Comparison of the Hydrolysis of the Three Types of Natriuretic Peptides by Human Kidney Neutral Endopeptidase 24.11

The degradation of 3 human natriuretic peptides by human kidney neutral endopeptidase 24.11 has been investigated. The studies revealed that hANP-28 and hCNP-22 are the preferred substrates, whereas hBNP-32 is not. The enzyme has been known to inactivate hANP-28 from cleavage at the Cys-Phe bond at...

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Veröffentlicht in:Biochemical and molecular medicine 1997-06, Vol.61 (1), p.47-51
Hauptverfasser: Watanabe, Yasuhiro, Nakajima, Kenjiro, Shimamori, Yoshimitsu, Fujimoto, Yukio
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Sprache:eng
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Zusammenfassung:The degradation of 3 human natriuretic peptides by human kidney neutral endopeptidase 24.11 has been investigated. The studies revealed that hANP-28 and hCNP-22 are the preferred substrates, whereas hBNP-32 is not. The enzyme has been known to inactivate hANP-28 from cleavage at the Cys-Phe bond at the beginning of its ring structure. Analysis of the cleavage sites of each peptide indicated that the initial cleavage site of hCNP-22 is analogous to that of hANP-28. The Cys-Phe bond of hBNP-32 was insensitive to this enzymatic cleavage. We speculate that the stability of hBNP-32 may result from the insusceptibility of its Cys-Phe bond at the beginning of the ring structure.
ISSN:1077-3150
1095-5577
DOI:10.1006/bmme.1997.2584