The integrins. This image portrays the integrin family of transmembrane molecules (receptors), which interact with the molecules of the ECM (ligands) and ligands associated with other cellular elements. Integrins are heterodimers, consisting of an alpha unit on the left made up of two disulfide bonded polypeptide chains. The beta unit on the right consists of a single polypeptide chain. Integrins bind to matrix ligand binding sties, which are specific amino acid sequences (usually 3–8) and at the top of this image the RGD (arginine, glycine, and aspartyl amino acids) matrix ligand – binding site is demonstrated. There are three domains: the extracellular domain – the transmembrane domain – the cytosolic domain, which interact with the cytosolic cytoskeletal proteins: Actin and Talin. These special transmembrane molecules allow for the "outside in" and "inside out" communication between cells and the ECM. Glucotoxicity affects integrin function through decreased perlecan within BMs and this may increase the susceptibility of endothelial cell dysfunction and demise (apoptosis), allowing for endothelial cell erosion and loss of endothelial cell stability upon its BM increasing the possibility of plaque erosion – rupture and thrombosis.