Phorbol ester and neomycin dissociate bradykinin receptor-mediated arachidonic acid release and polyphosphoinositide hydrolysis in Madin-Darby canine kidney cells. Evidence that bradykinin mediates noninterdependent activation of phospholipases A2 and C.
作者： S R Slivka , P A Insel
DOI: 10.1016/S0021-9258(18)68085-8
关键词:
摘要: Many types of peptide hormone and neurotransmitter receptors mediate hydrolysis phosphoinositides (PI) arachidonic acid metabolite (AA) release, but the relation between these responses is not clearly defined. We have characterized bradykinin (BK)-mediated AA release PI in clonal Madin-Darby canine kidney cells (MDCK-D1). Both occurred over a similar dose range response to B1 B2 receptor agonist, BK, receptor-selective agonist des-Arg-BK. To test whether occurs via mechanism which sequential dependent upon hydrolysis, we used phorbol ester, 12-O-tetradecanoylphorbol-13-acetate (TPA), activates protein kinase C. TPA treatment blocked BK-mediated MDCK-D1 cells, while at same time concentrations enhancing release. Thus, dissociated from hydrolysis. In addition, with neomycin phosphatidylinositol bisphosphate without reducing BK increased formation lysophospholipids course accord indicating that least part was likely derived activation phospholipase A2. lysophospholipid production enhanced by pretreatment TPA, suggesting before after same. on presence extracellular calcium, were calcium. also calcium ionophore A23187. From data propose acting receptors, promotes MDCK 1) independent polyphosphoinositide C, 2) influx A2, 3)
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