Fibrinogen alpha C domains contain cryptic plasminogen and tPA binding sites.

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G Tsurupa; L Medved (Profiled Author: Leonid Medved)

Biochemistry Department, Holland Laboratory, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855, USA. tsiouriog@usa.redcross.org
Annals of the New York Academy of Sciences 2001;936():328-30.

PubMed

Abstract

Surface plasmon resonance and ELISA experiments revealed that recombinant fibrinogen alpha C fragment (residues A alpha 221-610) corresponding to the alpha C domain binds tPA and plasminogen with high affinity. This binding was found to be Lys-dependent and occurred via independent binding sites. Study with truncated variants of the alpha C fragment located these sites in its COOH-terminal half. Binding of tPA and plasminogen to these sites stimulated activation of the latter whereas proteolytic degradation of the alpha C fragment reduced this effect substantially, suggesting the importance of the alpha C domains in regulation of fibrinolysis.

1 Originating Grant

1.

MEDVED, LEONID V.

Fibrin(ogen) Structure and Interactions

1 January 1998 - 31 July 2012
NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

Scientific Context

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