Regulation of biosynthesis of the basic fibroblast growth factor binding domains of heparan sulfate by heparan sulfate-N-deacetylase/N-sulfotransferase expression
Heparan sulfate-N-deacetylase/N-sulfotransferase catalyzes both the N-deacetylation and N-sulfation reactions that initiate the modification of the oligosaccharide backbone of heparan sulfate (HS). The glycosaminoglycan polymer appears to modulate the activity of growth factors by mediating their in...
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Published in | The Journal of biological chemistry Vol. 268; no. 27; pp. 20091 - 20095 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
25.09.1993
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Abstract | Heparan sulfate-N-deacetylase/N-sulfotransferase catalyzes both the N-deacetylation and N-sulfation reactions that initiate
the modification of the oligosaccharide backbone of heparan sulfate (HS). The glycosaminoglycan polymer appears to modulate
the activity of growth factors by mediating their initial binding. To understand how the biosynthesis of these binding sites
is regulated, a rat liver-derived cDNA encoding the above activities was overexpressed in a COS cell mutant (CM-15) that has
reduced levels of the enzyme and binds poorly to immobilized basic fibroblast growth factor (bFGF). This resulted in increased
synthesis of sulfated blocks of decasaccharide size or longer. These blocks exhibited high affinity binding to bFGF and contained
a high content of 2-O-sulfated iduronate and at least five consecutive N-sulfated disaccharides. An increase in the synthesis
of these high affinity blocks was not seen in transfected wild-type COS cells even though they showed a 4-fold increase of
both enzyme activities, suggesting that once sufficient levels of highly sulfated blocks of saccharides with high affinity
for bFGF are attained, no further synthesis of these domains occurs. |
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AbstractList | Heparan sulfate-N-deacetylase/N-sulfotransferase catalyzes both the N-deacetylation and N-sulfation reactions that initiate the modification of the oligosaccharide backbone of heparan sulfate (HS). The glycosaminoglycan polymer appears to modulate the activity of growth factors by mediating their initial binding. To understand how the biosynthesis of these binding sites is regulated, a rat liver-derived cDNA encoding the above activities was overexpressed in a COS cell mutant (CM-15) that has reduced levels of the enzyme and binds poorly to immobilized basic fibroblast growth factor (bFGF). This resulted in increased synthesis of sulfated blocks of decasaccharide size or longer. These blocks exhibited high affinity binding to bFGF and contained a high content of 2-O-sulfated iduronate and at least five consecutive N-sulfated disaccharides. An increase in the synthesis of these high affinity blocks was not seen in transfected wild-type COS cells even though they showed a 4-fold increase of both enzyme activities, suggesting that once sufficient levels of highly sulfated blocks of saccharides with high affinity for bFGF are attained, no further synthesis of these domains occurs. Heparan sulfate-N-deacetylase/N-sulfotransferase catalyzes both the N-deacetylation and N-sulfation reactions that initiate the modification of the oligosaccharide backbone of heparan sulfate (HS). The glycosaminoglycan polymer appears to modulate the activity of growth factors by mediating their initial binding. To understand how the biosynthesis of these binding sites is regulated, a rat liver-derived cDNA encoding the above activities was overexpressed in a COS cell mutant (CM-15) that has reduced levels of the enzyme and binds poorly to immobilized basic fibroblast growth factor (bFGF). This resulted in increased synthesis of sulfated blocks of decasaccharide size or longer. These blocks exhibited high affinity binding to bFGF and contained a high content of 2-O-sulfated iduronate and at least five consecutive N-sulfated disaccharides. An increase in the synthesis of these high affinity blocks was not seen in transfected wild-type COS cells even though they showed a 4-fold increase of both enzyme activities, suggesting that once sufficient levels of highly sulfated blocks of saccharides with high affinity for bFGF are attained, no further synthesis of these domains occurs. |
Author | M Ishihara Z Wei S J Swiedler A Orellana Z Yang C B Hirschberg Y Guo |
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Keywords | Ligand binding Vertebrata Mammalia Rat Rodentia Glycosaminoglycan Heparitin sulfate Carbohydrate Biosynthesis Growth factor |
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Snippet | Heparan sulfate-N-deacetylase/N-sulfotransferase catalyzes both the N-deacetylation and N-sulfation reactions that initiate
the modification of the... Heparan sulfate-N-deacetylase/N-sulfotransferase catalyzes both the N-deacetylation and N-sulfation reactions that initiate the modification of the... |
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SubjectTerms | Amidohydrolases - biosynthesis Amidohydrolases - metabolism Analytical, structural and metabolic biochemistry Animals Binding Sites Biological and medical sciences Carbohydrate Sequence Carbohydrates Cell Line Chromatography, Affinity Chromatography, Gel Fibroblast Growth Factor 2 - metabolism Fundamental and applied biological sciences. Psychology Gene Expression Heparan Sulfate Proteoglycans Heparitin Sulfate - biosynthesis Heparitin Sulfate - isolation & purification Heparitin Sulfate - metabolism Miscellaneous Molecular Sequence Data Oligosaccharides - biosynthesis Oligosaccharides - isolation & purification Other biological molecules Proteoglycans - biosynthesis Proteoglycans - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sulfates - metabolism Sulfotransferases - biosynthesis Sulfotransferases - metabolism Sulfur Radioisotopes Transfection |
Title | Regulation of biosynthesis of the basic fibroblast growth factor binding domains of heparan sulfate by heparan sulfate-N-deacetylase/N-sulfotransferase expression |
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