HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nishioka, J. Articles by Suzuki, K. Search for Related Content PubMed PubMed Citation Articles by Nishioka, J. Articles by Suzuki, K. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 16, 9072-9076, 06, 1990

Inhibition of cofactor activity of protein S by a complex of protein S and C4b-binding protein. Evidence for inactive ternary complex formation between protein S, C4b-binding protein, and activated protein C

J Nishioka and K Suzuki
Department of Laboratory Medicine, Mie University School of Medicine, Japan.

To elucidate the mechanism by which C4b-binding protein inhibits the cofactor activity of protein S for anticoagulant-activated protein C, the interactions between protein S, activated protein C, and C4b- binding protein were studied using solid-phase enzyme immunoassays. Both activated protein C and C4b-binding protein bound to protein S fixed to microplate wells. C4b-binding protein did not inhibit the binding of activated protein C to protein S, nor did activated protein C inhibit the binding of C4b-binding protein to protein S. Activated protein C bound to a protein S-C4b-binding protein complex which was cross-linked with a chemical reagent as well as it bound to free protein S. Protein S-C4b-binding protein complex competitively inhibited activated protein C-binding to free protein S and also the cofactor activity of free protein S. Immunoblotting analysis showed ternary complex formation with protein S, C4b-binding protein, and activated protein C in the liquid phase by treatment with the cross- linking reagent. These findings suggest that the protein S-C4b-binding protein complex inhibits the cofactor activity of free protein S probably by inhibition of functionally active protein S-activated protein C complex formation by the apparent competitive formation of an inactive ternary complex with protein S, C4b-binding protein, and activated protein C.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				L. F. A. Maurissen, M. C. L. G. D. Thomassen, G. A. F. Nicolaes, B. Dahlback, G. Tans, J. Rosing, and T. M. Hackeng Re-evaluation of the role of the protein S-C4b binding protein complex in activated protein C-catalyzed factor Va-inactivation Blood, March 15, 2008; 111(6): 3034 - 3041. [Abstract] [Full Text] [PDF]

				S. Schneider, T. Sakert, J. Lucke, P. McKeown, and A. Sharma Cardiopulmonary bypass for a coronary artery bypass graft patient with heterozygous protein C deficiency and protein S deficiency Perfusion, March 1, 2006; 21(2): 117 - 120. [Abstract] [PDF]

				R. H. L. van de Poel, J. C. M. Meijers, and B. N. Bouma Interaction between Protein S and Complement C4b-binding Protein (C4BP). AFFINITY STUDIES USING CHIMERAS CONTAINING C4BP beta -CHAIN SHORT CONSENSUS REPEATS J. Biol. Chem., May 21, 1999; 274(21): 15144 - 15150. [Abstract] [Full Text] [PDF]