Document Detail


Mode of cleavage of porcine big endothelin-1 by aspartic proteinases.
MedLine Citation:
PMID:  1725436     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cleavage sites of porcine big endothelin-1 (big ET-1, 1-39) by cathepsin D were examined and compared with those by other aspartic proteinases including pepsin. Cathepsin D cleaved not only the Trp21-Val22 bond, but also the Asp18-Ile19 bond of big ET-1[1-39]. The mature ET-1[1-21], generated by the cleavage between Trp21 and Val22, was subsequently degraded by removal of the C-terminal tripeptide (Ile19-Ile20-Trp21). On the other hand, pepsin cleaved the Trp21-Val22 bond of big ET-1[1-39] to produce ET-1[1-21], but did not degrade the generated ET-1[1-21]. These results indicate that aspartic proteinases such as cathepsin D and pepsin are capable of converting big ET-1[1-39] to ET-1[1-21], whereas the former proteinase is by no means specific for the Trp21-Val22 bond of big ET-1[1-39].
Authors:
M Takaoka; Y Hukumori; K Shiragami; R Ikegawa; Y Matsumura; S Morimoto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cardiovascular pharmacology     Volume:  17 Suppl 7     ISSN:  0160-2446     ISO Abbreviation:  J. Cardiovasc. Pharmacol.     Publication Date:  1991  
Date Detail:
Created Date:  1992-05-12     Completed Date:  1992-05-12     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  7902492     Medline TA:  J Cardiovasc Pharmacol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  S68-70     Citation Subset:  IM    
Affiliation:
Department of Pharmacology, Osaka University of Pharmaceutical Sciences, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Aspartic Acid Endopeptidases / metabolism*
Cathepsin D / metabolism
Endothelin-1
Endothelins / metabolism*
Hydrogen-Ion Concentration
Molecular Sequence Data
Pepsin A / metabolism
Protein Precursors / metabolism*
Swine
Chemical
Reg. No./Substance:
0/Endothelin-1; 0/Endothelins; 0/Protein Precursors; EC 3.4.23.-/Aspartic Acid Endopeptidases; EC 3.4.23.1/Pepsin A; EC 3.4.23.5/Cathepsin D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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