| pubmed-article:1872872 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C0079281 | lld:lifeskim |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C0026844 | lld:lifeskim |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:1872872 | lifeskim:mentions | umls-concept:C0053571 | lld:lifeskim |
| pubmed-article:1872872 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1872872 | pubmed:dateCreated | 1991-9-18 | lld:pubmed |
| pubmed-article:1872872 | 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. | lld:pubmed |
| pubmed-article:1872872 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1872872 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1872872 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1872872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1872872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1872872 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1872872 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1872872 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:1872872 | pubmed:author | pubmed-author:MatsumuraYY | lld:pubmed |
| pubmed-article:1872872 | pubmed:author | pubmed-author:TsukaharaYY | lld:pubmed |
| pubmed-article:1872872 | pubmed:author | pubmed-author:MorimotoSS | lld:pubmed |
| pubmed-article:1872872 | pubmed:author | pubmed-author:TakaokaMM | lld:pubmed |
| pubmed-article:1872872 | pubmed:author | pubmed-author:IkegawaRR | lld:pubmed |
| pubmed-article:1872872 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1872872 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1872872 | pubmed:volume | 178 | lld:pubmed |
| pubmed-article:1872872 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1872872 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1872872 | pubmed:pagination | 899-905 | lld:pubmed |
| pubmed-article:1872872 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1872872 | pubmed:meshHeading | pubmed-meshheading:1872872-... | lld:pubmed |
| pubmed-article:1872872 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1872872 | pubmed:articleTitle | Conversion of big endothelin-1 to endothelin-1 by two-types of metalloproteinases of cultured porcine vascular smooth muscle cells. | lld:pubmed |
| pubmed-article:1872872 | pubmed:affiliation | Department of Pharmacology, Osaka University of Pharmaceutical Sciences, Japan. | lld:pubmed |
| pubmed-article:1872872 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1872872 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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