Roch-Arveiller M, Caranikas S, Regoli D, Giroud J P
Eur J Pharmacol. 1983 Mar 18;88(1):99-103. doi: 10.1016/0014-2999(83)90396-5.
Bradykinin (BK) and two of its C-terminal fragments, namely H-Phe-Ser-Pro-Phe-Arg-OH and H-Ser-Pro-Phe-Arg-OH were found to be potent inhibitors of the chemotaxis of rat polymorphonuclear neutrophils (PMN). The activity of the three peptides was significantly enhanced by SQ 14225, a rather specific inhibitor of kininase II. A shorter C-terminal sequence of BK (Phe-Arg-OH) was inactive. The whole peptide (BK) exerted potent actions on blood pressure and on isolated organs, e.g. the rabbit mesenteric vein or the guinea pig ileum, but none of its fragments showed similar effects. The present findings suggest that rat PMN possess membrane receptors which cannot be considered identical to B1- and B2-receptors, previously characterized on isolated smooth muscles.
发现缓激肽（BK）及其两个C末端片段，即H-Phe-Ser-Pro-Phe-Arg-OH和H-Ser-Pro-Phe-Arg-OH是大鼠多形核中性粒细胞（PMN）趋化作用的有效抑制剂。三种肽的活性通过激肽酶II的一种相当特异的抑制剂SQ 14225得到显著增强。BK的一个较短的C末端序列（Phe-Arg-OH）没有活性。整个肽（BK）对血压和离体器官，如兔肠系膜静脉或豚鼠回肠有强大作用，但它的任何片段都没有显示出类似作用。目前的研究结果表明，大鼠PMN拥有的膜受体不能被认为与先前在离体平滑肌上鉴定的B1和B2受体相同。
