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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1992-5-12
|
| pubmed:abstractText |
We investigated endothelin (ET)-converting enzyme and its localization in the vasculature. The membrane and cytosol fractions of cultured endothelial cells of bovine carotid artery contain phosphoramidon-sensitive ET-converting enzymes, and their molecular weights are about 100 and 540 kDa, respectively. The specific conversion of big ET-1 by these enzymes proceeds at pH 7.0 +/- 0.5, and it is inhibited by EDTA, o-phenanthroline, and phosphoramidon. Big ET-3 is converted by the membrane enzyme at a rate about one-tenth that of big ET-1, but it is not converted by the cytosol enzyme. Big ET-1 (but not ET-1)-induced hypertension in rats was remarkably suppressed by pretreatment with phosphoramidon, and big ET-1 (but not ET-1)-induced contraction of isolated coronary arteries, either with or without the endothelium, was substantially suppressed by phosphoramidon. These results suggest an essential role of phosphoramidon-sensitive enzyme(s) in the vascular conversion of big ET-1, and the existence of such enzymes also in nonendothelial cells. We found three converting enzymes operating at different optimal pH values in noncultured vascular smooth muscle cells; two pepstatin-sensitive, cytosolic acid proteinases and a phosphoramidon-sensitive neutral enzyme(s) in the membrane and cytosol. All of these findings strongly suggest the importance of phosphoramidon-sensitive neutral enzymes in the vascular conversion of big ET-1.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/endothelin-converting enzyme,
http://linkedlifedata.com/resource/pubmed/chemical/phosphoramidon
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| pubmed:status |
MEDLINE
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| pubmed:issn |
0160-2446
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
17 Suppl 7
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
S26-8
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| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:1725349-Animals,
pubmed-meshheading:1725349-Aspartic Acid Endopeptidases,
pubmed-meshheading:1725349-Blood Pressure,
pubmed-meshheading:1725349-Carotid Arteries,
pubmed-meshheading:1725349-Cattle,
pubmed-meshheading:1725349-Cell Membrane,
pubmed-meshheading:1725349-Cells, Cultured,
pubmed-meshheading:1725349-Cytosol,
pubmed-meshheading:1725349-Endothelin-1,
pubmed-meshheading:1725349-Endothelins,
pubmed-meshheading:1725349-Endothelium, Vascular,
pubmed-meshheading:1725349-Glycopeptides,
pubmed-meshheading:1725349-Humans,
pubmed-meshheading:1725349-Metalloendopeptidases,
pubmed-meshheading:1725349-Muscle, Smooth, Vascular,
pubmed-meshheading:1725349-Muscle Contraction,
pubmed-meshheading:1725349-Protein Precursors,
pubmed-meshheading:1725349-Rats,
pubmed-meshheading:1725349-Swine
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| pubmed:year |
1991
|
| pubmed:articleTitle |
Endothelin-converting enzyme and its in vitro and in vivo inhibition.
|
| pubmed:affiliation |
Biochemistry, Central Research Laboratory, Banyu Pharmaceutical Co., Ltd., Tokyo, Japan.
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| pubmed:publicationType |
Journal Article,
In Vitro
|