TY - JOUR
T1 - Enzymatic inactivation of major circulating forms of atrial and brain natriuretic peptides
AU - Ozaki, Junko
AU - Shimizu, Hiromasa
AU - Hashimoto, Yukiya
AU - Itoh, Hiroshi
AU - Nakao, Kazuwa
AU - Inui, Ken Ichi
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan.
PY - 1999/4/16
Y1 - 1999/4/16
N2 - We compared the enzymatic inactivation of major circulating forms of atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). Both ANP and BNP induced a significant increase in cyclic GMP (cGMP) formation in cultured epithelial cell line derived from porcine kidney, LLC-PK1. The cGMP formation stimulated by ANP in LLC-PK1 cells was significantly decreased by pre-treatment of the peptide with rat renal brush-border membranes, and the inactivation of ANP was inhibited by neutral endopeptidase inhibitors, phosphoramidon and S-thiorphan. BNP exhibited greater resistance to enzymatic inactivation than did ANP. In addition, phosphoramidon potentiated the natriuresis with a low dose (7.5 pmol min-1 kg-1) of ANP but not of BNP in rats. These results suggest that enzymatic degradation of natriuretic peptides is highly dependent on peptide structure, and that the affinity of BNP to neutral endopeptidase is less than that of ANP. Copyright (C) 1999 Elsevier Science B.V.
AB - We compared the enzymatic inactivation of major circulating forms of atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). Both ANP and BNP induced a significant increase in cyclic GMP (cGMP) formation in cultured epithelial cell line derived from porcine kidney, LLC-PK1. The cGMP formation stimulated by ANP in LLC-PK1 cells was significantly decreased by pre-treatment of the peptide with rat renal brush-border membranes, and the inactivation of ANP was inhibited by neutral endopeptidase inhibitors, phosphoramidon and S-thiorphan. BNP exhibited greater resistance to enzymatic inactivation than did ANP. In addition, phosphoramidon potentiated the natriuresis with a low dose (7.5 pmol min-1 kg-1) of ANP but not of BNP in rats. These results suggest that enzymatic degradation of natriuretic peptides is highly dependent on peptide structure, and that the affinity of BNP to neutral endopeptidase is less than that of ANP. Copyright (C) 1999 Elsevier Science B.V.
KW - ANP (Atrial natriuretic peptide)
KW - BNP (Brain natriuretic peptide)
KW - Kidney epithelial cell line (LLC-PK)
KW - Neutral endopeptidase
KW - Phosphoramidon
KW - Thiorphan
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U2 - 10.1016/S0014-2999(99)00115-6
DO - 10.1016/S0014-2999(99)00115-6
M3 - Article
C2 - 10334507
AN - SCOPUS:0032952423
VL - 370
SP - 307
EP - 312
JO - European Journal of Pharmacology
JF - European Journal of Pharmacology
SN - 0014-2999
IS - 3
ER -