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Atrial natriuretic peptide degradation by CPA47 cells - Evidence for a divalent cation-independent cell-surface proteolytic activityAtrial natriuretic peptide (ANP) is rapidly cleared and degraded in vivo. Nonguanylate-cyclase receptors (C-ANPR) and a metalloproteinase, neutral endopeptidase (EC 3.4.24.11) (NEP 24.11), are thought to be responsible for its metabolism. We investigated the mechanisms of ANP degradation by an endothelial-derived cell line, CPA47. CPA47 cells degraded 88 percent of 125I-ANP after 1 h at 37 degrees C as determined by HPLC. Medium preconditioned by these cells degraded 41 percent of the 125I-ANP, and this activity was inhibited by a divalent cation chelator, EDTA. Furthermore, a cell-surface proteolytic activity degraded 125I-ANP in the presence of EDTA when receptor-mediated endocytosis was inhibited either by low temperature (4 degrees C) or by hyperosmolarity at 37 degrees C. The metalloproteinase, NEP 24.11, is unlikely to be the cell-surface peptidase because 125I-ANP is degraded by CPA47 cells at 4 degrees C in the presence of 5 mM EDTA. These data indicate that CPA47 cells can degrade ANP by a novel divalent cation-independent cell-surface proteolytic activity.
Document ID
19930044729
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Frost, S. J.
(NASA Lyndon B. Johnson Space Center Houston, TX, United States)
Chen, Y. M.
(NASA Lyndon B. Johnson Space Center Houston, TX, United States)
Whitson, P. A.
(NASA Johnson Space Center Houston, TX, United States)
Date Acquired
August 16, 2013
Publication Date
November 23, 1992
Publication Information
Publication: Biochimica et Biophysica Acta
Volume: 1112
Issue: 1
ISSN: 0006-3002
Subject Category
Life Sciences (General)
Accession Number
93A28726
Distribution Limits
Public
Copyright
Other

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