The β2 integrin Mac‐1 but not p150,95 associates with FcγRIIA

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Abstract
In this study we have compared the ligand binding activity of the two closely related β2 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 FcγR, particularly FcγRIII, but K562 cells express only endogenous FcγRIIA. We have, therefore, taken advantage of this situation to examine a possible relationship between FcγRIIA with Mac‐1 and p150,95 in the absence of other FcγR. The main finding is that anti‐FcγRII 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.

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