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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1991-9-18
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pubmed:abstractText |
Incubation of big endothelin-1 (big ET-1, 1-39) with the membrane fraction obtained from cultured vascular smooth muscle cells (VSMCs) resulted in an increase in immunoreactive-ET (IR-ET), which was inhibited by EDTA but not by phosphoramidon, a metalloproteinase inhibitor. When the incubation was performed in the presence of N-ethylmaleimide (NEM), the generation of IR-ET was markedly augmented and this augmentation was abolished by phosphoramidon. The pH profile for IR-ET generation in the presence of NEM was apparently distinct from that observed in the absence of NEM. Reverse-phase HPLC of the incubation mixture with or without NEM revealed one major IR-ET component corresponding to the elution position of synthetic ET-1 (1-21). When the cultured VSMCs were incubated with big ET-1, a conversion to the mature ET-1 was observed. This ET-1 generation from exogenously applied big ET-1 was markedly inhibited by the addition of phosphoramidon, although the inhibitor did not influence the basal secretion of ET-1-like materials. These results suggest the presence of two types of metalloproteinases, which can generate ET-1, in VSMCs. The possibility that ET-1 functions in an autocrine manner to control the cardiovascular system warrants further attention.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endothelin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
178
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
899-905
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1872872-Animals,
pubmed-meshheading:1872872-Aorta,
pubmed-meshheading:1872872-Cell Membrane,
pubmed-meshheading:1872872-Cells, Cultured,
pubmed-meshheading:1872872-Chromatography, High Pressure Liquid,
pubmed-meshheading:1872872-Endothelin-1,
pubmed-meshheading:1872872-Endothelins,
pubmed-meshheading:1872872-Isoenzymes,
pubmed-meshheading:1872872-Kinetics,
pubmed-meshheading:1872872-Metalloendopeptidases,
pubmed-meshheading:1872872-Muscle, Smooth, Vascular,
pubmed-meshheading:1872872-Protein Precursors,
pubmed-meshheading:1872872-Protein Processing, Post-Translational,
pubmed-meshheading:1872872-Radioimmunoassay,
pubmed-meshheading:1872872-Swine
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pubmed:year |
1991
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pubmed:articleTitle |
Conversion of big endothelin-1 to endothelin-1 by two-types of metalloproteinases of cultured porcine vascular smooth muscle cells.
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pubmed:affiliation |
Department of Pharmacology, Osaka University of Pharmaceutical Sciences, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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