It is thought that HG is due to a combination of factors which may vary between women and include genetics. Women with family members who had HG are more likely to develop the disease.One factor is an adverse reaction to the hormonal changes of pregnancy, in particular, elevated levels of beta human chorionic gonadotropin (β-hCG). This theory would also explain why hyperemesis gravidarum is most frequently encountered in the first trimester (often around 8–12 weeks of gestation), as β-hCG levels are highest at that time and decline afterward. Another postulated cause of HG is an increase in maternal levels of estrogens (decreasing intestinal motility and gastric emptying leading to nausea/vomiting).More recently, another cause of HG was discovered: "Evidence suggests abnormal levels of the hormone GDF15 are associated with HG. The validation of a second risk variant, rs1054221, provides further support for GDF15s role in the etiology of HG. Additionally, maternal genes appear to play a more significant role than paternal DNA in contributing to the severity of NVP." Pathophysiology
Although the pathophysiology of HG is poorly understood, the most commonly accepted theory suggests that levels of β-hCG are associated with it. Leptin, a hormone that inhibits hunger, may also play a role.Possible pathophysiological processes involved are summarized in the following table:

Diagnosis
Hyperemesis gravidarum is considered a diagnosis of exclusion. HG can be associated with serious problems in the mother or baby, such as Wernickes encephalopathy, coagulopathy and peripheral neuropathy.Women experiencing hyperemesis gravidarum often are dehydrated and lose weight despite efforts to eat.
Role in metabolism
Reduced sulfate availability due to impaired activity of ARSB has been linked to increased aerobic glycolysis, as shown by an increase in NADH and NADPH, reduced oxygen consumption, increased extracellular acidification and serum lactate, and a decline in mitochondrial membrane potential in ARSB-silenced cells and ARSB-null mouse tissues. Extra-lysosomal localization
Although primarily a lysosomal enzyme, ARSB was also found to localize at the cell membrane of hepatocytes, sinusoidal endothelial cells, and Kupffer cells in the liver, as well as in the apical membranes of normal and malignant colonic and prostatic epithelial cells, by immunohistochemistry and immunofluorescence studies. Membrane immunostaining in the colon and prostate was lower in malignant than in normal tissue and also was lower in higher grade malignancies. ARSB activity assay in the membrane and cytosol fractions of cultured bronchial epithelial cells showed that the activity was several-fold greater in the membrane fraction. See also
Aryl
Sulfatase

References
Further reading
Brunelli MJ, Atallah ÁN, da Silva EM (September 2021). "Enzyme replacement therapy with galsulfase for mucopolysaccharidosis type VI". Cochrane Database Syst Rev. 2021 (9): CD009806. doi:10.1002/14651858.CD009806.pub3. PMC 8447860. PMID 34533215. "Galsulfase (Naglazyme)". Common Drug Review. Ottawa (ON): Canadian Agency for Drugs and Technologies in Health (CADTH). November 2016. PMID 28121110. Ferreira CR, Gahl WA (May 2017). "Lysosomal storage diseases". Transl Sci Rare Dis. 2 (1–2): 1–71. doi:10.3233/TRD-160005. PMC 5685203. PMID 29152458. External links
Medical Dictionary, Arylsulfatase B function. Protein Data Base (PDB), Arylsulfatase structure. Genetics Home Reference, Arylsulfatase B function. Overview of all the structural information available in the PDB for UniProt: P15848 (Arylsulfatase B) at the PDBe-KB. "Galsulfase".