The beta 2 integrin Mac-1 but not p150,95 associates with Fc gamma RIIA.

In this study we have compared the ligand binding activity of the two closely related beta 2 integrins, Mac-1 and p150,95, which are expressed separately as receptors permanently transfected into K562 cells. Mac-1 has previously been shown to associate with Fc gamma R, particularly Fc gamma RIII, but K562 cells express only endogenous Fc gamma RIIA. We have, therefore, taken advantage of this situation to examine a possible relationship between Fc gamma RIIA with Mac-1 and p150,95 in the absence of other Fc gamma R. The main finding is that anti-Fc gamma RII mAb have a profound inhibitory effect on cell adhesion mediated by Mac-1, but not on the adhesion mediated by p150,95. Thus, in spite of the fact that Mac-1 and p150,95 bind to the same or at least a very similar selection of ligands, their association with other receptors on the cellular membrane, and therefore their mode of regulation may be different.