Haitoglou C S, Tsilibary E C, Brownlee M, Charonis A S
Department of Laboratory Medicine and Pathology, University of Minnesota Medical School, Minneapolis 55455.
J Biol Chem. 1992 Jun 25;267(18):12404-7.
Laminin and type IV collagen are two major basement membrane glycoproteins. In previous studies it has been shown that nonenzymatic glucosylation induces structural alterations of these macromolecules and also reduces their ability to self-associate. In the present study, endothelial cells were tested for their ability to adhere and spread on nonenzymatically glucosylated laminin and type IV collagen. Adhesion and spreading were reduced when glucosylated macromolecules were used as substrates. Glucosylation-induced changes in adhesion and spreading may be an important initial event signaling other phenotypic modifications of cells in the microvasculature and may be a crucial factor in order to understand the pathogenesis of diabetic microangiopathy at the molecular level.
层粘连蛋白和IV型胶原蛋白是两种主要的基底膜糖蛋白。在先前的研究中已经表明,非酶糖基化会诱导这些大分子的结构改变,并且还会降低它们自我缔合的能力。在本研究中,测试了内皮细胞在非酶糖基化的层粘连蛋白和IV型胶原蛋白上的黏附与铺展能力。当使用糖基化的大分子作为底物时,黏附与铺展减少。糖基化诱导的黏附与铺展变化可能是一个重要的初始事件,预示着微血管中细胞的其他表型修饰,并且可能是在分子水平理解糖尿病微血管病变发病机制的一个关键因素。