Analogy between fibrinogen and casein. Effect of an undecapeptide isolated from k-casein on platelet function

Pierre JOLLES(Centre National de la Recherche Scientifique), S Lévy-Toledano(Centre National de la Recherche Scientifique), Anne‐Marie Fiat(Centre National de la Recherche Scientifique), Claudine Soria(Centre National de la Recherche Scientifique), Dieter Gillessen(Roche (Switzerland)), Annick Thomaïdis(Centre National de la Recherche Scientifique), F. Dunn(Centre National de la Recherche Scientifique), Jacques Caen(Centre National de la Recherche Scientifique)
European Journal of Biochemistry
July 1, 1986
10.1111/j.1432-1033.1986.tb09764.x
Cited by 180Open Access
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Abstract

A large number of similarities have previously been noted between the blood and milk clotting phenomena [Jollès, P. (1975) Mol. Cell. Biochem. 7, 73-85; Jollès, P. & Henschen, A. (1982) Trends Biochem. Sci. 7, 325-328]: some analogous features have also been found between fibrinogen and kappa-casein. In this connection, the effect of a natural and a synthetic peptide derived from kappa-casein on platelet function was studied: the undecapeptide Met-Ala-Ile-Pro-Pro-Lys-Lys-Asn-Gln-Asp-Lys (residues 106----116 of cow kappa-casein) inhibited both aggregation of ADP-treated platelets and binding of 125I-fibrinogen to ADP-treated platelets: its behaviour was similar to that of the structurally related C-terminal dodecapeptide of human fibrinogen gamma-chain.

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