Xylosyltransferase 1 (XYLT1)

Xylosyltransferase 1 (XYLT1) is an enzyme that catalyzes the transfer of UDP-xylose to specific serine residues in the core protein of proteoglycans, serving as the initiating step in glycosaminoglycan biosynthesis. This activity is fundamental for the formation of chondroitin sulfate and dermatan sulfate proteoglycans, which are key structural and functional components of the extracellular matrix. XYLT1 is critical for normal skeletal development, chondrocyte maturation, and extracellular matrix organization; mutations or deficiency cause several rare developmental disorders including Baratela-Scott syndrome and Desbuquois dysplasia type II. While there are no approved drugs currently targeting XYLT1 directly, nucleic acid therapeutics (DNA-enzymes) have been studied experimentally to suppress its expression, particularly to promote neuroregeneration following spinal cord injury. Its role in disease and tissue homeostasis makes it a candidate biomarker and experimental target in metabolic and developmental disorders.

Other names

Xylosyltransferase 1XYLT1XT1XT-IXylT-IPXYLT1Peptide O-xylosyltransferase 1Xylosyltransferase Iprotein xylosyltransferase 1DBQD2beta-D-xylosyltransferase 1xylosyltransferase iota

DNA-enzymes: Cleavage and degradation of XYLT1 mRNA, leads to suppressed glycosaminoglycan chain initiation and altered extracellular matrix properties