| Mode of cleavage of porcine big endothelin-1 by aspartic proteinases. | |
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MedLine Citation:
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PMID: 1725436 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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]. |
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Authors:
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M Takaoka; Y Hukumori; K Shiragami; R Ikegawa; Y Matsumura; S Morimoto |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of cardiovascular pharmacology Volume: 17 Suppl 7 ISSN: 0160-2446 ISO Abbreviation: J. Cardiovasc. Pharmacol. Publication Date: 1991 |
Date Detail:
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Created Date: 1992-05-12 Completed Date: 1992-05-12 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 7902492 Medline TA: J Cardiovasc Pharmacol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: S68-70 Citation Subset: IM |
Affiliation:
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Department of Pharmacology, Osaka University of Pharmaceutical Sciences, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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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:
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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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