The submaxillary gland of mouse contains a renin-like enzyme which represents as much as 5% of the total protein content. Its physico-chemical and enzymatic characteristics are similar to those of renal renin. Recently, the amino-acid sequence of the submaxillary pre-prorenin molecule has been deduced from the nucleotide sequence of the renin structural gene. A model for pre-prorenin processing into active renin has been proposed. Comparison of the structures of mouse submaxillary renin and of aspartyl proteases shows that renin belongs to this class of proteins and shares a similar catalytic site. Although the structure of renal renin is not yet known, preliminary studies suggest that the renal pro-enzyme is processed as the submaxillary enzyme. However, glycosylation would occur in the case of renal renin, whereas submaxillary renin is not glycosylated. Genetic studies and DNA hybridization experiments in mouse with high or low renin content in the submaxillary gland show that submaxillary renin in high renin producing strains results from a gene duplication. Submaxillary renin is therefore an isoenzyme and a useful model for the study of renal renin.
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Cell Physiol Biochem
August 2004
Renal Division, Department of Medicine, Universidade Federal de Sao Paulo, SP, Brasil.
It was analyzed the forms of renin produced by a mouse immortalized mesangial cell line (MIC) and their ability to generate angiotensin II (AII). The synthesis, localization and secretion of renin and AII by MIC were evaluated under conditions of normal (10 mM) or high (30 mM) glucose concentration. Two major bands of 35 kDa and 70 kDa were observed in SDS-PAGE.
View Article and Find Full Text PDFJ Am Soc Nephrol
June 2002
Division of Hypertension and Vascular Medicine, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland.
Several studies have demonstrated that mice are polymorphic for the number of renin genes, with some inbred strains harboring one gene (Ren-1(c)) and other strains containing two genes (Ren-1(d) and Ren-2). In this study, the effects of 1% salt and deoxycorticosterone acetate (DOCA)/salt were investigated in one- and two-renin gene mice, for elucidation of the role of renin in the modulation of BP, cardiac, and renal responses to salt and DOCA. The results demonstrated that, under baseline conditions, mice with two renin genes exhibited 10-fold higher plasma renin activity, 100-fold higher plasma renin concentrations, elevated BP (which was angiotensin II-dependent), and an increased cardiac weight index, compared with one-renin gene mice (all P < 0.
View Article and Find Full Text PDFAm J Physiol
May 1998
Franz Volhard Clinic, Berlin, Germany.
The (mRen2)27 transgenic rat [TGR(mRen2)27] is said to have low plasma levels of active renin. We used a direct radioimmunoassay (RIA) for mouse submaxillary renin, as well as an indirect enzyme-kinetic assay based on the generation of angiotensin I with modification of the pH optimum, to measure rat and mouse plasma renin activity (PRA), plasma renin concentration (PRC), and plasma prorenin in TGR before and after lisinopril. The relationship between rat PRC and % rat kidney extract was steepest at pH 6.
View Article and Find Full Text PDFJ Mol Biol
February 1994
Department of Crystallography, Birkbeck College, University of London, U.K.
The structure of mouse submaxillary renin complexed with a decapeptide inhibitor, CH-66 (Piv-His-Pro-Phe-His-Leu-OH-Leu-Tyr-Tyr-Ser-NH2), where Piv denotes a pivaloyl blocking group, and -OH- denotes a hydroxyethylene (-(S)CHOH-CH2-) transition state isostere as a scissile bond surrogate, has been refined to an agreement factor of 0.18 at 2.0 A resolution.
View Article and Find Full Text PDFC R Acad Sci III
November 1993
Unité de Géétique et Biochimie du Développement, Paris, France.
Inbred strains of mice, which produce high levels of submaxillary gland (SMG) renin have two renin genes, Ren 1 and Ren 2, per haploid genome, while strains with low levels of SMG renin have only the Ren 1 gene. Ren 1 codes for a glycosylated protein and Ren 2 codes for a highly homologous but unglycosylated and less thermostable protein. In order to determine if this difference in thermostability is related to the absence of glycosylation of renin-2 and/or to some amino acid difference between both renins we have compared the thermostability of renin-2 and a renin-2 mutant containing two potential N-glycosylation sites added by in vitro mutagenesis.
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