Expression and function of AIM, an activation inducer molecule of human lymphocytes, is dependent on the activation of protein kinase C
- 1 May 1989
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 19 (5), 809-815
- https://doi.org/10.1002/eji.1830190505
Abstract
AIM is an activation inducer molecule selectively expressed by activated lymphocytes through which agonistic proliferative signals can be triggered. The relationship between the expression of AIM with the activation of protein kinase C (PKC) has been studied. Different activators of PKC such as the active phorbol esters, phorbol myristate acetate and phorbol dibutyrate, or the phorbol‐related ester mezerein were able to induce AIM expression on peripheral blood lymphocytes as assessed by immunofluorescence flow cytometry. Moreover, the expression of this activation antigen was also induced by treatment of peripheral blood lymphocytes either with dioctanoyl‐rac‐glycerol, a synthetic analogue of diacylglycerol, the physiological mediator of PKC activation. Further indirect evidence that AIM expression was dependent on the activation of PKC was obtained by blockade of the induction of its expression in cells treated with H7, an inhibitor of PKC. The AIM expression can be detected as early as 3 h after addition of phorbol esters and it requires active RNA and protein synthesis. The activation of PKC appears to be also required in the proliferative response induced by anti‐AIM monoclonal antibody (mAb) in conjunction with phorbol esters. Agents such as phorbol myristate acetate, phorbol dibutyrate or mezerein but not the inactive phorbol ester methyl‐phorbol myristate acetate induced a high proliferation of peripheral blood lymphocytes in the presence of anti‐AIM mAb. In addition, we have demonstrated that the anti‐AIM mAb is not sufficient by itself to induce cellular proliferation once the AIM antigen is expressed at the cell surface, requiring the simultaneous stimulation of the PKC to trigger high proliferative responses. Furthermore, the anti‐AIM mAb did not appear to exert its effect on proliferation by rapidly increasing the intracytoplasmic Ca2+ levels. Taken together all these results indicate that the expression and function of AIM antigen is dependent on the activation of PKC.This publication has 49 references indexed in Scilit:
- The same inducible nuclear proteins regulates mitogen activation of both the interleukin-2 receptor-alpha gene and type 1 HIVCell, 1988
- Purified transcription factor AP-1 interacts with TPA-inducible enhancer elementsCell, 1987
- Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factorCell, 1987
- Signal transduction and intracellular events in T-lymphocyte activationImmunology Today, 1986
- Protein kinase C activation by diacylglycerol second messengersCell, 1986
- Functional modifications of cytotoxic T-lymphocyte T200 glycoprotein recognized by monoclonal antibodiesNature, 1985
- Early steps of lymphocyte activation bypassed by synergy between calcium ionophores and phorbol esterNature, 1985
- Platelet-derived growth factor induces rapid but transient expression of the c-fos gene and proteinNature, 1984
- 1-(5-isoquinol inesulfonyl)-2-methylpiperazine (H-7) is a selective inhibitor of protein kinase c in rabbit plateletsBiochemical and Biophysical Research Communications, 1984
- Stimulation of 3T3 cells induces transcription of the c-fos proto-oncogeneNature, 1984