Source:http://linkedlifedata.com/resource/pubmed/id/10758005
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
15
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| pubmed:dateCreated |
2000-6-16
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| pubmed:abstractText |
Functional interactions of heparan sulfate (HS) with selected proteins depend on distinct saccharide sequences which are generated during biosynthesis of the polysaccharide. Glucosaminyl N-deacetylase/N-sulfotransferases (NDSTs) catalyze both the N-deacetylation and N-sulfation reactions that initiate the modification of the (GlcNAc-GlcA)(n) polysaccharide backbone. The N-acetyl/N-sulfate exchange is restricted to certain regions of the polysaccharide chains, and only these can be further modified by glucuronyl C5-epimerization and O-sulfation at various positions. To investigate whether NDST isoforms influenced differently the structure of HS, murine NDST-1 was overexpressed in human kidney 293 cells, and the structure of the HS produced was compared to HS from NDST-2 overexpressing cells [Cheung, W. F., Eriksson, I., Kusche-Gullberg M., Lindahl, U., and Kjellén, L. (1996) Biochemistry 35, 5250-5256]. The level of N-sulfation increased from 40% in control cells to 60% and 80%, respectively, in NDST-1 and NDST-2 transfected cells. Interestingly, the increase in N-sulfation was accompanied by an increased chain length, while no effect on IdoA content or O-sulfation was seen. The most extended N-sulfated domains were found in HS synthesized by NDST-2 transfected cells. Since both the N-deacetylase and the N-sulfotransferase activities were lower in these cells than in the NDST-1 overexpressing cells, we conclude that, in addition to the level of enzyme expression, the NDST isoform also is important in determining the N-sulfation pattern in HS.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Iduronic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/NDST2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ndst2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/heparitin sulfotransferase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
|
| pubmed:issn |
0006-2960
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
18
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| pubmed:volume |
39
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
4552-8
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10758005-Acetylation,
pubmed-meshheading:10758005-Amidohydrolases,
pubmed-meshheading:10758005-Animals,
pubmed-meshheading:10758005-Cell Line,
pubmed-meshheading:10758005-Chromatography, Gel,
pubmed-meshheading:10758005-Disaccharides,
pubmed-meshheading:10758005-Glucuronic Acid,
pubmed-meshheading:10758005-Heparitin Sulfate,
pubmed-meshheading:10758005-Humans,
pubmed-meshheading:10758005-Iduronic Acid,
pubmed-meshheading:10758005-Isoenzymes,
pubmed-meshheading:10758005-Mice,
pubmed-meshheading:10758005-Molecular Weight,
pubmed-meshheading:10758005-Polysaccharides,
pubmed-meshheading:10758005-RNA, Messenger,
pubmed-meshheading:10758005-Sulfates,
pubmed-meshheading:10758005-Sulfotransferases,
pubmed-meshheading:10758005-Transfection
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| pubmed:year |
2000
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| pubmed:articleTitle |
Overexpression of different isoforms of glucosaminyl N-deacetylase/N-sulfotransferase results in distinct heparan sulfate N-sulfation patterns.
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| pubmed:affiliation |
Department of Medical Biochemistry and Microbiology, University of Uppsala, Uppsala, Sweden.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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