ArticleBiochemical and biophysical research communications2015
Xylosyltransferase II is the predominant isoenzyme which is responsible for the steady-state level of xylosyltransferase activity in human serum.
Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Xylosyltransferase engineering to manipulate proteoglycans in mammalian cells.Nature chemical biology · 2026Article
- Mammalian cell-based production of glycans, glycopeptides and glycomodules.Nature communications · 2024Article
- First Characterization of Human Dermal Fibroblasts Showing a Decreased Xylosyltransferase-I Expression Induced by the CRISPR/Cas9 System.International journal of molecular sciences · 2022Article
- Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region.Organic & biomolecular chemistry · 2021Article
- Recent advances on glycosyltransferases involved in the biosynthesis of the proteoglycan linkage region.Advances in carbohydrate chemistry and biochemistry · 2021Review
- Endoglycosidases for the Synthesis of Polysaccharides and Glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2016Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
In mammals, two active xylosyltransferase isoenzymes (EC 2.4.2.16) exist. Both xylosyltransferases I and II (XT-I and XT-II) catalyze the transfer of xylose from UDP-xylose to select serine residues in the proteoglycan core protein. Altered XT activity in human serum was found to correlate directly with various diseases such as osteoarthritis, systemic sclerosis, liver fibrosis, and pseudoxanthoma elasticum. To interpret the significance of the enzyme activity alteration observed in disease states it is important to know which isoenzyme is responsible for the XT activity in serum. Until now it was impossible for a specific measurement of XT-I or XT-II activity, respectively, because of the absence of a suitable enzyme substrate. This issue has now been solved and the following experimental study demonstrates for the first time, via the enzyme activity that XT-II is the predominant isoenzyme responsible for XT activity in human serum. The proof was performed using natural UDP-xylose as the xylose donor, as well as the artificial compound UDP-4-azido-4-deoxyxylose, which is a selective xylose donor for XT-I.
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