Amino acids 225-235** of the protein C serine-protease domain are important for the interaction with the thrombin-thrombomodulin complex

FEBS Letters
A VincenotM Aiach

Abstract

Protein C (PC) is a vitamin K-dependent zymogen that inactivates factors Va and VIIIa after its activation by thrombin complexed to thrombomodulin. We characterized a monoclonal antibody (mAb) against PC, whose only influence on PC functions was to inhibit PC activation by the thrombin-thrombomodulin complex. It recognized an epitope in the PC heavy chain, the conformation of which is calcium-dependent. The mAb did not recognize a natural PC variant that was not activated by the thrombin-thrombomodulin complex (mutation R229Q) and did recognize a synthetic peptide corresponding to PC amino acids 225-235 in an Elisa assay. The peptide inhibited PC activation by the thrombin-thrombomodulin complex. These data confirm that the calcium-binding loop of the serine-protease domain is involved in the interaction of PC with the thrombin-thrombomodulin complex.

References

Feb 1, 1992·Arteriosclerosis and Thrombosis : a Journal of Vascular Biology·C T Esmon
May 1, 1992·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·F J Walker, P J Fay
May 20, 1988·Cell·B Furie, B C Furie
Apr 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·C BornerD Fabbro
Apr 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·C T Esmon, W G Owen
Apr 1, 1994·Protein Science : a Publication of the Protein Society·C L FisherJ H Griffin
Sep 1, 1993·Protein Science : a Publication of the Protein Society·R M MestersJ H Griffin

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Citations

Nov 11, 2011·Thrombosis and Haemostasis·Karin C A A WildhagenGerry A F Nicolaes
Feb 17, 2006·Blood Cells, Molecules & Diseases·Wolfram Bode
Oct 1, 2018·Journal of Cellular Biochemistry·Najmeh JaberiSeyed Mahdi Hassanian
Jan 17, 2003·The Journal of Biological Chemistry·Likui Yang, Alireza R Rezaie

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