Molecular forms of atrial natriuretic polypeptides in mammalian tissues and plasma
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Cited by (219)
Natriuretic peptides and neprilysin inhibition in hypertension and hypertensive organ damage
2020, PeptidesCitation Excerpt :This review summarizes the biological actions and pathophysiological roles of NPs, focusing on those related to BP regulation and/or hypertension, and discusses clinical implications of NPs and neprilysin inhibition in treating patients with hypertension and/or hypertensive organ damage. ANP is a cardiac hormone biosynthesized mostly by atrial myocytes and stored in specific granules as the precursor ANP(1–126), proANP [14,15]. Upon secretion, ANP-28, an active form of the peptide, is cleaved from the C-terminus of ANP(1–126) by the convertase enzyme corin (Fig. 1) [16].
Direct chemiluminescent enzyme immunoassay for atrial natriuretic peptide in mammalian plasma using a PEGylated antibody
2014, Analytical BiochemistryCitation Excerpt :Briefly, 100 μl each of sample, antibody, and tracer solutions of RIA buffer (50 mM sodium phosphate [pH 7.4] containing 80 mM NaCl, 25 mM EDTA, 0.05% NaN3, 0.5% BSA, and 0.5% Triton X-100) was mixed and incubated at 4 °C for 40 h. Free and bound 125I-labeled tracers were separated by the PEG precipitation method. Double antibody RIA was used to measure plasma ANP, as reported previously [21] with modifications. Briefly, a mixture of 100 μl each of sample and antibody solutions was preincubated at 4 °C overnight and then incubated with 100 μl of tracer solution of the RIA buffer containing dextran T-40 (final concentration = 1.0%) at 4 °C for 40 h. Normal rabbit serum and goat anti-rabbit IgG antiserum (Shibayagi, Gumma, Japan) diluted with RIA buffer were added to form the pellet for free/bound tracer separation.
Human coronary atherosclerosis modulates cardiac natriuretic peptide release
2009, AtherosclerosisCitation Excerpt :Yet in these patients, no further increase of NT-proANP was observed in response to cold pressor test. Cardiac natriuretic peptides – ANP and BNP are produced at the level of the atrial and ventricular myocardium, respectively [16–20]. In addition, gene expression of both ANP and BNP has been demonstrated in human explants of coronary arteries suggesting that they might also be locally released from the coronary arteries [5].
Isolation and identification of proangiotensin-12, a possible component of the renin-angiotensin system
2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :First, samples of rat small intestine were immediately boiled and acidified after resection in the extraction procedure. Non-specific cleavage of peptides can be avoided with this step which inactivates enzymes with proteolytic activity [20,21]. Second, the HPLC analysis of immunoreactive N-terminal Ang II (Fig. 1) showed three clear peaks, which correspond to Ang II, Ang I, and proangiotensin-12, without fragmentation of peptides.