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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Vincenot A,Gaussem P,Pittet JL,Debost S,Aiach Mdoi
10.1016/0014-5793(95)00552-ksubject
Has Abstractpub_date
1995-06-26 00:00:00pages
153-7issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(95)00552-Kjournal_volume
367pub_type
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