W. Ge et Re. Peter, ACTIVIN-LIKE PEPTIDES IN SOMATOTROPHS AND ACTIVIN STIMULATION OF GROWTH-HORMONE RELEASE IN GOLDFISH, General and comparative endocrinology, 95(2), 1994, pp. 213-221
Activin and inhibin, dimeric protein hormones originally isolated from
mammalian gonads, are involved in the regulation of pituitary gonadot
ropin secretion. Using domain-specific antibodies against activin and
inhibin alpha, beta A, and beta B subunits, the present study demonstr
ates that immunoreactive activin and inhibin subunits, especially beta
A, exist in goldfish pituitary. Immunocytochemical staining with anti
-gonadotropin-II and anti-growth hormone showed that the pituitary cel
ls containing immunoreactive activin beta subunits are somatotrophs. T
his is different from the situation in mammals where it is the gonadot
rophs that produce activin molecules within the pituitary. The stainin
g with anti-beta B was overall weak compared to that with anti-beta A,
but both appear to localize in the same cells. Strong immunostaining
with the anti-inhibin alpha subunit was also observed in the goldfish
pituitary; however, the immunoreactivity is dissociated from those of
beta A and beta B, and mainly associated with nerve fibers in the neur
ointermediate lobe. Based on this evidence, it is suggested that the g
oldfish pituitary predominantly produced activin-like molecules. Both
porcine activin and inhibin stimulate growth hormone release from peri
fused goldfish pituitary fragments. Taken together with our previous f
indings that porcine activin stimulates gonadotropin-II release in gol
dfish, and the fact that the somatotrophs and gonadotrophs are in clos
e contact with each other in the goldfish pituitary, it is hypothesize
d that somatotroph-derived activin may exert paracrine actions on the
adjacent gonadotrophs to stimulate gonadotropin release and autocrine
actions on somatotrophs to stimulate growth hormone secretion. This al
so provides a mechanism for communication between these two pituitary
Cell types. (C) 1994 Academic Press, Inc.