors. </s>


Input: Is ataxia-telangiectasia inherited ?

Output: Ataxia-telangiectasia is inherited in an autosomal recessive pattern, which means both copies of the ATM gene in each cell have mutations. Most often, the parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but do not show signs and symptoms of the condition.  About 1 percent of the United States population carries one mutated copy and one normal copy of the ATM gene in each cell. These individuals are called carriers. Although ATM mutation carriers do not have ataxia-telangiectasia, they are more likely than people without an ATM mutation to develop cancer; female carriers are particularly at risk for developing breast cancer. Carriers of a mutation in the ATM gene also may have an increased risk of heart disease. </s>


Input: What are the treatments for ataxia-telangiectasia ?

Output: These resources address the diagnosis or management of ataxia-telangiectasia:  - Gene Review: Gene Review: Ataxia-Telangiectasia  - Genetic Testing Registry: Ataxia-telangiectasia syndrome  - MedlinePlus Encyclopedia: Ataxia-Telangiectasia   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) choroideremia ?

Output: Choroideremia is a condition characterized by progressive vision loss that mainly affects males. The first symptom of this condition is usually an impairment of night vision (night blindness), which can occur in early childhood. A progressive narrowing of the field of vision (tunnel vision) follows, as well as a decrease in the ability to see details (visual acuity). These vision problems are due to an ongoing loss of cells (atrophy) in the specialized light-sensitive tissue that lines the back of the eye (retina) and a nearby network of blood vessels (the choroid). The vision impairment in choroideremia worsens over time, but the progression varies among affected individuals. However, all individuals with this condition will develop blindness, most commonly in late adulthood. </s>


Input: How many people are affected by choroideremia ?

Output: The prevalence of choroideremia is estimated to be 1 in 50,000 to 100,000 people. However, it is likely that this condition is underdiagnosed because of its similarities to other eye disorders. Choroideremia is thought to account for approximately 4 percent of all blindness. </s>


Input: What are the genetic changes related to choroideremia ?

Output: Mutations in the CHM gene cause choroideremia. The CHM gene provides instructions for producing the Rab escort protein-1 (REP-1). As an escort protein, REP-1 attaches to molecules called Rab proteins within the cell and directs them to the membranes of various cell compartments (organelles). Rab proteins are involved in the movement of proteins and organelles within cells (intracellular trafficking). Mutations in the CHM gene lead to an absence of REP-1 protein or the production of a REP-1 protein that cannot carry out its protein escort function. This lack of functional REP-1 prevents Rab proteins from reaching and attaching (binding) to the organelle membranes. Without the aid of Rab proteins in intracellular trafficking, cells die prematurely.  The REP-1 protein is active (expressed) throughout the body, as is a similar protein, REP-2. Research suggests that when REP-1 is absent or nonfunctional, REP-2 can perform the protein escort duties of REP-1 in many of the body's tissues. Very little REP-2 protein is present in the retina, however, so it cannot compensate for the loss of REP-1 in this tissue. Loss of REP-1 function and subsequent misplacement of Rab proteins within the cells of the retina causes the progressive vision loss characteristic of choroideremia. </s>


Input: Is choroideremia inherited ?

Output: Choroideremia is inherited in an X-linked recessive pattern. The CHM gene is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation must be present in both copies of the gene to cause the disorder. Males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons.  In X-linked recessive inheritance, a female with one mutated copy of the gene in each cell is called a carrier. She can pass on the altered gene, but usually does not experience signs and symptoms of the disorder. Females who carry a CHM mutation may show small areas of cell loss within the retina that can be observed during a thorough eye examination. These changes can impair vision later in life. </s>


Input: What are the treatments for choroideremia ?

Output: These resources address the diagnosis or management of choroideremia:  - Gene Review: Gene Review: Choroideremia  - Genetic Testing Registry: Choroideremia  - MedlinePlus Encyclopedia: Vision - night blindness  - MedlinePlus Encyclopedia: Visual field   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) pulmonary veno-occlusive disease ?

Output: Pulmonary veno-occlusive disease (PVOD) is characterized by the blockage (occlusion) of the blood vessels that carry oxygen-rich (oxygenated) blood from the lungs to the heart (the pulmonary veins). The occlusion is caused by a buildup of abnormal fibrous tissue in the small veins in the lungs, which narrows the vessels and impairs blood flow. Because blood flow through the lungs is difficult, pressure rises in the vessels that carry blood that needs to be oxygenated to the lungs from the heart (the pulmonary arteries). Increased pressure in these vessels is known as pulmonary arterial hypertension.  The problems with blood flow in PVOD also impair the delivery of oxygenated blood to the rest of the body, which leads to the signs and symptoms of the condition. Shortness of breath (dyspnea) and tiredness (fatigue) during exertion are the most common symptoms of this condition. Other common features include dizziness, a lack of energy (lethargy), difficulty breathing when lying down, and a cough that does not go away. As the condition worsens, affected individuals can develop a bluish tint to the skin (cyanosis), chest pains, fainting spells, and an accumulation of fluid in the lungs (pulmonary edema).  Certain features commonly seen in people with PVOD can be identified using a test called a CT scan. One of these features, which is seen in the lungs of affected individuals, is an abnormality described as centrilobular ground-glass opacities. Affected individuals also have abnormal thickening of certain tissues in the lungs, which is described as septal lines. In addition, lymph nodes in the chest (mediastinal lymph nodes) are abnormally enlarged in people with PVOD.  PVOD can begin at any age, and the blood flow problems worsen over time. Because of the increased blood pressure in the pulmonary arteries, the heart must work harder than normal to pump blood to the lungs, which can eventually lead to fatal heart failure. Most people with this severe disorder do not live more than 2 years after diagnosis. </s>


Input: How many people are affected by pulmonary veno-occlusive disease ?

Output: The exact prevalence of PVOD is unknown. Many cases are likely misdiagnosed as idiopathic pulmonary arterial hypertension, which is increased blood pressure in the pulmonary arteries without a known cause. Research suggests that 5 to 25 percent of people diagnosed with idiopathic pulmonary arterial hypertension have PVOD. Based on these numbers, PVOD is thought to affect an estimated 1 to 2 per 10 million people. </s>


Input: What are the genetic changes related to pulmonary veno-occlusive disease ?

Output: The primary genetic cause of PVOD is mutations in the EIF2AK4 gene. Mutations in other genes may cause a small percentage of cases. Other suspected causes of PVOD include viral infection and exposure to toxic chemicals, including certain chemotherapy drugs.  The protein produced from the EIF2AK4 gene helps cells respond appropriately to changes that could damage the cell. For example, when the level of protein building blocks (amino acids) in a cell falls too low, the activity of the EIF2AK4 protein helps reduce the production of other proteins, which conserves amino acids. The EIF2AK4 gene mutations involved in PVOD likely eliminate functional EIF2AK4 protein; however, it is unknown how absence of this protein's function leads to the pulmonary vessel abnormalities that underlie PVOD. </s>


Input: Is pulmonary veno-occlusive disease inherited ?

Output: When caused by mutations in the EIF2AK4 gene, PVOD is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition.  In contrast, when caused by mutations in another gene, the condition can have an autosomal dominant pattern of inheritance, which means one copy of the altered gene in each cell is sufficient to cause the disorder. In these cases, one parent of an affected individual typically has increased blood pressure in the vessels of the lungs. </s>


Input: What are the treatments for pulmonary veno-occlusive disease ?

Output: These resources address the diagnosis or management of pulmonary veno-occlusive disease:  - Genetic Testing Registry: Pulmonary veno-occlusive disease   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) 3-hydroxyacyl-CoA dehydrogenase deficiency ?

Output: 3-hydroxyacyl-CoA dehydrogenase deficiency is an inherited condition that prevents the body from converting certain fats to energy, particularly during prolonged periods without food (fasting).  Initial signs and symptoms of this disorder typically occur during infancy or early childhood and can include poor appetite, vomiting, diarrhea, and lack of energy (lethargy). Affected individuals can also have muscle weakness (hypotonia), liver problems, low blood sugar (hypoglycemia), and abnormally high levels of insulin (hyperinsulinism). Insulin controls the amount of sugar that moves from the blood into cells for conversion to energy. Individuals with 3-hydroxyacyl-CoA dehydrogenase deficiency are also at risk for complications such as seizures, life-threatening heart and breathing problems, coma, and sudden death. This condition may explain some cases of sudden infant death syndrome (SIDS), which is defined as unexplained death in babies younger than 1 year.  Problems related to 3-hydroxyacyl-CoA dehydrogenase deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections. </s>


Input: How many people are affected by 3-hydroxyacyl-CoA dehydrogenase deficiency ?

Output: The exact incidence of 3-hydroxyacyl-CoA dehydrogenase deficiency is unknown; it has been reported in only a small number of people worldwide. </s>


Input: What are the genetic changes related to 3-hydroxyacyl-CoA dehydrogenase deficiency ?

Output: Mutations in the HADH gene cause 3-hydroxyacyl-CoA dehydrogenase deficiency. The HADH gene provides instructions for making an enzyme called 3-hydroxyacyl-CoA dehydrogenase.  Normally, through a process called fatty acid oxidation, several enzymes work in a step-wise fashion to break down (metabolize) fats and convert them to energy. The 3-hydroxyacyl-CoA dehydrogenase enzyme is required for a step that metabolizes groups of fats called medium-chain fatty acids and short-chain fatty acids.  Mutations in the HADH gene lead to a shortage of 3-hydroxyacyl-CoA dehydrogenase. Medium-chain and short-chain fatty acids cannot be metabolized properly without sufficient levels of this enzyme. As a result, these fatty acids are not converted to energy, which can lead to characteristic features of 3-hydroxyacyl-CoA dehydrogenase deficiency, such as lethargy and hypoglycemia. Medium-chain and short-chain fatty acids that are not broken down can build up in tissues and damage the liver, heart, and muscles, causing serious complications.  Conditions that disrupt the metabolism of fatty acids, including 3-hydroxyacyl-CoA dehydrogenase deficiency, are known as fatty acid oxidation disorders. </s>


Input: Is 3-hydroxyacyl-CoA dehydrogenase deficiency inherited ?

Output: This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. </s>


Input: What are the treatments for 3-hydroxyacyl-CoA dehydrogenase deficiency ?

Output: These resources address the diagnosis or management of 3-hydroxyacyl-CoA dehydrogenase deficiency:  - Baby's First Test  - Genetic Testing Registry: Deficiency of 3-hydroxyacyl-CoA dehydrogenase  - United Mitochondrial Disease Foundation: Treatments & Therapies   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) distal arthrogryposis type 1 ?

Output: Distal arthrogryposis type 1 is a disorder characterized by joint deformities (contractures) that restrict movement in the hands and feet. The term "arthrogryposis" comes from the Greek words for joint (arthro-) and crooked or hooked (gryposis). The characteristic features of this condition include permanently bent fingers and toes (camptodactyly), overlapping fingers, and a hand deformity in which all of the fingers are angled outward toward the fifth finger (ulnar deviation). Clubfoot, which is an inward- and upward-turning foot, is also commonly seen with distal arthrogryposis type 1. The specific hand and foot abnormalities vary among affected individuals. However, this condition typically does not cause any signs and symptoms affecting other parts of the body. </s>


Input: How many people are affected by distal arthrogryposis type 1 ?

Output: Distal arthrogryposis type 1 affects an estimated 1 in 10,000 people worldwide. </s>


Input: What are the genetic changes related to distal arthrogryposis type 1 ?

Output: Distal arthrogryposis type 1 can be caused by mutations in at least two genes: TPM2 and MYBPC1. These genes are active (expressed) in muscle cells, where they interact with other muscle proteins to help regulate the tensing of muscle fibers (muscle contraction). It is unclear how mutations in the TPM2 and MYBPC1 genes lead to the joint abnormalities characteristic of distal arthrogryposis type 1. However, researchers speculate that contractures may be related to problems with muscle contraction that limit the movement of joints before birth.  In some cases, the genetic cause of distal arthrogryposis type 1 is unknown. Researchers are looking for additional genetic changes that may be responsible for this condition. </s>


Input: Is distal arthrogryposis type 1 inherited ?

Output: This condition is inherited in an autosomal dominant pattern, which means one copy of an altered gene in each cell is sufficient to cause the disorder. In many cases, a person with distal arthrogryposis type 1 has a parent and other close family members with the condition. </s>


Input: What are the treatments for distal arthrogryposis type 1 ?

Output: These resources address the diagnosis or management of distal arthrogryposis type 1:  - Genetic Testing Registry: Arthrogryposis multiplex congenita distal type 1  - Merck Manual for Health Care Professionals  - New York University Langone Medical Center   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) Saethre-Chotzen syndrome ?

Output: Saethre-Chotzen syndrome is a genetic condition characterized by the premature fusion of certain skull bones (craniosynostosis). This early fusion prevents the skull from growing normally and affects the shape of the head and face.  Most people with Saethre-Chotzen syndrome have prematurely fused skull bones along the coronal suture, the growth line that goes over the head from ear to ear. Other parts of the skull may be malformed as well. These changes can result in an abnormally shaped head, a high forehead, a low frontal hairline, droopy eyelids (ptosis), widely spaced eyes, and a broad nasal bridge. One side of the face may appear noticeably different from the other (facial asymmetry). Most people with Saethre-Chotzen syndrome also have small, unusually shaped ears.  The signs and symptoms of Saethre-Chotzen syndrome vary widely, even among affected individuals in the same family. This condition can cause mild abnormalities of the hands and feet, such as fusion of the skin between the second and third fingers on each hand and a broad or duplicated first (big) toe. Delayed development and learning difficulties have been reported, although most people with this condition are of normal intelligence. Less common signs and symptoms of Saethre-Chotzen syndrome include short stature, abnormalities of the bones of the spine (the vertebra), hearing loss, and heart defects.  Robinow-Sorauf syndrome is a condition with features similar to those of Saethre-Chotzen syndrome, including craniosynostosis and broad or duplicated great toes. It was once considered a separate disorder, but was found to result from mutations in the same gene and is now thought to be a mild variant of Saethre-Chotzen syndrome. </s>


Input: How many people are affected by Saethre-Chotzen syndrome ?

Output: Saethre-Chotzen syndrome has an estimated prevalence of 1 in 25,000 to 50,000 people. </s>


Input: What are the genetic changes related to Saethre-Chotzen syndrome ?

Output: Mutations in the TWIST1 gene cause Saethre-Chotzen syndrome. The TWIST1 gene provides instructions for making a protein that plays an important role in early development. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of particular genes. The TWIST1 protein is active in cells that give rise to bones, muscles, and other tissues in the head and face. It is also involved in the development of the limbs.  Mutations in the TWIST1 gene prevent one copy of the gene in each cell from making any functional protein. A shortage of the TWIST1 protein affects the development and maturation of cells in the skull, face, and limbs. These abnormalities underlie the signs and symptoms of Saethre-Chotzen syndrome, including the premature fusion of certain skull bones.  A small number of cases of Saethre-Chotzen syndrome have resulted from a structural chromosomal abnormality, such as a deletion or rearrangement of genetic material, in the region of chromosome 7 that contains the TWIST1 gene. When Saethre-Chotzen syndrome is caused by a chromosomal deletion instead of a mutation within the TWIST1 gene, affected children are much more likely to have intellectual disability, developmental delay, and learning difficulties. These features are typically not seen in classic cases of Saethre-Chotzen syndrome. Researchers believe that a loss of other genes on chromosome 7 may be responsible for these additional features. </s>


Input: Is Saethre-Chotzen syndrome inherited ?

Output: This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. In some cases, an affected person inherits the mutation from one affected parent. Other cases may result from new mutations in the gene. These cases occur in people with no history of the disorder in their family.  Some people with a TWIST1 mutation do not have any of the obvious features of Saethre-Chotzen syndrome. These people are still at risk of passing on the gene mutation and may have a child with craniosynostosis and the other typical signs and symptoms of the condition. </s>


Input: What are the treatments for Saethre-Chotzen syndrome ?

Output: These resources address the diagnosis or management of Saethre-Chotzen syndrome:  - Gene Review: Gene Review: Saethre-Chotzen Syndrome  - Genetic Testing Registry: Robinow Sorauf syndrome  - Genetic Testing Registry: Saethre-Chotzen syndrome  - MedlinePlus Encyclopedia: Craniosynostosis  - MedlinePlus Encyclopedia: Skull of a Newborn (image)   These resources from MedlinePlus offer information about the diagnosis and management of various health conditions:  - Diagnostic Tests  - Drug Therapy  - Surgery and Rehabilitation  - Genetic Counseling   - Palliative Care </s>


Input: What is (are) mucolipidosis III gamma ?

Output: Mucolipidosis III gamma is a slowly progressive disorder that affects many parts of the body. Signs and symptoms of this condition typically appear around age 3.  Individuals with mucolipidosis III gamma grow slowly and have short stature. They also have stiff joints and dysostosis multiplex, which refers to multiple skeletal abnormalities seen on x-ray. Many affected individuals develop low bone mineral density (osteoporosis), which weakens the bones and makes them prone to fracture. Osteoporosis and progressive joint problems in people with mucolipidosis III gamma also cause pain, which becomes more severe over time.  People with mucolipidosis III gamma often have heart valve abnormalities and mild clouding of the clear covering of the eye (cornea). Their facial features become slightly thickened or "coarse" as they get older. A small percentage of people with this condition have mild intellectual disability or learning problems. Individuals with mucolipidosis III gamma generally survive into adulthood, but they may have a shortened lifespan. </s>


Input: How many people are affected by mucolipidosis III gamma ?

Output: Mucolipidosis III gamma is a rare disorder, although its exact prevalence is unknown. It is estimated to occur in about 1 in 100,000 to 400,000 individuals worldwide. </s>


Input: What are the genetic changes related to mucolipidosis III gamma ?

Output: Mutations in the GNPTG gene cause mucolipidosis III gamma. This gene provides instructions for making one part (subunit) of an enzyme called GlcNAc-1-phosphotransferase. This enzyme helps prepare certain newly made enzymes for transport to lysosomes. Lysosomes are compartments within the cell that use digestive enzymes to break down large molecules into smaller ones that can be reused by cells. GlcNAc-1-phosphotransferase is involved in the process of attaching a molecule called mannose-6-phosphate (M6P) to specific digestive enzymes. Just as luggage is tagged at the airport to direct it to the correct destination, enzymes are often "tagged" after they are made so they get to where they are needed in the cell. M6P acts as a tag that indicates a digestive enzyme should be transported to the lysosome.  Mutations in the GNPTG gene that cause mucolipidosis III gamma result in reduced activity of GlcNAc-1-phosphotransferase. These mutations disrupt the tagging of digestive enzymes with M6P, which prevents many enzymes from reaching the lysosomes. Digestive enzymes that do not receive the M6P tag end up outside the cell, where they have increased activity. The shortage of digestive enzymes within lysosomes causes large molecules to accumulate there. Conditions that cause molecules to build up inside lysosomes, including mucolipidosis III gamma, are called lysosomal storage disorders. The signs and symptoms of mucolipidosis III gamma are most likely due to the shortage of digestive enzymes inside lysosomes and the effects these enzymes have outside the cell. </s>


Input: Is mucolipidosis III gamma inherited ?

Output: This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. </s>