PGAIPG, a Repeated Hexapeptide of Bovine Tropoelastin, is a Ligand for the 67-kDa Bovine Elastin Receptor

Abstract

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.