Source:http://linkedlifedata.com/resource/pubmed/id/21602602
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2011-5-23
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pubmed:abstractText |
Herein, we investigated the possible mechanisms by which recombinant modified CRP(m(r)CRP) modulates blood platelet function. Modified CRP could activate blood platelets and stimulate their adhesion and aggregation in the absence of any other physiological stimuli. Preincubation of isolated blood platelets with m(r)CRP at a concentration as low as 2 ?g/ml resulted in significant platelet degranulation (fraction of CD62-positive platelets increased 2-fold, p < 0.0002), and at concentrations of 20 ?g/ml and 100 ?g/ml, increased exposure of the platelet procoagulant surface was observed (expression of annexin V-positive platelets increased to 5.7 ± 1.0% and 10.4 ± 2.2%, respectively, p < 0.03, vs. 2.9 ± 0.2% in control). Furthermore, m(r)CRP (100 ?g/ml) strongly augmented spontaneous and ADP-induced fibrinogen binding to platelets (p < 0.05), platelet adhesion to fibrinogen and platelet aggregation. Using the Biacore™ surface plasmon resonance technique and glycoprotein Ib? (GPIb?) immobilized on the sensor surface, we demonstrated direct binding between platelet GPIb? and m(r)CRP. Binding of m(r)CRP to GPIb? and C1q was also observed by ELISA, irrespective of the immobilized ligand. These outcomes strongly support a role of the GPIb-IX-V complex in the interactions of m(r)CRP with blood platelets.
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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/Annexin A5,
http://linkedlifedata.com/resource/pubmed/chemical/C-Reactive Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIb-IX...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1734-1140
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
464-75
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pubmed:meshHeading |
pubmed-meshheading:21602602-Adult,
pubmed-meshheading:21602602-Annexin A5,
pubmed-meshheading:21602602-Blood Platelets,
pubmed-meshheading:21602602-C-Reactive Protein,
pubmed-meshheading:21602602-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:21602602-Female,
pubmed-meshheading:21602602-Fibrinogen,
pubmed-meshheading:21602602-Humans,
pubmed-meshheading:21602602-Male,
pubmed-meshheading:21602602-Platelet Adhesiveness,
pubmed-meshheading:21602602-Platelet Aggregation,
pubmed-meshheading:21602602-Platelet Glycoprotein GPIb-IX Complex,
pubmed-meshheading:21602602-Protein Binding,
pubmed-meshheading:21602602-Recombinant Proteins,
pubmed-meshheading:21602602-Surface Plasmon Resonance,
pubmed-meshheading:21602602-Young Adult
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pubmed:articleTitle |
Modified C-reactive protein interacts with platelet glycoprotein Ib?.
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pubmed:affiliation |
Department of Haemostasis and Haemostatic Disorders, Medical University of Lodz, ?eromskiego 113, PL 90-549 ?ód?, Poland. mboncler@csk.umed.lodz.pl
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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