Chondroitin polymerizing factor 2 (CHPF2)

Chondroitin polymerizing factor 2 (CHPF2) is a membrane-bound enzyme classified as a glycosyltransferase that contributes to the biosynthesis of chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycan chains[3][1]. It has dual enzymatic activities: as a β1,3-glucuronyltransferase and β1,4-N-acetylgalactosaminyltransferase, enabling it to elongate the polymer backbone of chondroitin sulfate through alternating additions of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) onto proteoglycan core proteins[1][3]. CHPF2 functions in concert with other chondroitin synthase family members (such as CHSY3) to catalyze the assembly and extension of CS chains. CHPF2's activity is essential for proper formation and structural diversity of CS chains, which are critical in cell signaling, cell proliferation, tissue morphogenesis, and interactions with growth factors and cytokines[1]. Mutations or deficiencies in CHPF2 are associated with skeletal development disorders and some forms of Ehlers-Danlos syndrome[3]. CHPF2 is considered a potential therapeutic target due to its involvement in extracellular matrix formation and disease pathogenesis, although no specific drugs currently target it directly[3][1].

Other names

Chondroitin sulfate glucuronyltransferaseChondroitin synthase 3 (CHSY3)CSGLCATKIAA1402UNQ299/PRO339ChPF-2ChSy-3CSGlcA-TChondroitin glucuronyltransferaseN-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferaseChondroitin synthase-3CSGLCA-TCSGlcAT