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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1981-8-20
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pubmed:abstractText |
There are several approaches for interfering with the renin-angiotensin system. Antibodies against renin angiotensins I and II (AI and AII) have not been consistently successful in the past, probably because of nonspecific effects; however, recent purification of renin now makes this approach more promising. Renin inhibitors include pepstatin and analogs, lipids and phospholipids, and renin-substrate analogs. Pepstatin and analogs are the most potent and specific but they are not orally active. The phospholipids are the most effective in vivo but their specificity is yet to be established. No renin-substrate analogs have been developed that have biologically significant effects. Some of the most potent and specific agents available for interfering with the renin-angiotensin system are the AII-receptor antagonists. While these compounds effectively prevent the actions of AII, they suffer from several severe deficiencies: partial agonist activity, short duration of action, and lack of oral activity. The recent development of angiotensin-converting enzyme ACE) inhibitors that are orally active has provided the greatest degree of clinical success for inhibitors of the renin-angiotensin system and, consequently, the impetus to develop still better compounds. Captopril (SQ 14,225) is the prototype ACE inhibitor, being highly potent and specific with no other demonstrated pharmacological activity. Captopril is effective in all forms of human and animal models of hypertension except mineralocorticoid hypertension, which requires concomitant diuretic therapy. Because ACE is the same enzyme as kininase II, the enzyme that degrades kinins, the possibility exists that kinins are involved in the cardiovascular action of captopril, although this prospect is unlikely.
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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/Angiotensin I,
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin II,
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin-Converting Enzyme...,
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensins,
http://linkedlifedata.com/resource/pubmed/chemical/Captopril,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Pepstatins,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Renin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-9446
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2275-84
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:6263716-Amino Acid Sequence,
pubmed-meshheading:6263716-Angiotensin I,
pubmed-meshheading:6263716-Angiotensin II,
pubmed-meshheading:6263716-Angiotensin-Converting Enzyme Inhibitors,
pubmed-meshheading:6263716-Angiotensins,
pubmed-meshheading:6263716-Animals,
pubmed-meshheading:6263716-Blood Pressure,
pubmed-meshheading:6263716-Captopril,
pubmed-meshheading:6263716-Cardiac Output,
pubmed-meshheading:6263716-Dogs,
pubmed-meshheading:6263716-Hypertension,
pubmed-meshheading:6263716-Lipids,
pubmed-meshheading:6263716-Pepstatins,
pubmed-meshheading:6263716-Phospholipids,
pubmed-meshheading:6263716-Rats,
pubmed-meshheading:6263716-Renin,
pubmed-meshheading:6263716-Structure-Activity Relationship,
pubmed-meshheading:6263716-Substrate Specificity
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pubmed:year |
1981
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pubmed:articleTitle |
Drugs inhibiting the renin - angiotensin system.
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pubmed:publicationType |
Journal Article,
Review
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