Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0020538 (hypertension)
 170,190 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have isolated a cardiac natriuretic peptide of 5,000 d from atrial tissues from 500 rats and determined its amino acid sequence. The 5,000 d atrial natriuretic factor was elucidated to be a 45 amino acid peptide with the sequence of S-Q-D-S-A-F-R-I-Q-E-R-L-R-N-S-K-M- A-H-S-S-S-C-F-G-Q-K-I-D-R-I-G-A-V-S-R-L-G-C-D-G-L-R-L-F by sequencing the native peptide and its lysyl endopeptidase digests. The sequence of this peptide was identical to the amino acid sequence (51-95) of the rat brain natriuretic peptide precursor deduced from the complementary DNA (cDNA) sequence. The cardiac natriuretic peptide with a molecular weight of 5,000, or rat brain natriuretic peptide, was identified as the major storage form and as the sole secretory form derived from the brain natriuretic peptide precursor in the rat heart. The rat brain natriuretic peptide level in the atrium was 3.68 +/- 0.61 micrograms/g, which represents about 4% of that of atrial natriuretic factor. Rat brain natriuretic peptide was also detected in the ventricle. The ratio of brain natriuretic peptide to atrial natriuretic peptide in the ventricle was approximately 30% and much higher than that in the atrium. Rat brain natriuretic peptide, however, was not detectable in the brain. We conclude that the 5,000 d cardiac natriuretic peptide is rat brain natriuretic peptide with 45 amino acids derived from the brain natriuretic peptide precursor and is secreted from the rat heart as a novel cardiac hormone.
Hypertension 1990 Jun
PMID:Rat brain natriuretic peptide. Isolation from rat heart and tissue distribution. 235 30

Two-kidney, one clip Goldblatt hypertension of 2, 4 and 8 weeks duration was induced in 100-g male Wistar-Kyoto rats. Nucleic acid content was determined in the isolated cardiac muscle cells from the left ventricle. The profile for several major proteolytic activities in either isolated cardiac muscle cells or left ventricle preparations was also studied, using [3H]acetyl-casein as substrate. From the soluble fraction of the tissue or cell preparation, a pH 6 proteolytic activity, two forms of calcium-activated protease as well as cathepsin D were identifiable by inhibitor assay or DEAE-cellulose chromatography. From the myofibrillar fraction of the same preparation, two kinds of proteolytic activity were detected at alkaline pH: a phenylmethylsulfonyl fluoride (PMSF) inhibitable activity that was serine protease-like and the other a N-ethylmaleimide (NEM) inhibitable activity that resembled Ca2+-activated protease. At 2 weeks of hypertension, there was a significant increase in the pH 6 proteolytic activity as well as the calcium-activated protease I and the NEM-inhibitable alkaline protease activities, while the other identifiable proteolytic activities remained unchanged. Lysosomal cathepsin D showed a rise in activity only after 8 weeks of hypertension. These results may be related to the development of myocyte necrosis and lysis that occur in this model of hypertensive cardiomyopathy.
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PMID:Proteolytic activities in hypertensive cardiomyopathy of rats. 634 96