rdf:type |
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lifeskim:mentions |
umls-concept:C0019137,
umls-concept:C0036733,
umls-concept:C0040018,
umls-concept:C0205214,
umls-concept:C0332120,
umls-concept:C0439855,
umls-concept:C0449297,
umls-concept:C0699900,
umls-concept:C1515655,
umls-concept:C1704259,
umls-concept:C1705987
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pubmed:issue |
1
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pubmed:dateCreated |
1988-5-10
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pubmed:abstractText |
The plasma clearance of 125I-labeled human heparin cofactor II and its complex with thrombin was studied in mice to determine whether a specific mechanism exists for the catabolism of the inhibitor-proteinase complex. Initial studies demonstrated that murine plasma contains a heparin cofactor II-like inhibitor as shown by the presence of a dermatan sulfate-sensitive thrombin inhibitor. Human heparin cofactor II cleared from the circulation of mice with an apparent half-life of 80 min while heparin cofactor II-thrombin complexes cleared with an apparent half-life of only 10 min. The specificity of the clearance mechanism was investigated by clearance competition studies involving coinjection of excess unlabeled heparin cofactor II-alpha-thrombin, antithrombin III-alpha-thrombin, or alpha 1-proteinase inhibitor-elastase, and by tissue distribution studies. The results demonstrated that the clearance of 125I-labeled heparin cofactor II-alpha-thrombin is a receptor-mediated process, and that the same hepatocyte receptor system recognizes complexes containing heparin cofactor II, antithrombin III, and alpha 1-proteinase inhibitor.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antithrombin III,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin Cofactor II,
http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha 1-Antitrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha 1-antitrypsin-leukocyte...
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
111-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3258496-Animals,
pubmed-meshheading:3258496-Antithrombin III,
pubmed-meshheading:3258496-Glycoproteins,
pubmed-meshheading:3258496-Half-Life,
pubmed-meshheading:3258496-Heparin Cofactor II,
pubmed-meshheading:3258496-Humans,
pubmed-meshheading:3258496-Leukocyte Elastase,
pubmed-meshheading:3258496-Macromolecular Substances,
pubmed-meshheading:3258496-Metabolic Clearance Rate,
pubmed-meshheading:3258496-Mice,
pubmed-meshheading:3258496-Pancreatic Elastase,
pubmed-meshheading:3258496-Protease Inhibitors,
pubmed-meshheading:3258496-Serine Proteinase Inhibitors,
pubmed-meshheading:3258496-Thrombin,
pubmed-meshheading:3258496-Tissue Distribution,
pubmed-meshheading:3258496-alpha 1-Antitrypsin
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pubmed:year |
1988
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pubmed:articleTitle |
In vivo catabolism of heparin cofactor II and its complex with thrombin: evidence for a common receptor-mediated clearance pathway for three serine proteinase inhibitors.
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pubmed:affiliation |
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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