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Papers In Press, published online ahead of print December 22, 2006
J. Biol. Chem, 10.1074/jbc.M611048200
Submitted on November 30, 2006
Revised on December 18, 2006
Accepted on December 22, 2006

Biosynthesis of chondroitin and heparan sulfate in CHO cells depends on Xylosyltransferase II

Karen Cuellar, Hoa Chuong, Sherry M. Hubbell, and Myron E. Hinsdale

Oklahoma Medical Research Foundation, Oklahoma City, OK 73104

Corresponding Author: Myron-Hinsdale{at}omrf.ouhsc.edu

Xylosyltransferase (XylT) catalyzes the initial enzymatic reaction in the glycosaminoglycan assembly pathway for proteoglycan biosynthesis. Its activity is thought to be rate limiting. Two xylosyltransferases have been found using genomic analyses and one of these, XylT1, has been shown to have xylosyltransferase activity. On the other hand, the less studied XylT2 in recombinant form lacks xylosyltransferase activity and has no known function. Wild-type Chinese hamster ovary (CHO) cells express abundant Xylt2 mRNA levels and lack detectable Xylt1 mRNA levels. Analysis of a previously described CHO cell xylosyltransferase mutant (psgA-745) shows that it harbors a Xylt2 nonsense mutation and fails to assemble glycosaminoglycans onto recombinant biglycan. Transfection of this cell line with a murine Xylt2 minigene results in the production of recombinant chondroitin sulfate modified biglycan core protein and restoration of fibroblast growth factor binding to cell surface associated heparan sulfate. Expression analyses on 10 different human transformed cell lines detects exclusive XYLT2 expression in 2 and co-expression of XYLT1 and XYLT2 in the others, but at disparate ratios where XYLT2 expression is greater than XYLT1 in most cell lines. These results indicate that XylT2 has a significant role in proteoglycan biosynthesis and that cell type may control which family member is utilized.


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