Differential inhibition of wild-type endothelin-converting enzyme-1 and its mutants

Journal of Cardiovascular Pharmacology

Volumn 31, Issue SUPPL. 1, 1998, Pages

  Savage, Paula ^a   De Lombaert, Stéphane ^a   Shimada, Kohei ^b   Tanzawa, Kazuhiko ^b   Jeng, Arco Y ^a  

^a NOVARTIS PHARMA AG   (Switzerland)

^b DAIICHI SANKYO CO   (Japan)

Author keywords

CGS 26303; CGS 31447; Endothelin converting enzyme; Mutants; Phosphoramidon; Zinc metalloprotease inhibitor

Indexed keywords

ASPARTIC PROTEINASE; ENDOTHELIN CONVERTING ENZYME; ENDOTHELIN-CONVERTING ENZYME 1; METALLOPROTEINASE; PROTEINASE INHIBITOR;

ANIMAL; ARTICLE; DRUG ANTAGONISM; GENETICS; HUMAN; MUTATION; PHYSIOLOGY; RAT; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ANIMALS; ASPARTIC ENDOPEPTIDASES; HUMANS; METALLOENDOPEPTIDASES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEASE INHIBITORS; RATS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031627569     PISSN: 01602446     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005344-199800001-00007     Document Type: Article

References (6)

1. Rubanyi GM, Polokoff MA. Endothelins: molecular biology, biochemistry, pharmacology, physiology, and pathophysiology. Pharmacol Rev 1994;46:325-415.
2. Turner AJ, Murphy LJ. Molecular pharmacology of endothelin converting enzymes. Biochem Pharmacol 1996;51:91-102.
3. 412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11. Biochem J 1996;315: 863-7.
4. Trapani AJ, Balwierczak JL, Lappe RW, et al. Effects of metalloprotease inhibitors on the conversion of proendothelin-1 to endothelin-1. Biochem Mol Biol Int 1993;31:861-7.
5. Savage P, Jeng AY. Quantitation of plasma endothelins. Anal Biochem 1993;213:434-6.
6. De Lombaert S, Stamford LB, Blanchard L, et al. Potent non-peptidic dual inhibitors of endothelin-converting enzyme and neutral endopeptidase 24.11. Bioorg Med Chem Lett 1997;7:1059-64.