Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-8-22
pubmed:abstractText
Cultured arterial smooth muscle cells synthesize two proteoheparan sulfate species. One is found associated with the cells, whereas the other is excreted into the medium. The two proteoheparan sulfates have similar hydrodynamic sizes but differ in the Mr of their core proteins. The cell-associated proteoheparan sulfate has a Mr of 92,000 while that of soluble proteoheparan sulfate is 38,000. The cell-associated and the soluble proteoheparan sulfate species differ in their ability to suppress the proliferation of smooth muscle cells. When added to the culture medium 2-5 micrograms/ml of the cell-associated and 20-25 micrograms/ml of the soluble proteoheparan sulfate species inhibit the growth of smooth muscle cells half maximally. The antiproliferative potency of both species resides in the heparan sulfate chains. Commercially available heparin has no antiproliferative effect and is not able to prevent the antiproliferative action of cellular heparan sulfate. In contrast to heparin, none of the heparan sulfate preparations has anticoagulant activity. Smooth muscle cells endocytose the soluble heparan sulfate at a rate three to four times higher than that of the cell-associated heparan sulfate. The data suggest that the cell-associated and the soluble proteoheparan sulfate species are separate and possibly genetically distinct molecules. Furthermore, the structural determinants for antiproliferative activity and the recognition sites for endocytotic uptake appear to be different.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
189
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
269-75
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:2142464-Animals, pubmed-meshheading:2142464-Aorta, Thoracic, pubmed-meshheading:2142464-Cattle, pubmed-meshheading:2142464-Cell Division, pubmed-meshheading:2142464-Cells, Cultured, pubmed-meshheading:2142464-Chondroitin Sulfate Proteoglycans, pubmed-meshheading:2142464-Chromatography, DEAE-Cellulose, pubmed-meshheading:2142464-Endocytosis, pubmed-meshheading:2142464-Glucosamine, pubmed-meshheading:2142464-Glycosaminoglycans, pubmed-meshheading:2142464-Heparan Sulfate Proteoglycans, pubmed-meshheading:2142464-Heparitin Sulfate, pubmed-meshheading:2142464-Methionine, pubmed-meshheading:2142464-Molecular Weight, pubmed-meshheading:2142464-Muscle, Smooth, Vascular, pubmed-meshheading:2142464-Proteoglycans, pubmed-meshheading:2142464-Radioisotope Dilution Technique, pubmed-meshheading:2142464-Sulfur Radioisotopes, pubmed-meshheading:2142464-Tritium
pubmed:year
1990
pubmed:articleTitle
Bovine arterial smooth muscle cells synthesize two functionally different proteoheparan sulfate species.
pubmed:affiliation
Institute for Arteriosclerosis Research, University of Münster, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't