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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1988-10-12
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pubmed:abstractText |
The effect of substances that affect platelet cytoskeleton on the interaction of gel-filtered platelets with surfaces coated with human monomeric type I, IV, and V collagen was studied. The sulfhydryl group oxidizing agent azodicarboxylic acid-bis-dimethylamide (diamide) which causes disulfide-linked polymer formation of certain cytoskeletal proteins, the actin-polymerization inhibitor, cytochalasin B, and 2-mercaptopropionylglycine (2-MPG), a cell-permeable SH-reagent, completely abolish adhesion-induced platelet spreading and mural platelet aggregate formation on collagen-coated surfaces. Extrusion of pseudopods was inhibited by cytochalasin B and 2-MPG as well as by diamide, but only the latter caused spherulation of platelets, whereas cytochalasin B and 2-MPG left the discoid shape of resting platelets intact. These effects are dose-dependent and are not accounted for by a chemical modification of the collagenous substrates by the cytoskeletal perturbing substances. The present data indicate that (i) cytoskeletal rearrangements are essential in adhesion-induced platelet spreading and aggregate formation on surfaces coated with collagen, but not in supporting the initial attachment of native platelets to the substrate; (ii) both, polymerization and depolymerization of actin filaments affect platelet activation; (iii) the sulfhydryl-disulfide status of the platelet seems to be a possible target for anti-platelet drugs, since chemical modification of platelets by the GSH-GSSG-active substances, diamide and 2-MPG, leads to a reversible inhibition of adhesion-induced platelet activation.
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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/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinolytic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/Tiopronin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0049-3848
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
|
pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
627-36
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:3413723-Chromatography, Gel,
pubmed-meshheading:3413723-Collagen,
pubmed-meshheading:3413723-Cytochalasin B,
pubmed-meshheading:3413723-Cytoskeletal Proteins,
pubmed-meshheading:3413723-Fibrinolytic Agents,
pubmed-meshheading:3413723-Humans,
pubmed-meshheading:3413723-Male,
pubmed-meshheading:3413723-Platelet Adhesiveness,
pubmed-meshheading:3413723-Platelet Aggregation Inhibitors,
pubmed-meshheading:3413723-Polymers,
pubmed-meshheading:3413723-Tiopronin
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pubmed:year |
1988
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pubmed:articleTitle |
Substances that polymerize or depolymerize cytoskeletal proteins affect platelet spreading and thrombus-formation on surfaces coated with human collagen isotypes I, IV, and V.
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pubmed:affiliation |
Central Institute for Cardiovascular Research, Academy of Sciences, Berlin-Buch, GDR.
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pubmed:publicationType |
Journal Article
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