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(Received for publication, April 19, 1996, and in revised form, October 30, 1996)
From The Population Council, New York, New York 10021
Testin, a Sertoli cell secretory protein whose
mRNA is predominantly expressed in the testis, was shown to become
tightly associated with Sertoli cell membrane upon its secretion whose solubilization requires the use of a detergent such as SDS. In the
in vitro studies using Sertoli cells cultured at high cell density, where specialized junctions were being formed, the
concentration of "soluble" testin in the spent media was greatly
reduced versus monolayer cultures at low cell density,
where specialized junctions were absent. Conversely, the concentration
of "membrane-bound" testin from detergent-solubilized Sertoli cell
membrane extract was positively correlated to the existence of
specialized junctions in these cultures. In normal rat testes, the
level of radioimmunoassayable soluble testin in the cytosol was low.
However, when the inter-testicular cell junctions were disrupted either
by a drug treatment such as lonidamine in vivo or by a
physical treatment in vitro such as exposing Sertoli-germ
cell co-cultures where specialized junctions were formed to a hypotonic
treatment, a drastic surge in the testin gene expression was noted.
Thus, testin can become tightly associated with Sertoli cell membrane
upon its secretion when intercellular junctions are formed. It is also
a marker to monitor the integrity of inter-testicular cell
junctions.
Volume 272, Number 10,
Issue of March 7, 1997
pp. 6499-6509
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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