Formisano P, Beguinot F
Department of Biology and Cellular and Molecular Pathology L. Califano, Federico II University of Naples, Italy.
J Endocrinol Invest. 2001 Jun;24(6):460-7. doi: 10.1007/BF03351048.
Insulin action on target tissues is mediated by specific tyrosine kinase receptors. Upon ligand binding insulin receptors autophosphorylate and phosphorylate intracellular substrates on tyrosine residues. These early events of insulin action are followed by the activation of a number of enzymes, including protein kinase C (PKC). At least 14 PKC isoforms have been identified and cloned to date. PKCs appear to play dual roles in insulin signaling. For instance, they are involved in transduction of specific insulin signals but also contribute to the generation of insulin resistance. In this article, we will analyze the experimental evidence addressing the mechanism by which insulin might activate individual PKC isoforms as well as the role of single PKCs in insulin-induced bioeffects.
胰岛素对靶组织的作用是由特定的酪氨酸激酶受体介导的。配体结合后,胰岛素受体发生自身磷酸化,并使细胞内底物的酪氨酸残基磷酸化。胰岛素作用的这些早期事件之后是多种酶的激活,包括蛋白激酶C(PKC)。迄今为止,已鉴定并克隆出至少14种PKC亚型。PKC在胰岛素信号传导中似乎发挥着双重作用。例如,它们参与特定胰岛素信号的转导,但也会导致胰岛素抵抗的产生。在本文中,我们将分析有关胰岛素激活单个PKC亚型的机制以及单个PKC在胰岛素诱导的生物效应中的作用的实验证据。