Sheppard A, Wu J, Bahr B A, Lynch G
Center for the Neurobiology of Learning and Memory, University of California, Irvine 92717-3800.
Synapse. 1991 Nov;9(3):231-4. doi: 10.1002/syn.890090310.
An activated form of calpain I associates with telencephalic membranes in a developmentally regulated fashion during early postnatal ontogeny. During this period, the cytoskeletal component spectrin is available and appears to be differentially susceptible to calpain-mediated cleavage. Lectin blotting techniques demonstrated that the leupeptin-sensitive action of calpain is primarily directed toward large proteins which are glycoconjugate in nature; neuronal cell adhesion molecules are among the glycoproteins whose associations with the telencephalic membranes decrease due to calpain activity. These data suggest that cytoplasmic calpain is translocated to the membrane during early brain development in order to act on the cytoskeletal and adhesive structures responsible in part for neuronal shape and function.
在出生后早期个体发育过程中，钙蛋白酶I的一种活化形式以发育调节的方式与端脑细胞膜相关联。在此期间，细胞骨架成分血影蛋白存在，并且似乎对钙蛋白酶介导的裂解具有不同的敏感性。凝集素印迹技术表明，钙蛋白酶对亮抑蛋白酶肽敏感的作用主要针对本质上为糖缀合物的大蛋白；神经元细胞粘附分子是由于钙蛋白酶活性而与端脑细胞膜的结合减少的糖蛋白之一。这些数据表明，在大脑早期发育过程中，细胞质中的钙蛋白酶会转移到膜上，以便作用于部分负责神经元形状和功能的细胞骨架和粘附结构。
