Source:http://linkedlifedata.com/resource/pubmed/id/19341245
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2009-6-8
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pubmed:abstractText |
Platelets are small blood cells vital for hemostasis. Following vascular damage, platelets adhere to collagens and activate, forming a thrombus that plugs the wound and prevents blood loss. Stimulation of the platelet collagen receptor glycoprotein VI (GPVI) allows recruitment of proteins to receptor-proximal signaling complexes on the inner-leaflet of the plasma membrane. These proteins are often present at low concentrations; therefore, signaling-complex characterization using mass spectrometry is limited due to high sample complexity. We describe a method that facilitates detection of signaling proteins concentrated on membranes. Peripheral membrane proteins (reversibly associated with membranes) were eluted from human platelets with alkaline sodium carbonate. Liquid-phase isoelectric focusing and gel electrophoresis were used to identify proteins that changed in levels on membranes from GPVI-stimulated platelets. Immunoblot analysis verified protein recruitment to platelet membranes and subsequent protein phosphorylation was preserved. Hsp47, a collagen binding protein, was among the proteins identified and found to be exposed on the surface of GPVI-activated platelets. Inhibition of Hsp47 abolished platelet aggregation in response to collagen, while only partially reducing aggregation in response to other platelet agonists. We propose that Hsp47 may therefore play a role in hemostasis and thrombosis.
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pubmed:grant | |
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/HSP47 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/SERPINH1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/platelet membrane glycoprotein VI
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1535-3893
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2903-14
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:19341245-Blood Platelets,
pubmed-meshheading:19341245-Chromatography, Liquid,
pubmed-meshheading:19341245-Collagen,
pubmed-meshheading:19341245-HSP47 Heat-Shock Proteins,
pubmed-meshheading:19341245-Humans,
pubmed-meshheading:19341245-Membrane Proteins,
pubmed-meshheading:19341245-Phosphorylation,
pubmed-meshheading:19341245-Platelet Activation,
pubmed-meshheading:19341245-Platelet Aggregation,
pubmed-meshheading:19341245-Platelet Membrane Glycoproteins,
pubmed-meshheading:19341245-Proteomics,
pubmed-meshheading:19341245-Signal Transduction,
pubmed-meshheading:19341245-Tandem Mass Spectrometry,
pubmed-meshheading:19341245-p38 Mitogen-Activated Protein Kinases
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pubmed:year |
2009
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pubmed:articleTitle |
A functional proteomic method for the enrichment of peripheral membrane proteins reveals the collagen binding protein Hsp47 is exposed on the surface of activated human platelets.
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pubmed:affiliation |
Institute for Cardiovascular and Metabolic Research, School of Biological Sciences, Hopkins Building, The University of Reading, Whiteknights, Reading, United Kingdom RG6 6UB.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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