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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1993-3-11
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pubmed:abstractText |
Heparan sulfate isolated from mammalian arterial tissue inhibits the growth of homologous arterial smooth muscle cells when added to subconfluent cell cultures at a concentration of 50 to 100 micrograms/ml culture medium. Disintegration of the heparan sulfate molecule by hydrazinolysis that deacetylates N-acetylglucosaminyl residues and by subsequent treatment with nitrous acid at pH 3.9 results in the formation of a mixture of oligosaccharides which was further resolved into sulfate-enriched oligosaccharides with antiproliferative activity in an in vitro bioassay system. A decasaccharide and dodeca/tetradecasaccharide fraction had a significantly higher antiproliferative effect on arterial smooth muscle cells than the native heparan sulfate molecule. The antiproliferative oligosaccharides have a sulfate content of 0.9 to 1.2 sulfate groups/disaccharide unit and consist of 60 to 70% monosulfated, disulfated, and trisulfated disaccharide units. Up to 32% of the sulfate groups were in 2-position of the uronic acid. In contrast, nitrous acid degradation of heparan sulfate at pH 1.5, which cleaves glycosidic linkages of N-sulfoglucosaminyl residues, results in the formation of sulfate-poor or sulfate-free oligosaccharides without antiproliferative potency. The results indicate that (a) heparan sulfate has a heterogeneous molecular organization where sulfate-rich domains are separated by sulfate-poor sequences and that (b) the antiproliferative activity of heparan sulfate resides in domains enriched with 2-O-sulfated uronic acid residues.
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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/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrous Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sepharose,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/Uronic Acids
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0171-9335
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
322-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1493797-Animals,
pubmed-meshheading:1493797-Aorta,
pubmed-meshheading:1493797-Cattle,
pubmed-meshheading:1493797-Cell Division,
pubmed-meshheading:1493797-Cells, Cultured,
pubmed-meshheading:1493797-Disaccharides,
pubmed-meshheading:1493797-Heparitin Sulfate,
pubmed-meshheading:1493797-Humans,
pubmed-meshheading:1493797-Muscle, Smooth, Vascular,
pubmed-meshheading:1493797-Nitrous Acid,
pubmed-meshheading:1493797-Oligosaccharides,
pubmed-meshheading:1493797-Proteins,
pubmed-meshheading:1493797-Sepharose,
pubmed-meshheading:1493797-Sulfates,
pubmed-meshheading:1493797-Uronic Acids
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pubmed:year |
1992
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pubmed:articleTitle |
Molecular organization and antiproliferative domains of arterial tissue heparan sulfate.
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pubmed:affiliation |
Institut für Arterioskleroseforschung an der Universität Münster, Deutschland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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