C. Mckinnell et Rm. Sharpe, REGULATION OF THE SECRETION AND SYNTHESIS OF RAT SERTOLI-CELL SGP-1, SGP-2 AND CP-2 BY ELONGATE SPERMATIDS, International journal of andrology, 20(3), 1997, pp. 171-179
The aim of this study was to investigate the effect of the absence of
elongate spermatids (ES) from the rat seminiferous epithelium on the q
uantitative secretion and synthesis of the three major Sertoli cell se
cretory proteins - SGP-1, SGP-2 and CP-2. Seminiferous tubules (ST) we
re isolated (a) from normal 28-day-old rats, in which the most mature
germ cell type is the round spermatid, (b) from normal adult rats at s
tages IX-XIV of the spermatogenic cycle, i.e. after spermiation, or at
stages I-V and VI-VIII, when ES are still attached to the Sertoli cel
l, and (c) at stages VI-VIII from normal adult rats and from rats trea
ted with methoxyacetic acid (MAA) in order to specifically deplete ES
at these stages. Two-dimensional SDS PAGE combined with computerized i
mage analysis was used to analyse S-35-methionine-labelled intracellul
ar and secreted proteins. In the case of SGP-1 and SGP-2, almost all o
f the protein synthesized by ST was secreted. The total amount of both
SGP-1 and CP-2 secreted by unstaged ST from immature rats was signifi
cantly lower than that secreted by unstaged ST from adult rats. The to
tal amount of SGP-1 and CP-2 secreted by-adult ST at stages IX-XIV of
the spermatogenic cycle also declined dramatically compared to ST at e
arlier stages. The proportion of the total CP-2 synthesized by ST whic
h was secreted also declined in all situations in which ES were absent
from the seminiferous epithelium. The synthesis of only SGP-2 was cha
nged by ES depletion from ST at stages VI-VIII, which was almost doubl
ed compared to synthesis of this protein by ST from control rats. Our
results suggest strongly that the secretion of SGP-1 and SGP-2 is via
the constitutive pathway, and that regulation of these two proteins by
ES is at the level of protein synthesis. In contrast, the regulation
of CP-2 by ES is predominantly at the level of secretion, suggesting t
hat this protein is secreted via a regulated pathway. Our findings add
to the evidence showing that ES play a major role in the regulation o
f Sertoli cell function.