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Beschreibung

Integrin alpha-4 (UniProt: D3ZMQ3, also known as CD49d, Protein Itga4) is encoded by the Itga4 gene in rat. Integrin-Alpha 4 contains 7 GF-GAP repeats. Unlike other integrin alpha chains, alpha 4 neither contains an I-domain, nor undergoes disulfide-linked cleavage. It associates with either beta-1 or beta-7 to generate a heterodimer. The alpha subunit can sometimes be cleaved into two non-covalently associated fragments. Integrin alpha-4/beta-1 (alpha 4/CD29, VLA-4) may regulate leukocyte to endothelial cells adhesion by controlling Junctional adhesion molecules-L homodimerization. Integrins alpha-4/beta-1 and alpha-4/beta-7 are receptors for fibronectin and they recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-4/beta-1 plays a major role in the regulation of immune cell recruitment to inflamed endothelia and sites of inflammation. On activated endothelial cells integrin alpha-4/beta-1 triggers homotypic aggregation for most alpha-4/beta-1-positive leukocyte cell lines. This monoclonal antibody (clone TA-2) is shown to inhibit rat lymphocyte adhesion to stimulated HUVEC. It also blocks adhesion small peritoneal exudate lymphocytes (sPEL) adhesion to TNF-alpha and IL-1 stimulated human umbilical vein endothelial cells. (Ref.: Issekutz, TB., and Wykretowicz, A (1991). J. Immunol. 147:109-116).