Rukavishnikova E V, Korolenko T A, Sassa T, Oka T, Horiuchi S, Natori Y
Department of Nutritional Chemistry, School of Medicine, University of Tokushima, Japan.
FEBS Lett. 1995 Aug 7;369(2-3):217-20. doi: 10.1016/0014-5793(95)00749-y.
In order to gain knowledge on the interaction of lysosomes with proteins, we have assessed the equilibrium densities of the lysosomal membrane and matrix markers after in vitro incubation of rat liver lysosomes with various polypeptides. The addition of basic polypeptides, polylysine or protamine, to the suspension of lysosomes brought about a profound alteration of lysosomal membrane, causing extensive leakage of lysosomal matrix enzymes. Electron microscopic observation revealed a remarkable aggregation of lysosomes by the basic polypeptides. Polyglutamic acid, an acidic polypeptide, did not produce such effect. ATP was found to stabilize lysosomes during incubation, particularly with basic polypeptides.
为了了解溶酶体与蛋白质之间的相互作用,我们在大鼠肝脏溶酶体与各种多肽进行体外孵育后,评估了溶酶体膜和基质标志物的平衡密度。向溶酶体悬浮液中添加碱性多肽、聚赖氨酸或鱼精蛋白会导致溶酶体膜发生显著改变,引起溶酶体基质酶的大量泄漏。电子显微镜观察显示碱性多肽可使溶酶体显著聚集。酸性多肽聚谷氨酸则不会产生这种效果。研究发现,ATP在孵育过程中可稳定溶酶体,尤其是在与碱性多肽共同孵育时。