豚鼠胃α-毒素通透平滑肌细胞中收缩蛋白对Ca2+的非蛋白激酶C依赖性致敏作用。
Protein kinase C-independent sensitization of contractile proteins to Ca2+ in alpha-toxin-permeabilized smooth muscle cells from the guinea-pig stomach.
作者信息
Oishi K, Mita M, Ono T, Hashimoto T, Uchida M K
机构信息
Department of Molecular Pharmacology, Meiji College of Pharmacy, Tokyo, Japan.
出版信息
Br J Pharmacol. 1992 Dec;107(4):908-9. doi: 10.1111/j.1476-5381.1992.tb13383.x.
Abstract
Involvement of protein kinase C in receptor-operated Ca2+ sensitization of cell shortening was investigated by use of alpha-toxin-permeabilized smooth muscle cells from the fundus of the guinea-pig. Most of the isolated cells responded to 0.6 microM Ca2+ with a maximal shortening to approximately 65% of the resting cell length. Addition of acetylcholine (ACh) at a maximal concentration (10 microM) resulted in a marked decrease in the concentration of Ca2+ required to trigger a threshold response from 0.6 microM to 0.2 microM. The augmentation of Ca2+ sensitivity by ACh was not inhibited by specific protein kinase C inhibitors, calphostin C and K-252b at a concentration of 1 microM. These findings suggest that protein kinase C is not involved in the muscarinic receptor-operated augmentation of Ca2+ sensitivity.
摘要
利用豚鼠胃底α-毒素通透的平滑肌细胞，研究蛋白激酶C在受体介导的细胞缩短Ca²⁺敏感性中的作用。大多数分离的细胞对0.6微摩尔/升Ca²⁺产生反应，最大缩短至静息细胞长度的约65%。以最大浓度（10微摩尔/升）添加乙酰胆碱（ACh）导致触发阈值反应所需的Ca²⁺浓度从0.6微摩尔/升显著降低至0.2微摩尔/升。1微摩尔/升浓度的特异性蛋白激酶C抑制剂钙泊素C和K-252b不抑制ACh对Ca²⁺敏感性的增强。这些发现表明蛋白激酶C不参与毒蕈碱受体介导的Ca²⁺敏感性增强。
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