Two functional domains in the phagocyte membrane glycoprotein Mo1 identified with monoclonal antibodies.

摘要: Granulocytes from patients genetically deficient in the leukocyte glycoprotein family, Mo1, LFA-1, and Leu-M5 (P150,94), have defective complement receptor type III (CR3) activity as well abnormal adhesion-dependent functions such spreading, chemotaxis, phagocytosis. To determine contribution of Mo1 heterodimer deficiency to various functional aberrations observed granulocytes, we mapped domains using several monoclonal antibodies this molecule. In addition iC3b binding, two granulocyte adhesion were examined: Cell spreading on plastic coverslips chemotaxis. One antibody 44, inhibits all three functions. Other (903, Leu-15, OKM10) inhibit binding granulocytes but no effect cell and/or Another antibody, 904, has significant inhibition These studies suggest presence Mo1: one involved other enhancing certain