CHST8 encodes a Golgi-localized sulfotransferase that catalyzes sulfation of N-acetylgalactosamine (GalNAc) residues at the 4-position of both N-linked and O-linked glycans 1. The enzyme is essential for biosynthesis of glycoprotein hormones, particularly lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. CHST8 specifically modifies terminal β1,4-linked GalNAc on glycoproteins rather than glycosaminoglycans 1. CHST8 mutations have been associated with autosomal recessive peeling skin syndrome (PSS) type A. A homozygous missense mutation (c.229C>T, R77W) was identified in consanguineous families with non-inflammatory PSS, with evidence suggesting loss-of-function through accelerated protein degradation 2. However, subsequent functional analysis demonstrated that the R77W variant exhibits normal catalytic activity and processing, indicating it likely represents a benign polymorphism rather than a disease-causing mutation 1. Beyond dermatological associations, CHST8 has been identified as a candidate gene in obesity-related epigenetic studies, with differential DNA methylation signatures observed in obese versus non-obese individuals and changes following bariatric surgery 3. A Drosophila functional screen identified CHST8 as a potential functional target gene for human BMI GWAS loci 4. Additionally, CHST8 is expressed in von Economo neurons of human anterior cingulate cortex, suggesting roles in social-emotional brain function 5.