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 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.
Watanabe
Y
Y
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
Nakajima
K
K
Shimamori
Y
Y
Fujimoto
Y
Y
D000595:Amino Acid Sequence; D009320:Atrial Natriuretic Factor / Q000378:metabolism; D004789:Enzyme Activation; D006801:Humans; D006868:Hydrolysis; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D045283:Natriuretic Agents / Q000378:metabolism*; D020097:Natriuretic Peptide, Brain; D020098:Natriuretic Peptide, C-Type; D015260:Neprilysin / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism; D011506:Proteins / Q000378:metabolism
D008565:Membrane Proteins; D045283:Natriuretic Agents; D009419:Nerve Tissue Proteins; D011506:Proteins; D020097:Natriuretic Peptide, Brain; C076910:brain natriuretic peptide, porcine; D020098:Natriuretic Peptide, C-Type; D009320:Atrial Natriuretic Factor; D015260:Neprilysin