蛋白激酶C调节磷脂酶C并增加缓激肽刺激的MDCK细胞中花生四烯酸的释放。
Protein kinase C modulates phospholipase C and increases arachidonic acid release in bradykinin stimulated MDCK cells.
作者信息
Portilla D, Mordhorst M, Bertrand W, Morrison A R
机构信息
Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
出版信息
Biochem Biophys Res Commun. 1988 May 31;153(1):454-62. doi: 10.1016/s0006-291x(88)81246-4.
The tumor promoter phorbol ester (PMA) has been shown to stimulate protein kinase C (PKC) in MDCK cells. At the concentrations that produce stimulation of PKC, PMA (100 microM) inhibits BK-induced I1,4,5P3 (IP3) formation and calcium transients in these cells. 1-5-isoquinolinyl-2-methyl-piperazine (H7) a known inhibitor of PKC in MDCK cells reverses the effect of PMA on BK-stimulated IP3 formation and Ca2+ transients in these cells. PMA also stimulates arachidonate release which can be inhibited by preincubation with H7. A dual mechanism of regulation by PKC at the level of phospholipase C (down regulation) and phospholipase A2 (stimulation) is suggested in these cells.
肿瘤促进剂佛波酯（PMA）已被证明可刺激MDCK细胞中的蛋白激酶C（PKC）。在产生PKC刺激作用的浓度下，PMA（100微摩尔）可抑制这些细胞中BK诱导的1,4,5-三磷酸肌醇（IP3）形成和钙瞬变。1-5-异喹啉基-2-甲基哌嗪（H7）是MDCK细胞中已知的PKC抑制剂，可逆转PMA对这些细胞中BK刺激的IP3形成和Ca2+瞬变的影响。PMA还可刺激花生四烯酸释放，而预先用H7孵育可抑制这种释放。这些细胞提示PKC在磷脂酶C水平（下调）和磷脂酶A2水平（刺激）存在双重调节机制。
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