| An oxidized analog of alpha-human atrial natriuretic polypeptide is a selective agonist for the atrial-natriuretic-polypeptide clearance receptor which lacks a guanylate cyclase. | |
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MedLine Citation:
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PMID: 1346519 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The differences in biological functions between alpha-human atrial natriuretic polypeptide (alpha-hANP) and its oxidized analog, MetSO-alpha-hANP, have been investigated. Analysis of the ANP receptor subtypes by affinity labeling has shown that a bovine pulmonary aortic endothelial cell line (CPAE cells) primarily expresses ANP-R1 (R, receptor) coupled to particulate guanylate cyclase, while Hela cells from human cervical carcinoma predominantly express ANP-R2, which lacks a guanylate cyclase. alpha-hANP could bind to both ANP receptor subtypes with high affinity, while MetSO-alpha-hANP showed more selective binding to ANP-R2 than to ANP-R1. The activity of MetSO-alpha-hANP for stimulation of guanylate cyclase coupled to ANP-R1 was about 520-fold less than that of alpha-hANP (median effective dose = 2.5 nM for alpha-hANP, 1.3 microM for MetSO-alpha-hANP), indicating that MetSO-alpha-hANP was a partial agonist for this receptor. While this oxidized analog could inhibit the cAMP production through ANP-R2, with 0.15 times the activity of alpha-hANP (median concentration = 0.31 nM for alpha-hANP, 2.0 nM for MetSO-alpha-hANP). In in vivo studies, the diuretic activity of MetSO-alpha-hANP was 25-100-fold less than that of alpha-hANP. In addition, MetSO-alpha-hANP could potentiate the diuretic activity of alpha-hANP that was also caused by C-ANF4-23, a specific agonist for ANP-R2. These results demonstrate that MetSO-alpha-hANP can act as an agonist more selective for ANP-R2 than for ANP-R1, both in vivo and in vitro. The relationship between receptor selectivities and the conformation of alpha-hANP or MetSO-alpha-hANP was also discussed. |
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Authors:
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S Koyama; T Terai; T Inoue; K Inomata; K Tamura; Y Kobayashi; Y Kyogoku; M Kobayashi |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 203 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1992 Feb |
Date Detail:
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Created Date: 1992-03-11 Completed Date: 1992-03-11 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY |
Other Details:
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Languages: eng Pagination: 425-32 Citation Subset: IM |
Affiliation:
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Research Laboratories, Fujisawa Pharmaceutical Co. Ltd., Osaka, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Affinity Labels Animals Atrial Natriuretic Factor / metabolism*, pharmacology Cells, Cultured Cross-Linking Reagents Cyclic AMP / biosynthesis Diuresis / drug effects Endothelium, Vascular / cytology, metabolism Guanylate Cyclase / metabolism* Hela Cells Humans Male Oxidation-Reduction Rats Rats, Inbred Strains Receptors, Atrial Natriuretic Factor Receptors, Cell Surface / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Affinity Labels; 0/Cross-Linking Reagents; 0/Receptors, Cell Surface; 0/oxidized methionine-alpha-human atrial natriuretic factor; 60-92-4/Cyclic AMP; 85637-73-6/Atrial Natriuretic Factor; EC 4.6.1.2/Guanylate Cyclase; EC 4.6.1.2/Receptors, Atrial Natriuretic Factor |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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