Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0020538 (hypertension)
 170,190 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The aim of the study was to evaluate effectiveness and safety of angiotensin II receptor blockers and inhibitors of angiotensin-converting enzyme (ECE) for protective therapy following medicamentous cardioversion with propafen at a loading dose of 600 mg in patients with paroxysmal atrial fibrillation and arterial hypertension. 101 patients were divided in 2 groups. Group 1 included 75 patients who received ACE inhibitor lisinopril (10 mg BID) after recovery of sinus rhythm by propanorm. 26 patients of group 2 were treated with angiotensin II receptor blocker candesartan (8 mg daily). Combined treatment with angiotensin II receptor blocker and propafenone leads to cardioversion faster than therapy with ACR inhibitor. It is concluded that alternative approach to the maintenance of sinus rhythm using angiotensin II receptor blockers has advantages over traditional anti-arrhythmic therapy; it is well tolerated by the patients and produced no serious side effects.
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PMID:[Preventive strategy for atrial fibrillation in arterial hypertension]. 2001 44

Endothelin-converting enzyme-1 (ECE-1) is a membrane-bound metalloprotease that cleaves biologically inactive big endothelin-1 (ET-1) into active ET-1. ET-1 is involved in the cardiovascular homeostasis and the development of cardiovascular diseases including pulmonary arterial hypertension and heart failure. Atrial natriuretic peptide (ANP) is an endogenous hormone that is released from the heart in response to myocardial stretch and overload. ANP was shown to be hydrolyzed by neutral endopeptidase 24.11 (NEP) which shares important structural features with ECE-1. Previous in vitro studies using recombinant soluble ECE-1 suggested that ECE-1 cleaved several biologically active peptides including ANP in addition to big ET-1. However, physiological relevance of ANP-degrading activity by ECE-1 has stayed unclear. Here, we aimed to investigate whether endogenous ECE-1 is able to hydrolyze ANP using live-cell based assay and ECE-1-deficient mice. Chinese hamster ovary (CHO) cells, which lack detectable levels of ECE activity, degraded ANP in the medium efficiently when transfected with ECE-1 cDNA. ANP peptide contents in the E14-15 embryos were significantly higher in ECE-1+/- mice compared with ECE-1+/+ mice. These observations strongly suggest that ECE-1 is involved in the physiological degradation of ANP in vivo. Thus, pharmacological inhibition of ECE-1 may provide a novel strategy to treat various cardiovascular diseases by suppressing and potentiating the ET and ANP pathway, respectively.
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PMID:Physiological relevance of hydrolysis of atrial natriuretic peptide by endothelin-converting enzyme-1. 2297 25


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