Abstract
Although in a gross sense fibrin is merely a collection of fibrinogen molecules packed together in bundles, numerous small structural differences can arise as a result of the conversion of the soluble precursor into the gelled product. Some of the consequences are obvious, others more subtle. In one way or another, all these changes are the result of a sequence of events that includes the release of the fibrinopeptides A and B, the formation of protofibrils, the cross-linking of γ chains, the assembly into mature fibers and the cross-linking of α chains. Numerous immunologic differences between fibrinogen and fibrin have been cataloged, and putative sites for fibrin enhancing the activity of plasminogen activators have been identified. Although some conformational changes have been found by X-ray crystallography, the structural changes leading to the exposure of sites thought to bind t-PA and/or plasminogen remain to be demonstrated.
Keywords: Fibrinogen, fibrin, tissue plasminogen activator, plasminogen, conformational changes, synthetic peptide knobs
Cardiovascular & Hematological Agents in Medicinal Chemistry
Title: Searching for Differences between Fibrinogen and Fibrin that Affect the Initiation of Fibrinolysis
Volume: 6 Issue: 3
Author(s): Russell F. Doolittle
Affiliation:
Keywords: Fibrinogen, fibrin, tissue plasminogen activator, plasminogen, conformational changes, synthetic peptide knobs
Abstract: Although in a gross sense fibrin is merely a collection of fibrinogen molecules packed together in bundles, numerous small structural differences can arise as a result of the conversion of the soluble precursor into the gelled product. Some of the consequences are obvious, others more subtle. In one way or another, all these changes are the result of a sequence of events that includes the release of the fibrinopeptides A and B, the formation of protofibrils, the cross-linking of γ chains, the assembly into mature fibers and the cross-linking of α chains. Numerous immunologic differences between fibrinogen and fibrin have been cataloged, and putative sites for fibrin enhancing the activity of plasminogen activators have been identified. Although some conformational changes have been found by X-ray crystallography, the structural changes leading to the exposure of sites thought to bind t-PA and/or plasminogen remain to be demonstrated.
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Cite this article as:
Doolittle F. Russell, Searching for Differences between Fibrinogen and Fibrin that Affect the Initiation of Fibrinolysis, Cardiovascular & Hematological Agents in Medicinal Chemistry 2008; 6 (3) . https://dx.doi.org/10.2174/187152508784871954
DOI https://dx.doi.org/10.2174/187152508784871954 |
Print ISSN 1871-5257 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6182 |
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