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CD45 ligation induces programmed cell death in T and B lymphocytes.

S J Klaus, S P Sidorenko and E A Clark
J Immunol April 15, 1996, 156 (8) 2743-2753;
S J Klaus
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S P Sidorenko
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E A Clark
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Abstract

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.

  • Copyright © 1996 by American Association of Immunologists

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The Journal of Immunology
Vol. 156, Issue 8
15 Apr 1996
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CD45 ligation induces programmed cell death in T and B lymphocytes.
S J Klaus, S P Sidorenko, E A Clark
The Journal of Immunology April 15, 1996, 156 (8) 2743-2753;

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CD45 ligation induces programmed cell death in T and B lymphocytes.
S J Klaus, S P Sidorenko, E A Clark
The Journal of Immunology April 15, 1996, 156 (8) 2743-2753;
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Print ISSN 0022-1767        Online ISSN 1550-6606