| B-type natriuretic peptide 8-32, which is produced from mature BNP 1-32 by the metalloprotease meprin A, has reduced bioactivity. | |
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MedLine Citation:
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PMID: 19386989 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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32-amino acid B-type natriuretic peptide (BNP 1-32) plays an important role in cardiovascular homeostasis. Recently, it was reported that BNP 1-32 is cleaved by the metalloprotease meprin A to BNP 8-32, the bioactivity of which is undefined. We hypothesized that BNP 8-32 has reduced vasodilating and natriuretic bioactivity compared with BNP 1-32 in vivo. Human BNP 8-32 and BNP 1-32 were compared in a crossover study in eight anesthetized normal canines. After a preinfusion clearance, BNP 1-32 was infused at 30 ng.kg(-1) x min(-1) for 45 min followed by a 60-min washout and a second preinfusion clearance. Then, equimolar BNP 8-32 was infused. In half of the studies, the peptide sequence was reversed. Changes with peptides from the respective preinfusion clearance to infusion clearance were compared with paired tests. Mean arterial pressure was reduced by both BNP 8-32 and BNP 1-32 (-8 +/- 3 vs. -6 +/- 2 mmHg, P = 0.48). Changes in right atrial pressure, pulmonary capillary wedge pressure, heart rate, cardiac output, and glomerular filtration rate were similar. However, urinary sodium excretion increased less with BNP 8-32 than with BNP 1-32 (+171 +/- 24 vs. +433 +/- 43 muEq/min; P = 0.008), as did urinary potassium excretion, urine flow, and renal blood flow. While BNP 8-32 has similar vasodilating actions as BNP 1-32, its diuretic and natriuretic actions are reduced, suggesting a role for meprin A in the regulation of BNP 1-32 bioactivity in the kidney. Meprin A inhibition may be a potential strategy to increase the bioactivity of endogenous and exogenous BNP 1-32 in cardiovascular diseases. |
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Authors:
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Guido Boerrigter; Lisa C Costello-Boerrigter; Gail J Harty; Brenda K Huntley; Alessandro Cataliotti; Harald Lapp; John C Burnett |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2009-04-22 |
Journal Detail:
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Title: American journal of physiology. Regulatory, integrative and comparative physiology Volume: 296 ISSN: 0363-6119 ISO Abbreviation: Am. J. Physiol. Regul. Integr. Comp. Physiol. Publication Date: 2009 Jun |
Date Detail:
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Created Date: 2009-05-21 Completed Date: 2009-07-02 Revised Date: 2010-09-27 |
Medline Journal Info:
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Nlm Unique ID: 100901230 Medline TA: Am J Physiol Regul Integr Comp Physiol Country: United States |
Other Details:
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Languages: eng Pagination: R1744-50 Citation Subset: IM |
Affiliation:
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Cardiorenal Research Laboratory, Guggenheim 915, Mayo Clinic and Mayo Clinic College of Medicine, 200 First St. SW, Rochester, MN 55905, USA. boerrigter.guido@mayo.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Biological Markers / blood Cardiovascular System / metabolism* Cells, Cultured Cyclic GMP / metabolism Diuresis* Dogs Endothelial Cells / metabolism Hemodynamics* Humans Infusions, Intravenous Kidney / metabolism* Male Metalloendopeptidases / metabolism* Molecular Sequence Data Natriuresis* Natriuretic Peptide, Brain / administration & dosage, chemistry, metabolism* Peptide Fragments / administration & dosage, chemistry, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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HL-07111/HL/NHLBI NIH HHS; HL-36634/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Biological Markers; 0/Peptide Fragments; 114471-18-0/Natriuretic Peptide, Brain; 7665-99-8/Cyclic GMP; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.18/meprin A |
| Comments/Corrections | |
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