Grosso L E, Scott M
Department of Pathology, Jewish Hospital of St. Louis, Washington University Medical Center, MO 63110.
Matrix. 1993 Mar;13(2):157-64. doi: 10.1016/s0934-8832(11)80074-0.
Tropoelastin is composed of alternating hydrophobic and hydrophilic domains. A hydrophobic peptide, VGVAPG, has been shown to be a ligand for a 67-kDa elastin cell surface receptor expressed on fetal bovine auricular chondrocytes and ligamentum nuchae fibroblasts. To explore the possibility that tropoelastin contains additional peptide ligands for this elastin receptor, we have constructed two deletion proteins that are expressed in E. coli and lack the repeated VGVAPG sequence. These proteins supported bovine fibroblast attachment implying the presence of a receptor binding site. Experiments using synthetic peptides contained within these proteins identify a chemotactic peptide, PGAIPG, and a chemokinetic peptide, GAIPG, PGAIPG was identified as a ligand for the bovine elastin receptor.
原弹性蛋白由交替的疏水结构域和亲水结构域组成。一种疏水肽VGVAPG已被证明是在胎牛耳廓软骨细胞和项韧带成纤维细胞上表达的67 kDa弹性蛋白细胞表面受体的配体。为了探究原弹性蛋白是否含有该弹性蛋白受体的其他肽配体,我们构建了两种在大肠杆菌中表达且缺乏重复VGVAPG序列的缺失蛋白。这些蛋白支持牛成纤维细胞附着,这意味着存在受体结合位点。使用这些蛋白中包含的合成肽进行的实验鉴定出一种趋化肽PGAIPG和一种趋动肽GAIPG,PGAIPG被鉴定为牛弹性蛋白受体的配体。