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Vasoinhibin is Generated by the Renin-angiotensin System.
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Physiology, 2007
The aspartyl-protease renin is the key regulator of the renin-angiotensin-aldosterone system, which is critically involved in salt, volume, and blood pressure homeostasis of the body. Renin is mainly produced and released into circulation by the so-called juxtaglomerular epithelioid cells, located in the walls of renal afferent arterioles at the ...
Schweda, Frank +4 more
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The aspartyl-protease renin is the key regulator of the renin-angiotensin-aldosterone system, which is critically involved in salt, volume, and blood pressure homeostasis of the body. Renin is mainly produced and released into circulation by the so-called juxtaglomerular epithelioid cells, located in the walls of renal afferent arterioles at the ...
Schweda, Frank +4 more
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Renin Tachyphylaxis and ‘Renin Hypertension’ in the Rabbit
American Journal of Physiology-Legacy Content, 1956A ‘renin hypertension’ was produced by means of a constant intravenous infusion of a carefully quantitated renin solution. Renin injections were then superimposed to the point of tachyphylaxis. In all cases when tachyphylaxis was established, the blood pressure gradually returned to preinfusion levels.
David B. Gordon +2 more
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Renin, Prorenin, and the (Pro)Renin Receptor [PDF]
, 2009 The discovery of a receptor for renin and for its inactive precursor prorenin, and the introduction of renin inhibitors in therapeutic, has renewed the interest for the physiology of the renin angiotensin system (RAS) and has brought prorenin back in the spotlight.
Aurélie Contrepas, Genevieve Nguyen
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Is Angiotensinogen a Renin Inhibitor and Not the Substrate for Renin?
Journal of Hypertension, 1986The cleavage of the angiotensinogen molecule by renin is slow. The rate constant for cleavage of the enzyme-substrate complex, Kcat (turnover number) is lower than usual for enzymes (0.6/s for the homologous human renin reactions and 0.15/s for the homologous mouse renin reaction).
Knud Poulsen, Jørgen Jacobsen
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Inactive Renin — A Renin Proenzyme?
1977Human plasma contains an inactive form of renin with a m.w. of 55,000, as against around 40,000 for active human renin. After acidification to pH 3.0 or incubation with trypsin, the inactive renin becomes more active and the molecular weight falls to that of active renin.
A. McConnell, B. J. Leckie, J. Jordan
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Physiology of local renin-angiotensin systems.
Physiological Reviews, 2006Since the first identification of renin by Tigerstedt and Bergmann in 1898, the renin-angiotensin system (RAS) has been extensively studied. The current view of the system is characterized by an increased complexity, as evidenced by the discovery of new ...
M. Paul, Ali Poyan Mehr, R. Kreutz
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The Journal of Clinical Endocrinology & Metabolism, 1977
Renin activity, concentration, substrate and reactivity were determined in normal subjects as well as in hypertensive subjects with suppressed and normal plasma renin activity. Renin substrate measurements were similar in all groups. Renin reactivity, a measure of circulating modifiers of the renin reaction, was significantly increased in both ...
Edwin L. Cohen +2 more
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Renin activity, concentration, substrate and reactivity were determined in normal subjects as well as in hypertensive subjects with suppressed and normal plasma renin activity. Renin substrate measurements were similar in all groups. Renin reactivity, a measure of circulating modifiers of the renin reaction, was significantly increased in both ...
Edwin L. Cohen +2 more
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Biochemical Society Transactions, 1984
Biochemical features of renin have been studied. Determination of the amino acid sequence and catalytically essential groups in the active sites of mouse submandibular gland revealed the similarity of renin with acid proteases. Yet stringent substrate specificity, neutral pH optimum of its enzyme activity and the unique structure of the activation ...
Tadashi Inagami +3 more
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Biochemical features of renin have been studied. Determination of the amino acid sequence and catalytically essential groups in the active sites of mouse submandibular gland revealed the similarity of renin with acid proteases. Yet stringent substrate specificity, neutral pH optimum of its enzyme activity and the unique structure of the activation ...
Tadashi Inagami +3 more
openaire +3 more sources