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The Journal of Immunology, Vol 156, Issue 8 2743-2753, Copyright © 1996 by American Association of Immunologists

ARTICLES

CD45 ligation induces programmed cell death in T and B lymphocytes

SJ Klaus, SP Sidorenko and EA Clark
Department of Immunology, Regional Primate Research Center, University of Washington, Seattle 98195, USA.

Studies have shown an essential role for the CD45 protein tyrosine phosphatase in regulating Ag receptor-derived signals in lymphocytes. Co-ligating CD45 with the Ag receptor, however, can also inhibit receptor signaling, as manifest in T cells by the lack of IL-2 production and proliferation. We report that CD45 ligation alone induces apoptosis in normal T cells, and that death was greatly potentiated by cross-linking CD3. Normal B cells and T and B cell lines were also induced to die with insoluble CD45 mAb. CD45-induced cell death was blocked by inhibitors of protein tyrosine kinases and protein tyrosine phosphatases, but not by inhibitors of RNA or protein synthesis or by cyclosporin A. Morphologically, CD45-mediated apoptosis resembled death induced via CD95 (Fas), as evidenced by nuclear condensation and membrane blebbing, but did not cause DNA fragmentation into oligonucleosomes. Co-ligating CD45 and CD95 either enhanced or inhibited CD45-induced cell death, depending on the degree of CD45 and CD95 cross-linking. Finally, CD45 cross-linking induced its rapid association with the detergent-insoluble cell fraction, suggesting that it becomes linked to the cytoskeleton during CD45-induced apoptosis. These data show a novel role for CD45 in regulating lymphocyte death as well as proliferation.


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