Biochemical analysis of neutral endopeptidase activity reveals independent catabolism of atrial and brain natriuretic peptide

Verfasser / Beitragende:
[T. Walther, H. Stepan, K. Pankow, M. Becker, H.-P. Schultheiss, W.-E. Siems]
Ort, Verlag, Jahr:
2004
Enthalten in:
Biological Chemistry, 385/2(2004-02-05), 179-184
Format:
Artikel (online)
ID: 378893106
LEADER caa a22 4500
001 378893106
003 CHVBK
005 20180305123500.0
007 cr unu---uuuuu
008 161128e20040205xx s 000 0 eng
024 7 0 |a 10.1515/BC.2004.036  |2 doi 
035 |a (NATIONALLICENCE)gruyter-10.1515/BC.2004.036 
245 0 0 |a Biochemical analysis of neutral endopeptidase activity reveals independent catabolism of atrial and brain natriuretic peptide  |h [Elektronische Daten]  |c [T. Walther, H. Stepan, K. Pankow, M. Becker, H.-P. Schultheiss, W.-E. Siems] 
520 3 |a Recent reports presented contradictory results regarding the catabolism of mature atrial (ANP) and brain (BNP) natriuretic peptides in circulation. Especially the role of neutral endopeptidase (NEP) in BNP degradation was conversely discussed. Our present in vitro-studies characterize the NEP-dependent metabolism of ANP and BNP in different tissues via HPLC-analysis using NEP-deficient mice and specific NEP inhibitors. Our results show a strong tissue-dependent degradation pattern of both peptides, which are not only due to the different NEP activities in these tissues. Whereas NEP rapidly degraded ANP, it had no influence in BNP-metabolism. Additional experiments with purified NEP confirmed this result. Moreover, we describe a degradation of ANP and BNP in NEP-deficient and NEP-inhibited membranes. Consequently, we postulate the existence of at least one further natriuretic peptide (NP) degrading enzyme, which has not been characterized yet. Thus, the commonly accepted model of the natriuretic peptide system with NEP as the central degrading peptidase has to be partly revised. Moreover, the NEP-independent BNP degradation provides an effective means for achieving a beneficial BNP increase in cardiovascular pathology by inhibiting the assumed novel NP-degrading peptidase(s). 
540 |a Copyright © 2004 by Walter de Gruyter GmbH & Co. KG 
690 7 |a Biochemistry  |2 nationallicence 
690 7 |a Molecular biology  |2 nationallicence 
690 7 |a Cellular biology  |2 nationallicence 
700 1 |a Walther  |D T.  |4 aut 
700 1 |a Stepan  |D H.  |4 aut 
700 1 |a Pankow  |D K.  |4 aut 
700 1 |a Becker  |D M.  |4 aut 
700 1 |a Schultheiss  |D H.-P  |4 aut 
700 1 |a Siems  |D W.-E  |4 aut 
773 0 |t Biological Chemistry  |d Walter de Gruyter  |g 385/2(2004-02-05), 179-184  |x 1431-6730  |q 385:2<179  |1 2004  |2 385  |o bchm 
856 4 0 |u https://doi.org/10.1515/BC.2004.036  |q text/html  |z Onlinezugriff via DOI 
908 |D 1  |a research article  |2 jats 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1515/BC.2004.036  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Walther  |D T.  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Stepan  |D H.  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Pankow  |D K.  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Becker  |D M.  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Schultheiss  |D H.-P  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Siems  |D W.-E  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Biological Chemistry  |d Walter de Gruyter  |g 385/2(2004-02-05), 179-184  |x 1431-6730  |q 385:2<179  |1 2004  |2 385  |o bchm 
900 7 |b CC0  |u http://creativecommons.org/publicdomain/zero/1.0  |2 nationallicence 
898 |a BK010053  |b XK010053  |c XK010000 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-gruyter