Chondroitin sulfate synthase 2 (CHPF)

Chondroitin sulfate synthase 2 (CHPF, also known as chondroitin polymerizing factor or CSS2) is an essential type II transmembrane glycosyltransferase responsible for the biosynthesis of chondroitin sulfate, a major glycosaminoglycan of the extracellular matrix[1][2][3][4]. CHPF acts primarily by catalyzing the transfer of glucuronic acid and N-acetylgalactosamine to growing chondroitin chains, thereby facilitating chondroitin chain extension and polymerization[1][2][3][4]. It forms complexes with other chondroitin synthases (such as CHSY1/CSS1) to regulate the length and structure of chondroitin sulfate chains, which are important for cell adhesion, morphogenesis, neural network formation, and cell division[1][3]. Aberrant expression or mutation of CHPF is associated with altered chondroitin sulfate biosynthesis and has been implicated in tumor progression and various developmental disorders[2][3][4]. Overexpression of CHPF promotes malignant cell proliferation, migration, and resistance to apoptosis, and its presence correlates with tumor aggressiveness, making it both a potential biomarker and a therapeutic target in cancer[2][3].

Other names

Chondroitin polymerizing factorChPFCSS2CHPF1Chondroitin glucuronyltransferase 2Chondroitin synthase 2Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase IIN-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase IIN-acetylgalactosaminyltransferase 2