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STRUCTURE OF HUMAN RENIN AND EXPRESSION OF THE RENIN GENE
Author(s) -
Morris Brian J.,
Catanzaro Daniel F.,
Hardman Judy,
Mesterovic Nikola,
Tellam Judy,
Hort Yvonne,
Bennetts Bruce H.,
Shine John
Publication year - 1984
Publication title -
clinical and experimental pharmacology and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.752
H-Index - 103
eISSN - 1440-1681
pISSN - 0305-1870
DOI - 10.1111/j.1440-1681.1984.tb00281.x
Subject(s) - renin–angiotensin system , gene , messenger rna , amino acid , exon , biology , recombinant dna , renin inhibitor , microbiology and biotechnology , protease , peptide sequence , kidney , gene expression , enzyme , biochemistry , endocrinology , blood pressure
SUMMARY 1. The amino acid sequence of human renin was identified for the first time. This was determined from the nucleotide sequence of exons in the human renin gene identified in a genomic library by recombinant DNA techniques. 2. Examination of amino acid residues involved in the enzymatic hydrolysis by human renin of the unique Leu 10 ‐Val 11 bond of human angiotensinogen revealed features peculiar to this highly specialized aspartyl protease. 3. The expression of the renin gene was examined with a hybridization probe for renin mRNA in sections and extracts of tissues. In the submandibular gland of mice renin mRNA, like renin, increased during development and in response to testosterone in females; sodium depletion increased renin mRNA in kidney.