Expression of the mouse mastocytoma glucosaminyl N-deacetylase/ N-sulfotransferase in human kidney 293 cells results in increased N-sulfation of heparan sulfate

Biochemistry
W F CheungL Kjellén

Abstract

The biosynthesis of heparin and heparan sulfate involves a series of polymer-modification reactions that is initiated by N-deacetylation and subsequent N-sulfation of N-acetylglucosamine residues. These reactions are catalysed by a combined N-deacetylase/N-sulfotransferase. Proteins expressing both activities have previously been purified from mouse mastocytoma, which generates heparin, and from rat liver, which produces heparan sulfate. In the present study, the mouse mastocytoma enzyme has been expressed in the human kidney cell line, 293, to investigate whether it could promote modification of the endogenous heparan sulfate precursor polysaccharide into a heparan-like molecule. The N-deacetylase activity of the stably transfected cell clones as approximately 8-fold higher, on a cell-protein basis, than that of control cells, while the N-sulfotransferase activity was increased approximately 2.5 fold. The amounts of glycosaminoglycans synthesized were the same in control and transfected cells, measured as incorporation of [3H]-glucosamine, whereas 35S-labeled glycosaminoglycans were approximately 50% increased in transfected cells, with an increased relative content of heparin sulfate. Structural analysis demonstrated the the ...Continue Reading

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Citations

Apr 1, 2000·Biochimica Et Biophysica Acta·O Habuchi
Jun 5, 2002·Annual Review of Biochemistry·Jeffrey D Esko, Scott B Selleck
Feb 22, 2012·Arteriosclerosis, Thrombosis, and Vascular Biology·Sébastien Le JanJohan Kreuger
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May 27, 2004·The Journal of Biological Chemistry·Shuhei YamadaMarion Kusche-Gullberg
Jul 9, 2016·The Journal of Biological Chemistry·Audrey DelignyLena Kjellén

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