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J Biol Chem, Vol. 274, Issue 38, 27056-27068, September 17, 1999
§ and
From the A novel testicular protein designated
sertolin was cloned. The full-length sertolin cDNA consists of 853 base pairs with an open reading frame of 381 base pairs coding for a
127-amino acid polypeptide that shares limited identities with
antaxin/josephin and thrombospondin proteins. Sertolin (calculated
molecular mass, 13,759 daltons) has two mRNA transcripts of 2.3 and
1 kilobase. A 22-amino acid peptide based on the deduced amino acid
sequence of sertolin (NH2-KKEHFNLFKAASVSHLVQVVPQ) was
synthesized and used for polyclonal antibody production. Immunoblot
analysis detected a 17-kDa immunoreactive band in the Sertoli cell
cytosol. Using Sertoli-germ cell cocultures, sertolin expression was
found to be reduced by as much as 5-fold at the time when germ cells
attach onto Sertoli cells but preceding the establishment of
specialized inter-Sertoli-germ cell junctions. Neither FSH nor
17
Population Council, Center for Biomedical
Research, New York, New York 10021 and the § Department
of Zoology, University of Hong Kong,
Hong Kong, People's Republic of China
-hydroxy-5
-androstan-3-one was able to affect sertolin
expression, whereas estradiol-17
and progesterone induced a
significant increase in Sertoli cell sertolin expression in
vitro. In addition, interleukin-1
, a germ cell-derived
cytokine, was also able to elicit a transient but significant increase
in Sertoli cell sertolin expression. Sertolin expression was also shown
to increase with testicular development and is likely to be associated
with the onset of spermatogenesis. In addition, sertolin expression
increased in the testis when generalized inflammation was induced in
adult rats by injection of fermented yeast. These results show that
sertolin will be useful in characterizing cell-cell interactions in the testis.
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