Immunomodulation by a2-macroglobulin and a2-macroglobulin-proteinase complexes: the effect
on the human T lymphocyte response
Heumann D., Vischer T.L.
Division of Rheumatology, Department of Medicine, Hopital Cantonal Universitaire, Geneva
Eur. J. Immunol. (1988):18, 755-760.
Alpha2-macroglobulin (a2M), various a2M-proteinase complexes and methylamine-treated a2M were added to human lymphocyte cultures stimulated with the specific antigen purified protein derivative of tuberculin (PPD), pokeweed mitogen (PWM) and anti-CD3. a2M-trypsin diminished all reactions in a dose-dependent way. In the PPD-induced stimulation of peripheral blood mononuclear cells, both change of configuration and remaining proteinase activity contributed to the suppressive activity. Separate exposure of adherent cells or the highly purified T lymphocytes to a2M-trypsin complexes indicated that the effect was mediated through adherent cells. Addition of indomethacin did not modify the results. In the interleukin 2 (IL 2)-dependent stimulation of purified T lymphocytes by anti-CD3 the effect of a2M-proteinase complexes was probably due to the digestion of IL2 through remaining proteinase activity. As a2M-proteinase complexes are formed at sites of inflammation, the multiple immunomodulatory effects of a2M-proteinase complexes might contribute to the dysregulation of the immune system in inflammatory diseases.
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