Chondroitin sulfate N-acetylgalactosaminyltransferase 2 (CSGALNACT2)

Chondroitin sulfate N-acetylgalactosaminyltransferase 2 (CSGALNACT2) is a type II Golgi membrane enzyme that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to glucuronic acid residues at the non-reducing end of chondroitin sulfate (CS) chains, primarily mediating the elongation step of CS biosynthesis[1][2][3]. Unlike its homolog CSGALNACT1, which initiates CS chain synthesis, CSGALNACT2 extends glycosaminoglycan chains, contributing to extracellular matrix structure and function[1][2][3]. It is highly expressed in tissues such as the small intestine, leukocytes, and spleen, and has a role in physiological and pathological extracellular matrix remodeling, including in cardiovascular diseases and certain inherited connective tissue disorders[1][2][3]. Experimental evidence also suggests that CSGALNACT2 supports the replication of some viruses, such as infectious bursal disease virus, by interacting with viral proteins within the Golgi apparatus[7].

Other names

GALNACT-2ChGn-2PRO0082CHGN2GALNACT2Beta4GalNAcT-2GalNAcT-2MGC40204CGAT2chondroitin beta-1,4-N-acetylgalactosaminyltransferase 2chondroitin beta1,4 N-acetylgalactosaminyltransferase 2glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase 2