Integrins are important extracellular matrix (ECM) receptor proteins located on cell surfaces. They are hetrodimers composed of an alpha and a beta transmembrane glycoprotein subunit. Around 22 different integrins (different alpha/ beta subunit combinations) are found in nature. Integrins are generally present in high concentrations at the cell surface, but, unlike most other cell surface receptors, they bind ligands with very low affinity. Due to their weak individual binding, integrins need to cluster and bind in groups in order to effectively bind the ECM. Integrins bind many different ligands including laminin. Each integrin is made up of a large N terminal extracellular domain that binds the ECM ligand and a small C terminal cytoplasmic domain that mediates interaction with the actin cytoskeleton and signaling function. The integrin subunit beta 5 has only been associated with the alpha v subunit to form the alpha v beta 5 heterodimer. This integrin mediates cell adhesion to vitronectin and also recognizes fibronectin when the integrin is activated. This integrin is found in a variety of cells in most normal tissue.