Source:http://linkedlifedata.com/resource/pubmed/id/20539917
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2010-8-4
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pubmed:abstractText |
The majority of the antiphospholipid antibodies, present in patients with antiphospholipid syndrome, are directed against conformational epitopes in beta2-glycoprotein I. beta2-glycoprotein I is an anionic phospholipid-binding 50-kDa plasma protein whose physiological role is not clear. Here we investigate the role of beta2-glycoprotein I in the phagocytosis of phosphatidylserine-expressing platelet microvesicles and the effect of autoantibodies to beta2-glycoprotein I on this process. We labelled the glycans of beta2-glycoprotein I with BODIPY (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene)-hydrazide without affecting its phospholipid binding capacity. BODIPY-beta2-glycoprotein I bound to platelet microvesicles in a concentration-dependent manner and promoted the phagocytosis of platelet microvesicles by THP-1 derived macrophages in vitro at physiological plasma concentrations with a half maximal effect at approximately 10 microg/ml. beta2-glycoprotein I-stimulated phagocytosis was inhibited by annexin A5 and the phosphatidylserine-binding C1C2 fragment of lactadherin. Furthermore, immunoaffinity purified beta2-glycoprotein I-dependent antiphospholipid antibodies from five patients with antiphospholipid syndrome inhibited the phagocytosis in a concentration-dependent manner. These studies suggest that the binding of beta2-glycoprotein I to phosphatidylserine-expressing procoagulant platelet microvesicles may promote their clearance by phagocytosis and autoantibodies to beta2-glycoprotein I may inhibit this process to induce a procoagulant state.
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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/4,4-difluoro-4-bora-3a,4a-diaza-s-in...,
http://linkedlifedata.com/resource/pubmed/chemical/Annexin A5,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Autoantibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Boron Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/MFGE8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Milk Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Glycoprotein I
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0340-6245
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
335-41
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pubmed:dateRevised |
2011-5-23
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pubmed:meshHeading |
pubmed-meshheading:20539917-Annexin A5,
pubmed-meshheading:20539917-Antigens, Surface,
pubmed-meshheading:20539917-Antiphospholipid Syndrome,
pubmed-meshheading:20539917-Autoantibodies,
pubmed-meshheading:20539917-Blood Coagulation,
pubmed-meshheading:20539917-Blood Platelets,
pubmed-meshheading:20539917-Boron Compounds,
pubmed-meshheading:20539917-Cell Line,
pubmed-meshheading:20539917-Cytoplasmic Vesicles,
pubmed-meshheading:20539917-Fluorescent Dyes,
pubmed-meshheading:20539917-Humans,
pubmed-meshheading:20539917-Macrophages,
pubmed-meshheading:20539917-Milk Proteins,
pubmed-meshheading:20539917-Peptide Fragments,
pubmed-meshheading:20539917-Phagocytosis,
pubmed-meshheading:20539917-Phosphatidylserines,
pubmed-meshheading:20539917-beta 2-Glycoprotein I
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pubmed:year |
2010
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pubmed:articleTitle |
Phagocytosis of platelet microvesicles and beta2- glycoprotein I.
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pubmed:affiliation |
Department of Pathology and Medicine, Michael E DeBakey Veterans Affairs Medical Center, Baylor College of Medicine, Houston, Texas 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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