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J. Biol. Chem., Vol. 264, Issue 23, 13399-13402, Aug, 1989
DJ McConkey, P Hartzell, M Jondal and S Orrenius
Glucocorticoid hormones and Ca2+ ionophores stimulate a suicide process in
immature thymocytes, known as apoptosis or programmed cell death, that
involves extensive DNA fragmentation. We have recently shown that a
sustained increase in cytosolic Ca2+ concentration stimulates DNA
fragmentation and cell killing in glucocorticoid- or ionophore-treated
thymocytes. However, a sustained increase in the cytosolic Ca2+ level also
mediates lymphocyte proliferation, suggesting that apoptosis is blocked in
proliferating thymocytes. In this study we report that phorbol esters,
which selectively stimulate protein kinase C (PKC), blocked DNA
fragmentation and cell death in thymocytes exposed to Ca2+ ionophore or
glucocorticoid hormone. The T cell mitogen, concanavalin A, which
stimulates thymocytes by a mechanism that involves PKC activation, caused
concentration-dependent increases in the cytosolic Ca2+ level that did not
result in DNA fragmentation, but incubation with concanavalin A and the PKC
inhibitor H-7 (1-(5- isoquinolinylsulfonyl)-2-methylpiperazine) resulted in
both DNA fragmentation and cell death. Phorbol ester directly inhibited
Ca2+- dependent DNA fragmentation in isolated thymocyte nuclei. Our results
strongly suggest that PKC activation blocks thymocyte apoptosis by
preventing Ca2+-stimulated endonuclease activation.
Inhibition of DNA fragmentation in thymocytes and isolated thymocyte nuclei by agents that stimulate protein kinase C
Department of Toxicology, Karolinska Institutet, Stockholm, Sweden.
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