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J. Biol. Chem., Vol. 262, Issue 17, 8288-8292, Jun, 1987
MM Compton and JA Cidlowski
Glucocorticoids initiate a cytolytic process in lymphoid cells that is
characteristic of programmed cell death. In vivo treatment of
adrenalectomized rats with glucocorticoids results in the rapid degradation
of the thymocyte genome at internucleosomal sites. This DNA degradation
occurs prior to cell death, and considerable evidence indicates that this
nucleolytic event is central to the initiation of lymphocytolysis. To
further characterize this process, we have searched for the gene products
in thymocytes which may be responsible for steroid-induced DNA degradation.
Adrenalectomized rats were treated in vivo with dexamethasone or a vehicle
control; nuclear thymocyte proteins were extracted with 0.6 M NaCl and
analyzed for protein content or nuclease activity on sodium dodecyl
sulfatepolyacrylamide gels containing calf thymus DNA. Glucocorticoid
treatment resulted in the induction of two major protein families, a
30-32-kDa protein doublet and a series of 3-4 proteins of 12-19 kDa, both
of which express prominent DNase activity. Induction of the lower molecular
weight nucleases increased with time after steroid treatment and paralleled
the time course of glucocorticoid-mediated DNA degradation. Nuclease
induction was blocked by the glucocorticoid antagonist RU 486, indicating a
steroid receptor-mediated process. When nuclei from
glucocorticoid-resistant cells were incubated with nuclear extracts from
glucocorticoid-treated rats, the DNA was cleaved at internucleosomal sites,
whereas extracts from vehicle-treated animals were virtually inactive.
Based on these findings we propose that glucocorticoids, acting via a
receptor-mediated pathway, induce a nucleolytic "lysis gene" product(s)
responsible for lymphocytolysis.
Identification of a glucocorticoid-induced nuclease in thymocytes. A potential "lysis gene" product
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