Source:http://linkedlifedata.com/resource/pubmed/id/12540953
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2003-1-23
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pubmed:abstractText |
Previous studies showed that alpha-fibrin monomer (lacking both A-fibrinopeptides, FPA) is normally cleared from the circulation before it assembles into a clot. Recent studies indicate that substantial quantities of an intermediate, alpha-profibrin lacking only one of the two FPA are produced in the course of conversion of human fibrinogen to fibrin. Since clearance of the alpha-fibrin monomer is saturable and receptor mediated, the extent to which alpha-profibrin or other fibrin(ogen) derivatives might compete for monomer uptake was deemed important. We compared plasma decay of injected human alpha-fibrin, fibrinogen, and alpha-profibrin in rabbits using rabbit anti-human fibrinogen for assays. The circulatory half-life of human alpha-fibrin monomer was short (t(1/2) = 2.3 h) and followed a simple exponential decay curve, as anticipated from clearance of rabbit alpha-fibrin. It was absorbed as fast as it permeated the extravascular space with no redistribution. Human fibrinogen had a long half-life (t(1/2) = 39.5 h), calculated from the double exponential plasma decay curves (redistribution + catabolism) observed over 28 h. The alpha-profibrin had an intermediary half-life (t(1/2) = 11 h) determined from double exponential decay curves. Since redistribution accompanied the slow clearance of alpha-profibrin, its binding by the fibrin receptor(s) must be weak, probably too weak to compete with the clearance of alpha-fibrin monomer. The initial production of alpha-fibrin monomer is only partially dependent on prior formation of alpha-profibrin, as recently shown. Thus, it is the slow clearance and the weak competition from alpha-profibrin that underlie the occurrence of substantial levels of alpha-profibrin unaccompanied by detectable levels of alpha-fibrin monomer in many subjects with vascular disease.
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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/Fibrin,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrin Fibrinogen Degradation...,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/fibrin receptor,
http://linkedlifedata.com/resource/pubmed/chemical/fibrinmonomer
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0340-6245
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
48-52
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12540953-Animals,
pubmed-meshheading:12540953-Binding, Competitive,
pubmed-meshheading:12540953-Blood Circulation,
pubmed-meshheading:12540953-Fibrin,
pubmed-meshheading:12540953-Fibrin Fibrinogen Degradation Products,
pubmed-meshheading:12540953-Fibrinogen,
pubmed-meshheading:12540953-Half-Life,
pubmed-meshheading:12540953-Humans,
pubmed-meshheading:12540953-Kinetics,
pubmed-meshheading:12540953-Metabolic Clearance Rate,
pubmed-meshheading:12540953-Protein Precursors,
pubmed-meshheading:12540953-Rabbits,
pubmed-meshheading:12540953-Receptors, Peptide
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pubmed:year |
2003
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pubmed:articleTitle |
The circulatory half-lives of alpha-profibrin and alpha-fibrin monomer, and comparisons with other fibrin(ogen) derivatives.
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pubmed:affiliation |
Department of Chemistry, Cleveland State University, Cleveland, OH 44115, USA. j.shainoff@csuohio.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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