The Ligand Recognition Motifs of α4-Integrins and Leukocyte Integrins

  • Johannes A. Eble


The linear peptide sequence arginine-glycine-aspartate (RGD) was the first integrin recognition site to be discovered on an extracellular matrix molecule, namely fibronectin.1 This RGD-sequence resides in the tenth fibronectin type III repeat within the fibronectin molecule and is recognized by the classical fibronectin receptor, the α5β1 integrin.2,3 Fibronectin (Fn) consists of two chains, which are covalently disulfide-linked in their C-terminal regions. Each Fn chain is composed of three types of repeat domains, termed Fn type I, II and III repeats. They are arranged into various modules which fulfill distinct tasks, e.g., mediating interactions with other extracellular matrix components or binding to cell surface receptors (Fig. 4.2.1). Cellular fibronectin (cFn), which forms the insoluble matrix around fibroblasts, and soluble plasma fibronectin (pFn) are isoforms, which differ in the presence and absence, respectively, of two commonly spliced domains EIIIA and EIIIB.4 Platelet fibronectin, a third isoform, resembles cellular fibronectin.4


Vascular Cell Adhesion Molecule Vascular Cell Adhesion Cellular Fibronectin Bivalent Ligand Cell BioI 
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  • Johannes A. Eble

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