A Function Blocking Monoclonal Antibody Against alpha4 Laminin ( 99053CIP
Recently researchers at Northwestern University have developed a function blocking monoclonal antibody (mAb) to the a4 subunit of laminins. This antibody, mAb 2A3, inhibits angiogenesis and endothelialization in vitro and in vivo.
SCIENTIFIC BACKGROUND: Integrins are cellular receptors that mediate cell-cell and cell-extracellular matrix interactions, and integrin avß3 is postulated to play a major role in angiogenesis by acting as a receptor for a subunits and modulating a variety of cell-cell interactions. The a4 subunit is a ligand for the avß3 integrin, and the 2A3 antibody acts to block a4 subunit interactions with avß3
RESULTS: In vivo matrigel assays have demonstrated that the 2A3 antibody can inhibit angiogenesis. Experiments have demonstrated that the 2A3 antibody is able to inhibit in vitro wound healing of endothelial cells. Currently, an antibody to avß3 integrin (Vitaxin) is being evaluated in clinical trials. However, data obtained by our investigators indicate that the 2A3 antibody developed at Northwestern is more efficient than Vitaxin at blocking two essential aspects of angiogenesis: branching morphogenesis and migration of endothelial cells.
STAGE OF DEVELOPMENT: Northwestern is interested in licensing the technology for commercialization. Further non-confidential information is available upon request and further information regarding the 2A3 antibody can be found in the following published papers:
Gonzales, M. et al., Molecular Biology of the Cell 12: 85-100, January 2001 Gonzalez, AM et al., PNAS 99 (25): 16075-16080, December 10, 2002
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