Se. Mau et H. Vilhardt, TRANSLOCATION OF PROTEIN-KINASE-C ISOZYMES IN RAT PITUITARY LACTOTROPH-ENRICHED CELL-CULTURES BY SUBSTANCE-P - EFFECTS OF SEX AND AGE, Journal of receptor and signal transduction research, 15(6), 1995, pp. 801-809
It is generally accepted that the phospholipid and calcium-dependent e
nzyme protein kinase C (PKC) plays a significant role in secretion of
hormones from anterior pituitary cells. The present study was undertak
en to study age and sex-related changes in 1, levels of immunoreactivi
ty of PKC isozymes and,distribution of immunoreactivity of PKC isozyme
s after stimulation with substance beta (SP) in rat lactotroph-enriche
d cell cultures. The alpha, beta, delta and zeta isozymes were present
in both sexes and at all ages. There was a sex-specific differential
regulation of the different PKC isozymes as a function of sexual matur
ation. In male rats there was an up-regulation of the alpha isozyme th
roughout the sexual development, while the beta subtype showed a small
, but significant decrease in immunoreactivity with increasing age. In
female rats, on the other hand, the beta species was up-regulated wit
h increasing age while the other subtypes remained constant. The conce
ntration of the delta and zeta isozymes was unaffected of sex and age.
Stimulation of lactotroph-enriched cell cultures with substance P (SP
) resulted in translocation of the alpha and beta isozymes from the so
luble to the particulate fraction while the delta and zeta species wer
e left unchanged independently of age and sex. However, a decrease in
responsiveness was observed in adult male rats, although a significant
degree of translocation of alpha and beta species was still detected.
On the basis of these results it is suggested that in lactotroph-enri
ched cell cultures basal levels of PKC subtype immunoreactivity and di
stribution of immunoreactivity of PKC isozymes after SP challenge migh
t be regulated as a function of sex and age.