Monoclonal antibody to an activation neoepitope of alpha M beta 2 inhibits multiple alpha M beta 2 functions.

摘要: alpha M beta 2, a 2 integrin expressed on cells of myelomonocytic differentiation, functions as receptor for factor X (X) and fibrinogen (Fg) participates in leukocyte adhesion to vascular endothelium. Acquisition high affinity ligand binding has been suggested result from conformational change response agonist-induced stimulation. We now describe mAb 7A10, which preferentially binds activated reports the functional activation this integrin. Agonist-stimulated monocytes monocytic cells, but not resting maximally 7A10 neoepitope, whereas expression other selected epitopes remained unchanged. The neoepitope was elicited equally by exposure either ADP or FMLP did require divalent cations expression. Saturation Ab stimulated THP-1 inhibited both Fg abolished 2-driven cellular coagulant response. Stimulated bound and/or Fg, exhibited sustained unstimulated endothelial cell monolayers adhesion. conclude that conformers mediate binding, assembly mediates endothelium through sparse ICAM-1, can report functionally inhibit pathway