S. Tawfic et al., ANDROGENIC REGULATION OF THE EXPRESSION AND PHOSPHORYLATION OF PROSTATIC NUCLEOLAR PROTEIN-B23, Cellular & molecular biology research, 39(1), 1993, pp. 43-51
Protein B23 is a nucleolar and nuclear matrix phosphoprotein which has
been implicated in ribosomal assembly and/or rRNA processing. Since a
ndrogen action in the prostate is accompanied by early changes in rRNA
synthesis, we have investigated androgenic regulation of protein B23
expression and phosphorylation in rat ventral prostatic nuclei. The mR
NA for prostatic protein B23 was relatively stable and decreased only
after several days of androgen deprivation. However, androgen deprivat
ion resulted in a rapid change in the amount and phosphorylation of pr
otein B23 in prostatic nuclei, which was reversed on administration of
androgens to orchiectomized animals. Phosphorylation of protein B23 a
ppears to be catalyzed primarily by casein kinase 2 (CK-2). Early andr
ogenic changes in phosphorylation of protein B23 appear to relate more
to modulations in the protein kinase activity than in the amount of p
rotein B23. The androgen mediated enhancement in the amount of protein
B23 and its phosphorylation precedes the cellular proliferative phase
following androgen administration to castrated rats, and appear to be
temporally concordant with the rRNA synthesis in the tissue. The andr
ogen mediated changes in the amount and phosphorylation of protein B23
are specific to the prostate and are not detected in the liver nuclei
. Thus, androgenic regulation of the amount and phosphorylation of pro
static protein B23 may be related to the early changes associated with
androgen mediated growth of the gland.