Macaulay S L, Larkins R G
University of Melbourne, Department of Medicine, Royal Melbourne Hospital, Parkville, Australia.
Cell Signal. 1990;2(1):9-19. doi: 10.1016/0898-6568(90)90028-9.
This study investigated the extent to which a purified phosphatidylinositol-specific and a commercial non-specific phospholipase C mimicked acute insulin action in rat adipocytes. The enzymes mimicked insulin stimulation of pyruvate dehydrogenase (PDH) and breakdown of a glycophospholipid proposed as a precursor for an intracellular mediator of insulin action, but were much less effective in stimulating glucose transport and utilization. These observations corroborate recent suggestions that insulin may activate a phospholipase C to generate a mediator that can account for insulin activation of PDH from a mediator precursor with a phosphatidylinositol anchor. This mediator precursor is probably an outer membrane component since effects were obtained with intact cells. It is unlikely that this mechanism accounts fully for insulin action since phosphatidylinositol-specific and commercial phospholipase C stimulation of glucose transport was significantly less than that elicited by insulin.
本研究调查了纯化的磷脂酰肌醇特异性磷脂酶C和市售非特异性磷脂酶C在多大程度上模拟了大鼠脂肪细胞中的急性胰岛素作用。这些酶模拟了胰岛素对丙酮酸脱氢酶(PDH)的刺激以及一种被认为是胰岛素作用细胞内介质前体的糖磷脂的分解,但在刺激葡萄糖转运和利用方面效果要差得多。这些观察结果证实了最近的观点,即胰岛素可能激活磷脂酶C以产生一种介质,该介质可以解释胰岛素从具有磷脂酰肌醇锚定的介质前体激活PDH的过程。这种介质前体可能是一种外膜成分,因为完整细胞能产生相应效应。由于磷脂酰肌醇特异性磷脂酶C和市售磷脂酶C对葡萄糖转运的刺激明显低于胰岛素引起的刺激,所以这种机制不太可能完全解释胰岛素的作用。