Liebmann C, Reissmann S, Robberecht P, Arold H
Department of Biology, Friedrich Schiller University Jena, GDR.
Biomed Biochim Acta. 1987;46(6):469-78.
Bradykinin binds to a single class of binding sites at rat duodenum plasma membranes. In the presence of endogenous calcium and at low bradykinin concentrations the receptor activation is followed by a stimulation of adenylate cyclase activity and the elevation of the cAMP level. In the absence of calcium and at high peptide concentrations the cAMP level is lowered via both inhibition of adenylate cyclase and stimulation of cAMP-phosphodiesterase. These different changes in the cAMP level might be correlated with the biphasic pharmacological action of bradykinin in the rat duodenum. The results suggest that one type of bradykinin (B2) receptor is able to initiate several effectuation mechanisms.
缓激肽与大鼠十二指肠质膜上的一类结合位点结合。在内源性钙存在且缓激肽浓度较低的情况下，受体激活后会刺激腺苷酸环化酶活性并提高环磷酸腺苷（cAMP）水平。在无钙且肽浓度较高的情况下，cAMP水平会因腺苷酸环化酶受抑制和cAMP磷酸二酯酶受刺激而降低。cAMP水平的这些不同变化可能与缓激肽在大鼠十二指肠中的双相药理作用相关。结果表明，一种类型的缓激肽（B2）受体能够启动多种效应机制。
