Colecystokinin octapeptide CCK‐8 and carbachol reduce [32P]orthophosphate labeling of phosphatidylcholine without modifying phospholipase D activity in rat pancreatic acini

FEBS Letters

Salido, Ginés¹  Ramos, Belén¹  Claro, Enrique³  Sarri, Elisabet² 

[1] Departamento de Fisiologı́a, Universidad de Extremadura, Cáceres, Spain;Departament de Bioquimica i Biologia Molecular, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain;Departmento de Bioquı́mica y Biologı́a Molecular, Universidad de Extremadura, Cáceres, Spain

关键词: Phospholipase D;    Phosphatidylcholine;    Phosphatidylethanol;    Pancreatic acinus;    CCK-8;    cholecystokinin octapeptide (26–33);    Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2;    Cch;    carbachol;    PMA;    phorbol myristate acetate;   

DOI  :  10.1016/S0014-5793(00)02233-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have studied phospholipase D activation in [³²P]orthophosphoric acid-prelabeled rat pancreatic acini by measuring the formation of ³²P-phosphatidylalcohols as stimulated in the presence of ethanol or butanol. A small but significant and time-dependent basal accumulation of [³²P]phosphatidylethanol and [³²P]phosphatidylbutanol was detected, which was further stimulated by phorbol myristate acetate, orthovanadate and pervanadate. However, the secretagogues cholecystokinin octapeptide and carbachol did not enhance basal accumulation of ³²P-phosphatidylalcohol, yet they decreased [³²P]phosphatidylcholine content and stimulated the generation of [³²P]phosphatidic acid. Our results stress the need to examine the transphosphatidylation reaction as well as agonist effects on the synthesis of phosphatidylcholine in order to assess unambiguously phospholipase D activity.

【 授权许可】

Unknown