Molecular cloning of a mouse submaxillary gland renin cDNA fragment.

Rougeon, François; Chambraud, Béatrice; Foote, Simon J.; Panthier, Jean‐Jacques; Nageotte, Roland; Corvol, Pierre

doi:10.1073/pnas.78.10.6367

Cited by 63 publications

(17 citation statements)

References 31 publications

(28 reference statements)

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“…In this system, @NGF, yNGF and renin precursors displayed M, values of about 26000, 31000 and 45000, respectively ( fig.3,4, slots 5). This latter value agrees with published data [12,20]. Slot 1, peptides synthesized in microinjected oocytes; slot 2, peptides secreted by the oocytes; slot 3, peptides synthesized in tunicamycintreated oocytes; slot 4, peptides secreted by tunicamycintreated oocytes; slot 5, translation products synthesized in a reticulocyte lysate.…”

Section: Identification Of the Precursors Of Cungf Yngf And Reninsupporting

confidence: 91%

Synthesis and partial maturation of the α‐ and γ‐subunits of the mouse submaxillary gland nerve growth factor in Xenopus laevis oocytes

1984

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Sera raised against the cy-, @-and y-subunits of the mouse 7 S NGF were used to characterize translation products coded by submaxillary gland mRNAs m~~ro~nje~ed into Xenctpus oocytes. Anti-@NGF sera did not cross-react with any material. In contrast, the precursors of the cy-and y-subunits, as well as that of renin were identified. Use of tunicamycin, and a comparison of the translation products obtained in oocytes or in the reticulocyte lysate indicated that oocytes achieved the cleavage of signal sequences, the glycosylation of the (Y-and y-precursors, and the subsequent secretion of the 3 proteins. In the submaxillary gland, however, the mature forms of CCNGF, yNGF and renin are composed of peptides of smaller size than those produced by the oocytes. These latter appear to lack specific proteases invoked in the terminal processing of the submaxillary gland proteins.

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Section: Identification Of the Precursors Of Cungf Yngf And Reninsupporting

confidence: 91%

Synthesis and partial maturation of the α‐ and γ‐subunits of the mouse submaxillary gland nerve growth factor in Xenopus laevis oocytes

1984

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“…This molecular weight is slightly lower than that determined from the electrophoretic mobility of the in vitro translation product (Mr 19,000). Such a discrepancy between the molecular weight predicted from sequence analysis and that determined from electrophoretic mobility has been described for other proteins of the SMG of rats (18) or mice (6,19). …”

Section: Iolation and Sequence Of A Cdna Complementary To A Ratmentioning

confidence: 95%

“…But surprisingly, these proteins are not detected in the SMG of related species. For instance, renin, which represents 2% of the SMG proteins in wild-type and most inbred male mice (6) is not found in the SMG of rats (7). This suggests that these SMG-synthesized polypeptides could be related to the especially aggressive behavior of male mice.…”

mentioning

confidence: 96%

High level of accumulation of a mRNA coding for a precursor-like protein in the submaxillary gland of male rats.

Rosinski‐Chupin

Tronik

Rougeon

1988

Proc. Natl. Acad. Sci. U.S.A.

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NaDodSO4/PAGE analysis of in vitro translation products of rat submaxillary gland (SMG) mRNAs has revealed an important sexual dimorphism. Moreover, most of the rat male-specific major translation products differ in size from those translated from male mouse SMG mRNAs. To characterize proteins accumulated in the rat SMG under androgen control, a cDNA library was constructed. Here we report the nucleotide sequence of a 0.7-kilobase mRNA that is 1000-3000 times more abundant in male rats than in female rats. The predicted corresponding protein, SMR1, has a molecular weight of 16,000 and contains a signal peptide for secretion and potential signals for glycosylation. An interesting feature of SMR1 is the presence, in a hydrophilic region, of the tetrapeptide Gln-His-Asn-Pro surrounded by two pairs of basic residues that represent potential cleavage sites for maturation enzymes. In rats, the tissue distribution of the SMR1 mRNA is restricted to the SMG and the prostate. Only very low amounts of SMR1 mRNA can be detected in the SMG of male or female mice. Southern blot analysis indicates the presence of three genes in rats but only one in mice. Hypotheses on the physiological role of SMR1-derived peptides in male rats are discussed.A large number of polypeptides with biologically defined properties are synthesized at high levels in the submaxillary gland (SMG) of rodents (1) and particularly of mice. These proteins, including nerve growth factor (NGF), epidermal growth factor (EGF), and renin, share a number of properties. All are synthesized in the same cell type-the granular convoluted tubular (GCT) cells-in response to various hormonal stimuli, in particular to androgens (2). Further, these secretory proteins can be found in the saliva of mice and are synthesized as precursors that become active after posttranslational processing events, possibly involving kallikrein-like proteinases. Some of these kallikrein-like proteinases are also synthesized under androgen-control in the SMG (3).The biological significance of the accumulation of these polypeptides in the SMG of mice and of their release into the saliva is still unclear. Aggressive behavior in male mice results in the release into the blood of large amounts of submaxillary NGF and renin (4,5), providing some evidence that these molecules play a physiological role. But surprisingly, these proteins are not detected in the SMG of related species. For instance, renin, which represents 2% of the SMG proteins in wild-type and most inbred male mice (6) is not found in the SMG of rats (7). This suggests that these SMG-synthesized polypeptides could be related to the especially aggressive behavior of male mice.Attempts to characterize the genes regulated by androgens in the SMG of rats led us to analyze the patterns of in vitro translation products directed by the mRNAs of this tissue. As in mice, an important sexual dimorphism was observed in the rat SMG translation products. Moreover, the major polypeptides accumulated in the two species appeared to be very ...

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“…CLONING AND STRUCTURAL ANALYSIS OF THE HUMAN RENIN GENE To obtain human renin gene sequences, we earlier cloned the human renin chromosomal gene [10], using a mouse cDNA probe [27], and later cloned a human renin cDNA [28]. The chromosomal gene was sequenced in the 5'-and 3'-flanking DNA, the exons, and portions of the introns.…”

Section: Introductionmentioning

confidence: 99%

Molecular Biology of Human Renin and Its Gene

Baxter

Duncan

Chu

et al. 1991

Proceedings of the 1990 Laurentian Hormone Conference

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Molecular cloning of a mouse submaxillary gland renin cDNA fragment.

Abstract: The mRNA encoding mouse renin has been partially purified from total poly(A)-containing RNA of submaxillary glands of male Swiss mice. Corresponding cDNAs were cloned in

Cited by 63 publications

References 31 publications

Synthesis and partial maturation of the α‐ and γ‐subunits of the mouse submaxillary gland nerve growth factor in Xenopus laevis oocytes

Synthesis and partial maturation of the α‐ and γ‐subunits of the mouse submaxillary gland nerve growth factor in Xenopus laevis oocytes

High level of accumulation of a mRNA coding for a precursor-like protein in the submaxillary gland of male rats.

Molecular Biology of Human Renin and Its Gene

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