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J. Biol. Chem., Vol. 276, Issue 34, 31698-31708, August 24, 2001
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From the Division of Reproductive Biology, Department of Gynecology
and Obstetrics, Stanford University School of Medicine,
Stanford, California 94305-5317
In mammalian germ cells, cAMP signaling is
dependent on two forms of adenylyl cyclase, the conventional
membrane-bound ACIII and a soluble form of adenylyl cyclase (sAC).
Recent elucidation of the sAC sequence indicates that this enzyme is
phylogenetically distinct from the membrane-bound AC, does not interact
with G proteins, and its activity is regulated by bicarbonate ions.
Here we have investigated the properties and regulation of this enzyme during spermatogenesis. Two different transcripts encoding a
full-length and truncated sAC were identified by reverse
transcriptase-polymerase chain reaction and RNase protection analysis.
The truncated sAC transcript lacks exon 11 with a premature termination
of the open reading frame after the catalytic domain. Reverse
transcriptase-polymerase chain reaction with testis RNA from adult
mouse and rat of different ages, as well as RNase protection, showed
that both transcripts are absent at 11 days of age, appear between 20 and 30 days of age, and are retained in the adult testis. The presence
of corresponding proteins in testis, germ cells, and spermatozoa was
demonstrated by fast protein liquid chromatography and differential
immunoprecipitation with full-length sAC-specific antibodies.
Bicarbonate ions activated both sAC forms and increased cAMP levels in
germ cells isolated from 25- and 50-day-old rats and adult rats in a
concentration-dependent manner. These findings provide
evidence that full-length and truncated sAC are generated by alternate
splicing. Both forms are active in spermatids, and the bicarbonate
present in the seminiferous tubule may be a signal that regulates cAMP
levels in these cells.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF271058.
Identification and Functional Analysis of Splice Variants of the
Germ Cell Soluble Adenylyl Cyclase*
*
This work was supported by National Institutes of Health
Grant HD31544 (to M. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Division
of Reproductive Biology, Dept. of Gynecology and Obstetrics, Stanford University School of Medicine, 300 Pasteur Dr., Rm. A344, Stanford, CA
94305-5317. Tel.: 650-725-2452; Fax: 650-725-7102; E-mail: marco.conti@stanford.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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