Abstract
Two small molecular weight fibrin degradation product, the pentapeptide 6A and the undecapeptide 6D, produced relaxations of norepinephrine-contracted rabbit aorta strips. The relaxations were slow-developing and were elicited by both peptides at supramicromolar concentrations; the amplitude of relaxations were small for 6D. The relaxations induced by 6A were not dependent on the presence of endothelium and were not modified by a mixture of indomethacin, pyrilamine, and cimetidine. The amplitude of the relaxations produced by 6A and 6D increased as a function of incubation time in vitro. In another experimental system, peptides 6A and 6D failed to increase 6-keto-PGF1 alpha release from cultured human umbilical endothelial cells. Histamine and bradykinin were both active in this system.
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