Carbohydrate sulfotransferase 11 (CHST11) (CHST11)

Carbohydrate sulfotransferase 11 (CHST11), also known as Chondroitin 4-sulfotransferase 1 (C4ST1), is a Golgi-localized enzyme that plays a pivotal role in the biosynthesis of chondroitin sulfate (CS) glycosaminoglycans (UniProt P82979). It specifically catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-4 position of N-acetylgalactosamine residues in chondroitin chains (NCBI Gene 9423). This enzymatic activity is crucial for maintaining the structural integrity and signaling properties of the extracellular matrix (ECM) (Klüppel et al., 2005). In oncology, CHST11 mRNA is frequently overexpressed, which leads to an abundance of chondroitin 4-sulfate that facilitates tumor cell adhesion to P-selectin on vascular endothelium, thereby promoting metastasis (Cooney et al., 2011; Willis et al., 2017). Beyond its role in cancer, CHST11 is essential for normal skeletal development, and its dysregulation is associated with osteoarthritis and various chondrodysplasias (NCBI Gene 9423). Therapeutic strategies targeting CHST11 mRNA, such as small interfering RNAs (siRNAs) or antisense oligonucleotides (ASOs), are currently being investigated to downregulate the enzyme's expression and inhibit disease progression (Willis et al., 2017). These RNA-targeted approaches aim to reduce the pro-tumorigenic and pro-fibrotic effects of aberrant chondroitin sulfation patterns. Monitoring CHST11 mRNA levels and the resulting sulfation profiles serves as a potential biomarker for disease severity and therapeutic efficacy.

Other names

Chondroitin 4-sulfotransferase 1C4ST1C4ST-1HSA269537

RNA interference (RNAi) or antisense-mediated degradation of CHST11 mRNA, resulting in reduced levels of the Chondroitin 4-sulfotransferase 1 enzyme and a subsequent decrease in chondroitin 4-sulfation.