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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
European Journal of Immunology 1988, Vol.18, No. 5, May
1998, pp. 755-760 - ISSN 0014-2980
469 KA |
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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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