Chaudhuri A G, Sen P C, Ganguly U
National Institute of Cholera and Enteric Diseases, Calcutta, India.
Biochem Mol Biol Int. 1995 Mar;35(3):567-74.
Plasma membranes isolated from Escherichia coli heat stable enterotoxin (STa) treated rat enterocytes were studied in respect to protein kinase C activity and fluidity change. Pretreatment of enterocytes with STa increased the membrane bound protein kinase C activity about 5 fold as compared to control. STa treatment made the membrane more fluid as evident from a higher phospholipid/cholesterol ratio and greater unsaturated fatty acid levels. Moreover, the phase transition temperature of the STa treated membrane appeared to be significantly lower than that of the corresponding control membrane, thereby further indicating a rise in fluidity of the membrane in the former case. Our results, therefore, suggested that following STa enterotoxin treatment an appropriate fluid environment in the rat intestinal cell membrane was essential for the activation of protein kinase C.
对从经大肠杆菌热稳定肠毒素（STa）处理的大鼠肠上皮细胞中分离出的质膜进行了蛋白激酶C活性和流动性变化方面的研究。与对照组相比，用STa预处理肠上皮细胞可使膜结合蛋白激酶C活性增加约5倍。STa处理使膜的流动性增强，这从较高的磷脂/胆固醇比率和更高的不饱和脂肪酸水平可以明显看出。此外，经STa处理的膜的相变温度似乎明显低于相应的对照膜，从而进一步表明在前一种情况下膜的流动性增加。因此，我们的结果表明，在STa肠毒素处理后，大鼠肠细胞膜中合适的流体环境对于蛋白激酶C的激活至关重要。
