Literature DB >> 1709373

The sequence gamma-(312-324) is a fibrin-specific epitope.

W J Schielen1, H P Adams, K van Leuven, M Voskuilen, G I Tesser, W Nieuwenhuizen.   

Abstract

Fibrin accelerates the activation of plasminogen catalyzed by tissue-type plasminogen activator much stronger than fibrinogen. Detailed studies showed that (part of) this rate-enhancing effect of fibrin is brought about by two sites in the fibrin molecule: one in A alpha-(148-160) and one in the gamma-chain stretch 311-379 (also known as FCB-5). During the fibrinogen-to-fibrin conversion, A alpha-(148-160) appears to become accessible, because a monoclonal antibody against synthetic A alpha-(148-160) reacts with fibrin, but not with fibrinogen. Because a similar situation may exist for (at least parts of) FCB-5, we have prepared a monoclonal antibody against a part (ie, gamma-[312-324]) of FCB-5, and found that this is fibrin-specific and does not bind fibrinogen. We conclude that gamma-(312-324) is hidden in fibrinogen and is exposed by the formation of fibrin.

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Year:  1991        PMID: 1709373

Source DB:  PubMed          Journal:  Blood        ISSN: 0006-4971            Impact factor:   22.113


  8 in total

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Journal:  Acta Biomater       Date:  2022-01-07       Impact factor: 8.947

6.  Structural control of fibrin bioactivity by mechanical deformation.

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7.  Tissue plasminogen activator (tPA) inhibits plasmin degradation of fibrin. A mechanism that slows tPA-mediated fibrinolysis but does not require alpha 2-antiplasmin or leakage of intrinsic plasminogen.

Authors:  J H Wu; S L Diamond
Journal:  J Clin Invest       Date:  1995-06       Impact factor: 14.808

Review 8.  Biophysical Mechanisms Mediating Fibrin Fiber Lysis.

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  8 in total

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