S. Tawfic et al., ANDROGENIC REGULATION OF PHOSPHORYLATION AND STABILITY OD NUCLEOLAR PROTEIN NUCLEOLIN IN RAT VENTRAL PROSTATE, The Prostate, 24(2), 1994, pp. 101-106
Nucleolin is an abundant nucleolar phosphoprotein which has been impli
cated as a factor in various stages of ribosome synthesis, including t
ranscription. Since androgens exert a profound effect on the rRNA synt
hesis in the target organ prostate, we have examined the nature of and
rogenic regulation of the amount and phosphorylation of nucleolin in t
his tissue. Phosphorylation of prostatic nucleolin is catalyzed in par
t by heparin-sensitive casein kinase 2 (CK-2) and by another (heparin-
insensitive) protein kinase. Both the amount and phosphorylation of pr
ostatic nucleolin are profoundly sensitive to androgens. Rapid reducti
on in the level and phosphorylation of nucleolin occurs following andr
ogen deprivation, which corresponds to the ensuing cessation of prosta
tic growth leading to involution. Further, the loss of nucleolin phosp
horylation and its degradation appear to be concordant. Administration
of a single injection of 5 alpha-dihydrotestosterone to castrated ani
mals causes an early increase in the amount and phosphorylation of nuc
leolin, starting in the prereplicative phase in the prostatic cell nuc
leus. These data suggest that early androgenic regulation of nucleolin
expression and phosphorylation may play a role in nucleolar control m
echanisms relevant to prostatic cell growth. (C) 1994 Wiley-Liss, Inc.