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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1993-5-19
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pubmed:abstractText |
Two structurally distinct series of potent and selective inhibitors of an aspartyl protease-like endothelin converting enzyme (ECE) activity identified in the rat lung have been developed. Pepstatin A, which potently inhibits the rat lung ECE, served as the basis for the first series. Alternatively, selected renin inhibitors containing the dihydroxyethylene moiety were shown to be inhibitors of rat lung activity. Subsequent modifications improved inhibition of the rat lung ECE while eliminating renin activity. Both series of ECE inhibitors demonstrated a range of selectivity over Cathepsin D. Water-solubilizing moieties were appended onto selected compounds to facilitate in vivo testing. Partial reduction of the pressor response to exogenously administered Big ET-1 was observed with selected rat lung ECE inhibitors.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin D,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Pepstatins,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Renin,
http://linkedlifedata.com/resource/pubmed/chemical/Streptomyces pepsin inhibitor,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/endothelin-converting enzyme,
http://linkedlifedata.com/resource/pubmed/chemical/pepstatin,
http://linkedlifedata.com/resource/pubmed/chemical/statine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-2623
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
468-78
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8474103-Amino Acid Sequence,
pubmed-meshheading:8474103-Amino Acids,
pubmed-meshheading:8474103-Animals,
pubmed-meshheading:8474103-Aspartic Acid Endopeptidases,
pubmed-meshheading:8474103-Blood Pressure,
pubmed-meshheading:8474103-Cathepsin D,
pubmed-meshheading:8474103-Cell Membrane,
pubmed-meshheading:8474103-Endothelins,
pubmed-meshheading:8474103-Humans,
pubmed-meshheading:8474103-Lung,
pubmed-meshheading:8474103-Metalloendopeptidases,
pubmed-meshheading:8474103-Molecular Sequence Data,
pubmed-meshheading:8474103-Molecular Structure,
pubmed-meshheading:8474103-Pepstatins,
pubmed-meshheading:8474103-Protease Inhibitors,
pubmed-meshheading:8474103-Rats,
pubmed-meshheading:8474103-Renin,
pubmed-meshheading:8474103-Solubility,
pubmed-meshheading:8474103-Structure-Activity Relationship,
pubmed-meshheading:8474103-Water
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pubmed:year |
1993
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pubmed:articleTitle |
Potent and selective inhibitors of an aspartyl protease-like endothelin converting enzyme identified in rat lung.
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pubmed:affiliation |
Pharmaceutical Products Division, Abbott Laboratories, Abbott Park, Illinois 60064.
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pubmed:publicationType |
Journal Article,
Comparative Study
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