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 |
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| container_title | Biochemical and molecular medicine |
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| creator | Watanabe, Yasuhiro Nakajima, Kenjiro Shimamori, Yoshimitsu Fujimoto, Yukio |
| description | 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. |
| doi_str_mv | 10.1006/bmme.1997.2584 |
| format | Article |
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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.</description><identifier>ISSN: 1077-3150</identifier><identifier>EISSN: 1095-5577</identifier><identifier>DOI: 10.1006/bmme.1997.2584</identifier><identifier>PMID: 9232196</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Atrial Natriuretic Factor - metabolism ; Enzyme Activation ; Humans ; Hydrolysis ; Kidney - enzymology ; Kinetics ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Natriuretic Agents - metabolism ; Natriuretic Peptide, Brain ; Natriuretic Peptide, C-Type ; Neprilysin - metabolism ; Nerve Tissue Proteins - metabolism ; Proteins - metabolism</subject><ispartof>Biochemical and molecular medicine, 1997-06, Vol.61 (1), p.47-51</ispartof><rights>1997 Academic Press</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-5dc2894782b551114b18f168297d0a67ee317b37526ab614b11604a38a4a1b233</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9232196$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Watanabe, Yasuhiro</creatorcontrib><creatorcontrib>Nakajima, Kenjiro</creatorcontrib><creatorcontrib>Shimamori, Yoshimitsu</creatorcontrib><creatorcontrib>Fujimoto, Yukio</creatorcontrib><title>Comparison of the Hydrolysis of the Three Types of Natriuretic Peptides by Human Kidney Neutral Endopeptidase 24.11</title><title>Biochemical and molecular medicine</title><addtitle>Biochem Mol Med</addtitle><description>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. 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| ispartof | Biochemical and molecular medicine, 1997-06, Vol.61 (1), p.47-51 |
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| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Atrial Natriuretic Factor - metabolism Enzyme Activation Humans Hydrolysis Kidney - enzymology Kinetics Membrane Proteins - metabolism Molecular Sequence Data Natriuretic Agents - metabolism Natriuretic Peptide, Brain Natriuretic Peptide, C-Type Neprilysin - metabolism Nerve Tissue Proteins - metabolism Proteins - metabolism |
| title | Comparison of the Hydrolysis of the Three Types of Natriuretic Peptides by Human Kidney Neutral Endopeptidase 24.11 |
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