The Na-K-Cl cotransporter of avian salt gland. Phosphorylation in response to cAMP-dependent and calcium-dependent secretogogues.
作者： J Torchia , C Lytle , D.J. Pon , B Forbush , A.K. Sen
DOI: 10.1016/S0021-9258(19)74061-7
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摘要: The effect of a cAMP-dependent secretogogue (VIP) on the phosphorylation an endogenous, membrane-bound protein (pp170) was assessed in intact cell preparation from avian salt gland. addition VIP, presence 100 microM isobutylmethylxanthine, resulted concentration-dependent increase pp170. This rapid and transient with 3-5-fold occurring 1 min after VIP. Under similar incubation conditions, VIP stimulated 4.6-fold cAMP accumulation that paralleled phosphorylation. Exposure cells to either forskolin or 8-Br-cAMP 5-8-fold dose dependent EC50 for stimulation secretion (35 nM). These results implicate involvement kinase identity pp170 utilizing monoclonal antibody (Q3) directed against Q3 recognized single 170-kDa band Western blots gland membrane protein. Immunoprecipitation selective extraction whose state increased approximately 5-fold response carbachol established using two criteria. First, affinity-purified Na:K:Cl cotransporter preparations shark rectal membranes. Second, selectively immunoprecipitated by antibodies (J3, J4, J7) recognize different epitopes transport suggest is homologous Na-K-Cl cotransporter, thus proteins may be functionally similar.
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