Effects of bradykinin and some of its fragments on smooth muscles and chemotaxis.
作者： Monique Roch-Arveiller , Stephanos Caranikas , Doménico Regoli , Jean-Paul Giroud
DOI: 10.1016/0014-2999(83)90396-5
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摘要: Abstract Bradykinin (BK) and two of its C-terminal fragments, namely H-Phe-Ser-Pro-Phe-Arg-OH H-Ser-Pro-Phe-Arg-OH were found to be potent inhibitors the chemotaxis rat polymorphonuclear neutrophils (PMN). The activity three peptides was significantly enhanced by SQ 14225, a rather specific inhibitor kininase II. A shorter sequence BK (Phe-Arg-OH) inactive. whole peptide exerted actions on blood pressure isolated organs, e.g. rabbit mesentric vein or guinea pig ileum, but none fragments showed similar effects. present findings suggest that PMN possess membrane receptors which cannot considered identical B1- B2-receptors, previously characterized smooth muscles.
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