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Volume 270, Number 33, Issue of August 18, pp. 19217-19224, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Factor V Is Complexed with Multimerin in Resting Platelet Lysates and Colocalizes with Multimerin in Platelet -Granules

(Received for publication, May 1, 1995)

Catherine P. M. Hayward ,&nbsp;<WBR> Emilia Furmaniak-Kazmierczak ,&nbsp;<WBR> Anne-Marie Cieutat ,&nbsp;<WBR> Jane C. Moore ,&nbsp;<WBR> Dorothy Ford Bainton ,&nbsp;<WBR> Michael E. Nesheim ,&nbsp;<WBR> John G. Kelton ,&nbsp;<WBR> Graham Côté

Factor V stored in platelets is an important source of factor Va for the prothrombinase complex. Investigations of potential platelet factor Va-binding proteins, using factor Va light chain affinity chromatography, identified a disulfide-linked multimeric protein with a reduced mobility of 155 kDa in the column eluate. Immunodepletion and immunoblotting indicated that this protein was multimerin. Multimerin specifically bound factors V and Va and the isolated factor Va light chain, but not the heavy chain of factor Va. Factor V stored in platelets, but not plasma factor V, was found to be complexed with multimerin. Multimerin immunodepletion of resting platelet lysates was associated with the removal of factor V and the loss of factor V coagulant activity. Immunoelectron microscopic studies colocalized factor V with multimerin in the alpha-granules of resting platelets. With thrombin-induced platelet activation, we observed dissociation of factor Va-multimerin complexes, multimerin-independent membrane binding of factor Va, and prothrombinase activity that was not inhibitable by multimerin antibodies. This study indicates that platelet factor V is stored as a complex with multimerin and suggests a possible role for multimerin as a carrier protein for factor V stored in platelets.




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