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Volume 270,
Number 36,
Issue of September 08, pp. 21009-21015, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Role of Protein
Phosphorylation in Post-translational Regulation of Protein B23 during
Programmed Cell Death in the Prostate Gland
(Received for publication, March 15, 1995; and in revised form, June 21, 1995)
Sherif
Tawfic ,
Mark O. J.
Olson
, <WBR>
Khalil
Ahmed
Protein B23 is a nucleolar and nuclear matrix-associated
phosphoprotein that is involved in ribosome synthesis. Its expression
and phosphorylation in rat ventral prostate, an androgen target organ,
are profoundly influenced by androgens. Induction of programmed cell
death (apoptosis) in the prostatic epithelium by androgen deprivation
in the animal induces an early decline in protein B23 in the absence of
a corresponding loss of protein B23 mRNA. We have now demonstrated that
prostatic nuclei retain the ability to transcribe the B23 mRNA and that
a significant amount of this mRNA persists even after 7 days of
androgen deprivation when >80% of the prostatic epithelial cells
have undergone apoptosis. The B23 mRNA from these nuclei is also
translatable in vitro. However, the majority of the B23 mRNA
is associated with free and short-stretch polysomes, which may account
for the castration-induced decline in synthesis of protein B23 in
vivo. In addition, the mechanism of down-regulation of protein B23
in apoptotic prostatic cells appears to relate to two coordinate
signals, which include loss of phosphorylation of the protein as well
as the expression of a protease active toward dephosphorylated protein
B23, under these conditions.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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