{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,4]],"date-time":"2025-09-04T13:13:36Z","timestamp":1756991616920},"reference-count":31,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2004,2,19]],"date-time":"2004-02-19T00:00:00Z","timestamp":1077148800000},"content-version":"vor","delay-in-days":3915,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[1993,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Atrial natriuretic peptide (ANP) is a fluid\u2010regulating peptide hormone that promotes vasorelaxation, natriuresis, and diuresis. The mechanisms for the release of ANP and for its clearance from the circulation play important roles in modulating its biological effects. Recently, we have reported that the cell surface of an endothelial cell line, CPA47, could degrade <jats:sup>125<\/jats:sup>I\u2010ANP in the presence of EDTA. In this study, we have characterized this degradation of <jats:sup>125<\/jats:sup>I\u2010ANP. The kinetics of ANP degradation by the surface of CPA47 cells were first order, with a K<jats:sub>m<\/jats:sub> of 320 \u00b1 60 nM and V<jats:sub>max<\/jats:sub> of 35 \u00b1 14 pmol of ANP degraded\/10 min\/10<jats:sup>5<\/jats:sup> cells at pH 7.4. ANP is degraded by the surface of CPA47 cells over a broad pH range from 7.0\u20138.5. Potato carboxypeptidase inhibitor and bestatin inhibited <jats:sup>125<\/jats:sup>I\u2010ANP degradation, suggesting that this degradative activity on the surface of CPA47 cells has exopeptidase characteristics. The selectivity of CPA47 cell\u2010surface degradation of ANP was demonstrated when <jats:sup>125<\/jats:sup>I\u2010ANP degradation was inhibited in the presence of neuropeptide Y and angiotensin I and II but not bradykinin, bombesin, endothelin\u20101, or substance P. The C\u2010terminal amino acids phe<jats:sup>26<\/jats:sup> and tyr<jats:sup>28<\/jats:sup> were deduced to be important for ANP interaction with the cell\u2010surface peptidase(s) based on comparison of the IC<jats:sub>50<\/jats:sub> of various ANP analogues and other natriuretic peptides for the inhibition of ANP degradation. These data suggest that a newly characterized divalent cation\u2010independent exopeptidase(s) that selectively recognizes ANP and some other vasoactive peptides exists on the surface of endothelial cells.<\/jats:p>","DOI":"10.1002\/jcb.240520214","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T21:12:53Z","timestamp":1117314773000},"page":"227-236","source":"Crossref","is-referenced-by-count":6,"title":["Characterization of atrial natriuretic peptide degradation by cell\u2010surface peptidase activity on endothelial cells"],"prefix":"10.1002","volume":"52","author":[{"given":"Stephen J.","family":"Frost","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peggy 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