Kidney and submaxillary gland renins are encoded by two non-allelic genes in Swiss mice.

Panthier, Jean‐Jacques; Rougeon, F

doi:10.1002/j.1460-2075.1983.tb01483.x

Cited by 36 publications

(14 citation statements)

References 23 publications

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“…This result appears to be corroborated by Panthier and coworkers, 30 who have recently reported a 76 bp kidney renin cDNA sequence from two-gene Swiss mice which agrees with a different portion of the Ren-1 exon. 2 Of the 319 residues in our kidney cDNA clone, nine differ from the sequence reported for mouse SMG renin 28 (see Results).…”

Section: Discussionsupporting

confidence: 79%

Tissue and gene specificity of mouse renin expression.

Field¹,

McGowan²,

Dickinson³

et al. 1984

Hypertension

130

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The Ren-1 locus of mice encodes the protease renin, which with converting enzyme processes angiotensinogen to the potent vasopressor angiotensin II. Some strains of mice appear to carry a duplication of the renin structural gene (Ren-2) near the Ren-1 locus. Strains with the gene duplication can exhibit as much as 100-fold higher levels of submaxillary gland renin compared to strains with a single gene copy. In contrast, kidney renin levels appear to be unaffected by the gene duplication. Sequence analysis of a 319 bp renin cDNA recombinant isolated from a kidney library from the two-gene strain DBA/2Ha corresponds to a transcript of the Ren-1 gene. Moreover, a single base substitution of A for G at residue #996 in the kidney renin mRNA creates a potential glycosylation recognition site that may, in part, account for the differential glycosylation of kidney and submaxillary gland renins. In addition, our tissue surveys indicate that mature mRNAs from the Ren loci are detectable in adrenal gland and testes, as well as sublingual and parotid salivary glands, and reveal length variation for the renin transcripts in at least the submaxillary gland.

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Section: Discussionsupporting

confidence: 79%

Tissue and gene specificity of mouse renin expression.

Field¹,

McGowan²,

Dickinson³

et al. 1984

Hypertension

130

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“…The glycosylated thermostable kidney renin is encoded by the Ren 1 gene present in all mouse subspecies while the unglycosylated thermolabile SMG renin of high producer strains is encoded by a second copy of the gene, Ren 2 (Inagami et al, 1980; Wilson and Taylor, 1982;Panthier et al, 1982b;Mullins et al, 1982;Piccini et al, 1982;Panthier and Rougeon, 1983 (Ollo et al, 1981). Independent overlapping clones containing the renin gene Ren 1 were identified.…”

Section: Introductionmentioning

confidence: 99%

Evolution of aspartyl proteases by gene duplication: the mouse renin gene is organized in two homologous clusters of four exons.

Holm¹,

Ollo²,

Panthier³

et al. 1984

The EMBO Journal

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Overlapping recombinant clones that appear to encompass the entire renin gene, named Ren 1, have been isolated from a library of BALB/c mouse genomic DNA fragments. Based on restriction endonuclease mapping and DNA sequence analysis, Ren 1 spans 9.6 kb and contains nine exons interrupted by eight intervening sequences of highly variable size. The first exon, encoding the signal peptide of preprorenin, is separated from the eight following exons by a 3-kb intron. These eight exons are organized into two clusters of four separated by a 2-kb intron. DNA stretches encoding the aspartyl residues, which are part of the active site of renin, are located at homologous positions in both clusters. Our results show that aspartyl protease genes have arisen by duplication and fusion of an ancestral gene containing five exons. The estimated date of the duplication event of the mouse renin genes Ren 1 and Ren 2 is discussed.Key words: kidney renin/protein glycosylation/rate of divergence/exon-intron boundaries Introduction Aspartyl protease represents one of the protein families most completely characterized by primary amino acid sequence and crystallographic studies. The aspartyl proteases active site contains two aspartate residues localized in two short amino acid stretches with sequence homology to one another, and separated by a distance of about half of the polypeptide chain (Sepulveda et al., 1975). Aspartyl proteases such as penicellopepsin have a bilobal structure in which the two lobes are related by a 2-fold symmetry axis (Hsu et al., 1977). These observations have led to a hypothesis that aspartyl protease genes have evolved by duplication and fusion of an ancestral gene coding for a 15 000 -20 000 dalton polypeptide having a fold similar to that of one lobe of pepsin (Tang et al., 1978).In contrast to the other aspartyl proteases, renin has an optimal activity at neutral pH and a substrate specificity restricted to the cleavage of the prohormone angiotensinogen. The primary source of renin is the kidney where its concentration is extremely low. However, in some mouse strains, high levels of renin activity are found in the submaxillary gland (SMG) of males (Wilson et al., 1977). The amino acid sequence of the SMG renin has been recently reported (Panthier et al., 1982a;Misono et al., 1982). Comparison of the amino acid sequence of renin and pepsin shows -420Wo homology. The two most homologous regions are those surrounding the active sites aspartates. These results strongly suggest that renin and pepsin genes derive from a common ancestor.

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“…Mouse strains vary in renin gene copy number (3,4); CBA/Ca contains the single ancestral gene Ren-1 c , whereas 129/Sv contains Ren-1 d and Ren-2, which are 97% homologous at the nucleotide level and are located 20 kb apart (5,6). The three renin genes are differentially expressed in a range of tissues such as the submandibular gland (where Ren-2 is highly expressed in the male) (7,8).…”

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confidence: 99%