Just as the term "articulation" can mean either "speech" or "joint movement", so is the combining form of arthr- the same in the terms "dysarthria", "dysarthrosis", and "arthropathy"; the term "dysarthria" is conventionally reserved for the speech problem and is not used to refer to arthropathy, whereas "dysarthrosis" has both senses but usually refers to arthropathy. Causes
There are many potential causes of dysarthria. They include toxic, metabolic, degenerative diseases, traumatic brain injury, or thrombotic or embolic stroke.Degenerative diseases include parkinsonism, amyotrophic lateral sclerosis (ALS), multiple sclerosis, Huntingtons disease, Niemann-Pick disease, and Friedreichs ataxia. Toxic and metabolic conditions include: Wilsons disease, hypoxic encephalopathy such as in drowning, and central pontine myelinolysis.These result in lesions to key areas of the brain involved in planning, executing, or regulating motor operations in skeletal muscles (i.e. muscles of the limbs), including muscles of the head and neck (dysfunction of which characterises dysarthria). These can result in dysfunction, or failure of: the motor or somatosensory cortex of the brain, corticobulbar pathways, the cerebellum, basal nuclei (consisting of the putamen, globus pallidus, caudate nucleus, substantia nigra etc. ), brainstem (from which the cranial nerves originate), or the neuromuscular junction (in diseases such as myasthenia gravis) which block the nervous systems ability to activate motor units and effect correct range and strength of movements.Causes:
Brain tumor
Cerebral palsy
Guillain–Barré syndrome
Hypothermia
Idiopathic intracranial hypertension (formerly known as pseudotumor cerebri)
Lyme disease
Stroke
Tay–Sachs disease, and late-onset Tay–Sachs disease (LOTS)
Transient ischemic attack, a mini stroke

Diagnosis
Classification
Dysarthrias are classified in multiple ways based on the presentation of symptoms.
The steady-state turnover number, kcat, of ODC was calculated to be 0.5 s−1 at 4 °C. From this characterization, the rate-limiting step was determined to be the release of the product putrescine from ODCs reaction with ornithine. In studying the hypothetical reaction mechanism for eflornithine, information collected from radioactive peptide and eflornithine mapping, high pressure liquid chromatography, and gas phase peptide sequencing suggested that Lys-69 and Cys-360 are covalently bound to eflornithine in T. brucei ODCs active site. Utilizing fast-atom bombardment mass spectrometry (FAB-MS), the structural conformation of eflornithine following its interaction with ODC was determined to be (S)-((2-(1-pyrroline-methyl) cysteine, a cyclic imine adduct. Presence of this particular product was supported by the possibility to further reduce the end product to (S)-((2-pyrrole) methyl) cysteine in the presence of NaBH4 and oxidize the end product to (S)-((2-pyrrolidine) methyl) cysteine (Figure 2). Active site
Eflornithines suicide inhibition of ODC physically blocks the natural substrate ornithine from accessing the active site of the enzyme (Figure 3). There are two distinct active sites formed by the homodimerization of ornithine decarboxylase. The size of the opening to the active site is approximately 13.6 Å. When these openings to the active site are blocked, there are no other ways through which ornithine can enter the active site. During the intermediate stage of eflornithine with PLP, its position near Cys-360 allows an interaction to occur.