膵腺房細胞Somatostatin受容体特性に関する研究:-第一報-C端octapeptide CCK, carbachol前処理のsomatostatin結合抑制効果
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Somatostatin binding to its receptors on rat pancreatic acinar membranes was characterized with [<SUP>125</SUP>I-Tyr<SUP>1</SUP> somatostatin. The COOH-terminal octapeptide of cholecystokinin (CCK8), when present at various concentrations in the reaction mixture for the binding study, reduced labeled somatostatin binding in a dose-dependent manner, whereas carbachol or Ca<SUP>2+</SUP> ionophore did not affect the binding. By contrast, when pancreatic acini were first treated with carbachol and thereafter [<SUP>125</SUP>I-Tyr<SUP>1</SUP> somatostatin binding to membranes prepared from these acini was examined, carbachol reduced subsequent somatostatin binding in a dose-dependent manner. Scatchard analysis of the labeled somatostatin binding revealed that carbachol pretreatment decreased the maximum binding capacity from 142±20 fmol/ mg of membrane protein to 63.5±3.5 fmol/mg of membrane protein without significantly affecting the binding affinity. To test for the possibility that CCK<SUB>8</SUB> also may affect labeled somatostatin binding through an intracellular process, pancreatic acini were first treated with CCK<SUB>8</SUB> and then the membrane bound CCK<SUB>8</SUB> was washed out. Subsequent labeled somatostatin binding to membranes from these acini was also decreased. When 1 mM EDTA was present in the pretreatment medium, the inhibitory effect of carbachol or CCK<SUB>8</SUB> was partially abolished, suggesting that an intracellular process to modulate somatostatin binding is dependent on Ca<SUP>2+</SUP>. On the other hand, pretreatment of acini with Ca<SUP>2+</SUP>ionophore almost failed to affect subsequent labeled somatostatin binding.<BR>Results therefore suggest that 1) CCK<SUB>8</SUB> can modulate labeled somatostatin binding to pancreatic acinar membranes not only acting through an intracellular process but also at membrane sites and 2) carbachol-or CCK<SUB>8</SUB>-activated intracellular process to modulate somatostatin binding is dependent on Ca<SUP>2+</SUP>, but Ca<SUP>2+</SUP>mobilization itself is not sufficient to affect subsequent somatostatin binding.
- 一般社団法人 日本内分泌学会の論文
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