Czogalla A, Sikorski A F
Institute of Biochemistry and Molecular Biology, University of Wrocław, ul. Przybyszewskiego 63/77, 51-148, Wrocław, Poland.
Cell Mol Life Sci. 2005 Sep;62(17):1913-24. doi: 10.1007/s00018-005-5097-0.
It is well documented that activation of calpain, a calcium-sensitive cysteine protease, marks the pathology of naturally and experimentally occurring neurodegenerative conditions. Calpain-mediated proteolysis of major membrane-skeletal protein, alphaII-spectrin, results in the appearance of two unique and highly stable breakdown products, which is an early event in neural cell pathology. This review focuses on spectrin degradation by calpain within neurons induced by diverse conditions, emphasizing a current picture of multi-pattern neuronal death and a recent success in the development of spectrin-based biomarkers. The issue is presented in the context of the major structural and functional properties of the two proteins.
有充分的文献记载,钙蛋白酶(一种钙敏感的半胱氨酸蛋白酶)的激活标志着自然发生和实验诱导的神经退行性疾病的病理过程。钙蛋白酶介导的主要膜骨架蛋白αII-血影蛋白的蛋白水解作用会产生两种独特且高度稳定的降解产物,这是神经细胞病理过程中的早期事件。本综述聚焦于多种条件诱导的神经元内钙蛋白酶介导的血影蛋白降解,强调了当前多模式神经元死亡的情况以及基于血影蛋白的生物标志物开发的最新成果。本文将在这两种蛋白质的主要结构和功能特性的背景下阐述这一问题。