Carbohydrate sulfotransferase 11 (CHST11)

Carbohydrate sulfotransferase 11 (CHST11) is a Golgi-localized enzyme of the sulfotransferase 2 family that catalyzes sulfate transfer to the 4-position of the N-acetylgalactosamine (GalNAc) residue in chondroitin, producing chondroitin 4-sulfate, a key structural glycosaminoglycan in cartilage and extracellular matrices. CHST11 is important in cartilage development, extracellular matrix composition, and regulation of cell signaling. Pathologically, aberrant or elevated CHST11 expression has been implicated in tumor progression and poor prognosis in several cancers—including hepatocellular carcinoma, glioblastoma, renal cell carcinoma, and breast cancer—by promoting tumor cell proliferation, metastasis, immune evasion, and modification of the tumor microenvironment. It is considered a potential biomarker and emerging therapeutic target for cancer, though clinically approved CHST11 inhibitors have yet to be developed. Loss-of-function mutations in CHST11 can cause skeletal abnormalities such as osteochondrodysplasia, brachydactyly, and malformed digits.

Other names

Chondroitin 4-O-sulfotransferase 1Chondroitin 4-sulfotransferase 1C4ST-1C4ST1C4S-1OCBMDIgH/CHST11 fusionHSA269537

C4Sp peptide inhibits CHST11-mediated chondroitin 4-sulfate functions, reducing tumor cell migration and invasion. Blockade may influence tumor immune microenvironment by decreasing Treg infiltration and enhancing antitumor immunity.