scholarly journals Peptide Metabolism

2020 ◽  
Author(s):  
Keyword(s):  
Peptide Metabolism

Clearance receptors and endopeptidase: equal role in natriuretic peptide metabolism in heart failure

1997 ◽  
Vol 273 (5) ◽  
pp. H2372-H2379 ◽  
Author(s):  
Miriam Tessa Rademaker ◽  
Christopher John Charles ◽  
Teddy Kosoglou ◽  
Andrew A. Protter ◽  
Eric Arnold Espiner ◽  
...  
Keyword(s):  
Heart Failure ◽  
Natriuretic Peptide ◽  
Urine Volume ◽  
Peripheral Resistance ◽  
Plasma Aldosterone ◽  
Peptide Receptor ◽  
Therapeutic Value ◽  
Combined Administration ◽  
Peptide Metabolism ◽  
Dose Dependent

The effects of separate and combined endopeptidase inhibition (by SCH-32615) and natriuretic peptide receptor C blockade [by C-ANP-(4—23)] on the clearance and bioactivity of atrial (ANP) and brain (BNP) natriuretic peptides was investigated in eight sheep with heart failure. SCH-32615 and C-ANP-(4—23) administered separately induced significant and proportionate dose-dependent rises in plasma ANP, BNP, and guanosine 3′,5′-cyclic monophosphate (cGMP) levels. Associated with these changes were reductions in arterial pressure, left atrial pressure, and peripheral resistance and increases in cardiac output, urine volume, sodium excretion, and creatinine clearance. SCH-32615 induced greater diuresis and natriuresis than C-ANP-(4—23). Combined administration of SCH-32615 and C-ANP-(4—23) induced greater than additive rises in plasma ANP, BNP, and cGMP concentrations, with enhanced hemodynamic effects, diuresis, and natriuresis and reduced plasma aldosterone levels. In conclusion, we find that the enzymatic and receptor clearance pathways contribute equally to the metabolism of endogenous ANP and BNP in sheep with heart failure. Combined inhibition of both degradative pathways was associated with enhanced hormonal, hemodynamic, and renal effects and may have greater potential therapeutic value than either agent separately.

scholarly journals Key Role for Sulfur in Peptide Metabolism and in Regulation of Three Hydrogenases in the Hyperthermophilic ArchaeonPyrococcus furiosus

2001 ◽  
Vol 183 (2) ◽  
pp. 716-724 ◽  
Author(s):  
Michael W. W. Adams ◽  
James F. Holden ◽  
Angeli Lal Menon ◽  
Gerrit J. Schut ◽  
Amy M. Grunden ◽  
...  
Keyword(s):  
Growth Rates ◽  
Elemental Sulfur ◽  
Pyrococcus Furiosus ◽  
Growth Conditions ◽  
Growth Media ◽  
Hyperthermophilic Archaeon ◽  
Order Of Magnitude ◽  
Membrane Bound ◽  
Peptide Metabolism ◽  
Specific Activities

ABSTRACT The hyperthermophilic archaeon Pyrococcus furiosusgrows optimally at 100°C by the fermentation of peptides and carbohydrates. Growth of the organism was examined in media containing either maltose, peptides (hydrolyzed casein), or both as the carbon source(s), each with and without elemental sulfur (S0). Growth rates were highest on media containing peptides and S0, with or without maltose. Growth did not occur on the peptide medium without S0. S0 had no effect on growth rates in the maltose medium in the absence of peptides. Phenylacetate production rates (from phenylalanine fermentation) from cells grown in the peptide medium containing S0 with or without maltose were the same, suggesting that S0 is required for peptide utilization. The activities of 14 of 21 enzymes involved in or related to the fermentation pathways of P. furiosus were shown to be regulated under the five different growth conditions studied. The presence of S0 in the growth media resulted in decreases in specific activities of two cytoplasmic hydrogenases (I and II) and of a membrane-bound hydrogenase, each by an order of magnitude. The primary S0-reducing enzyme in this organism and the mechanism of the S0 dependence of peptide metabolism are not known. This study provides the first evidence for a highly regulated fermentation-based metabolism in P. furiosus and a significant regulatory role for elemental sulfur or its metabolites.

ACE2 DOES NOT PLAY A MAJOR ROLE IN ANGIOTENSIN PEPTIDE METABOLISM IN THE HUMAN CORONARY CIRCULATIO

2004 ◽  
Vol 22 (Suppl. 2) ◽  
pp. S152
Author(s):  
D. J. Campbell ◽  
C. J. Zeitz ◽  
M. D. Esler ◽  
J. D. Horowitz
Keyword(s):  
Angiotensin Peptide ◽  
Peptide Metabolism
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