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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-5-6
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pubmed:abstractText |
Cultured arterial smooth muscle cells synthesize a cell-associated heparan sulfate proteoglycan which consists of a 92 kDa core protein with 3 to 4 heparan sulfate side chains covalently attached. Biosynthesis of the cell-associated heparan sulfate proteoglycan was compared in proliferating and in non-dividing vascular smooth muscle cells which are preincubated in the presence of [35]sulfate or a combination of [35S]methionine and [3H]glucosamine. The Mr of the core protein was identical in either growth state, but changes in the structure of the heparan sulfate side chains were observed. Non-dividing (postconfluent) arterial smooth muscle cells form longer heparan sulfate chains with a higher proportion of hydrophobic (N-acetyl) groups than proliferating (preconfluent) cells as judged from gel filtration experiments, hydrophobic interaction chromatography and heparitinase degradation. An enzyme preparation from proliferating cells catalyzes deacetylation and N-sulfation of heparan sulfate at a 5-fold higher activity than from non-dividing cells. Cell density-dependent structural differences of heparan sulfate are related to the finding that heparan sulfate isolated from non-dividing cells has a 10-fold higher antiproliferative potency than heparan sulfate from proliferating (preconfluent) cells.
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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/Chondroitin Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Heparan Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfurtransferases,
http://linkedlifedata.com/resource/pubmed/chemical/heparitin sulfotransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0171-9335
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
229-35
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2081526-Animals,
pubmed-meshheading:2081526-Aorta, Thoracic,
pubmed-meshheading:2081526-Cattle,
pubmed-meshheading:2081526-Cell Division,
pubmed-meshheading:2081526-Cell Membrane,
pubmed-meshheading:2081526-Cells, Cultured,
pubmed-meshheading:2081526-Chondroitin Sulfate Proteoglycans,
pubmed-meshheading:2081526-Chromatography, Liquid,
pubmed-meshheading:2081526-Heparan Sulfate Proteoglycans,
pubmed-meshheading:2081526-Heparitin Sulfate,
pubmed-meshheading:2081526-Muscle, Smooth, Vascular,
pubmed-meshheading:2081526-Proteins,
pubmed-meshheading:2081526-Sulfotransferases,
pubmed-meshheading:2081526-Sulfurtransferases
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pubmed:year |
1990
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pubmed:articleTitle |
Changes in heparan sulfate structure during transition from the proliferating to the non-dividing state of cultured arterial smooth muscle cells.
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pubmed:affiliation |
Institute of Arteriosclerosis Research, University of Münster, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article
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