Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.23.15 (renin)
 35,795 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recent studies employing molecular biological techniques demonstrate that renin and angiotensinogen genes are expressed in various tissues. We have observed tissue-specific regulation of renin and angiotensinogen gene expressions. Renin expression in kidney, heart, and adrenal are stimulated by sodium depletion and beta-adrenergic agonist. Submandibular gland and genital renins are not. Instead, the renin expression in these tissues are influenced by androgen and/or hormones that are activated during ontogeny. Genetic influence of tissue renin expression also exists, i.e., the submandibular gland, cardiac, and testicular renin activities are higher in the two gene strains, whereas kidney renin activity does not differ between different strains. Tissue-specific regulation of angiotensinogen mRNA is also observed when rats are placed on a low-sodium diet. Sodium depletion stimulates renin angiotensinogen mRNA expression but does not influence hepatic angiotensinogen mRNA levels. Tissue-specific regulation of renin angiotensin may have important functional implications. Increased local production of angiotensin should influence tissue angiotensin-mediated responses that may be independent of the circulating system.
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PMID:Regulation of tissue renin and angiotensin gene expressions. 243 84

1. The existence of a biosynthetic precursor of renin (prorenin) has been inferred, but never established experimentally. The aim of the present study was to provide this evidence. 2. In a continuous labelling experiment using submandibular glands of male Quackenbush mice (an extraordinarily rich source of renin) a molecule of Mr 44 500 was immunoprecipitated with antiserum to renin. 3. The Mr 44 500 protein was converted to Mr 40 000 renin in a time-dependent fashion during incubation of tissue at 37 degrees C: 15 min after addition of [35S] methionine only 16% of immunoprecipitable radioactivity was renin, whereas by 4 h this had increased to 86%. The Mr 44 500 protein would therefore appear to be a 'pro' form of renin. 4. Submandibular gland mRNA was translated in a cell-free system derived from rabbit reticulocyte lysate and a molecule of Mr 46 000 was immunoprecipitated with antirenin. This was preprorenin and the Mr of the 'pre' region would thus be 1500, which is consistent with the size generally found for the 'pre' region of secretory proteins. 5. The present study has therefore demonstrated for the first time the biosynthesis of a 'pro' form of renin (prorenin) and its conversion to renin intracellularly.
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PMID:Biosynthesis of preprorenin and intracellular conversion of prorenin to renin. 703 36