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J Biol Chem, Vol. 273, Issue 33, 21040-21053, August 14, 1998
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§,
,
, and
From the Testin is a testosterone-responsive Sertoli cell
secretory product. In the present study, we demonstrated that the
amount of testin secreted by Sertoli cells in vitro was
comparable with several other Sertoli cell secretory products. However,
virtually no testin was found in the luminal fluid and cytosols of the
testis and epididymis when the intercellular junctions were not
previously disrupted, suggesting that secreted testin may be reabsorbed
by testicular cells in vivo. Studies using Sertoli cells
with and without a cell surface cross-linker and radioiodination in
conjunction with immunoprecipitation illustrated the presence of two
polypeptides of 28 and 45 kDa, which constitute a binding protein
complex that anchors testin onto the cell surface. The 28- and 45-kDa
peptide appear to be residing on and inside the cell surface,
respectively. Immunogold EM studies illustrated testin was abundantly
localized on the Sertoli cell side of the ectoplasmic specialization (a modified adherens junction) surrounding developing spermatids. In
contrast, very few testin gold particles were found at the site of
inter-Sertoli tight junctions. When the inter-Sertoli tight junctions
were formed or disrupted, no significant change in testin expression
was noted. This is in sharp contrast to the disruption of Sertoli-germ
cell junctions, which is accompanied by a surge in testin expression.
These results demonstrate the usefulness of testin in examining
Sertoli-germ cell interactions.
The Population Council, New York, New York
10021 and § Department of Zoology, University of Hong Kong,
Hong Kong, People's Republic of China
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