Intravenous morphine reduces plasma endothelin 1 concentration through activation of neutral endopeptidase 24.11 in patients with myocardial infarction

2001 ◽  
Vol 37 (5) ◽  
pp. 445-449 ◽  
Author(s):  
Tzong-Luen Wang ◽  
Hang Chang
Keyword(s):  
Myocardial Infarction ◽  
Neutral Endopeptidase ◽  
Endothelin 1 ◽  
Endopeptidase 24.11 ◽  
Intravenous Morphine

Imbalance between Neutral Endopeptidase 24.11 and Endothelin-1 Expression in Human Endometrial Carcinoma

Oncology ◽  
2001 ◽  
Vol 60 (3) ◽  
pp. 258-267 ◽  
Author(s):  
Takahiro Suzuki ◽  
Fumitaka Kikkawa ◽  
Kazuhiko Ino ◽  
Tetsuro Nagasaka ◽  
Koji Tamakoshi ◽  
...  
Keyword(s):  
Endometrial Carcinoma ◽  
Neutral Endopeptidase ◽  
Endothelin 1 ◽  
Endopeptidase 24.11

scholarly journals The hydrolysis of endothelins by neutral endopeptidase 24.11 (enkephalinase).

1990 ◽  
Vol 265 (24) ◽  
pp. 14150-14155
Author(s):  
J. Vijayaraghavan ◽  
A.G. Scicli ◽  
O.A. Carretero ◽  
C. Slaughter ◽  
C. Moomaw ◽  
...  
Keyword(s):  
Neutral Endopeptidase ◽  
Endopeptidase 24.11 ◽  
Hydrolysis Of

scholarly journals Left ventricular unloading before reperfusion reduces endothelin-1 release and calcium overload in porcine myocardial infarction

2008 ◽  
Vol 136 (2) ◽  
pp. 343-351 ◽  
Author(s):  
Sophie Tamareille ◽  
Hela Achour ◽  
James Amirian ◽  
Patricia Felli ◽  
Roger J. Bick ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Left Ventricular ◽  
Calcium Overload ◽  
Endothelin 1

Non-peptidic inhibitors of neutral endopeptidase 24.11 2. Design and pharmacology of orally active phosphonate prodrugs

1995 ◽  
Vol 5 (2) ◽  
pp. 151-154 ◽  
Author(s):  
Stéphane De Lombaer ◽  
Louis Blanchard ◽  
Carol Berry ◽  
Rajendra D. Ghai ◽  
Angelo J. Trapani
Keyword(s):  
Neutral Endopeptidase ◽  
Endopeptidase 24.11 ◽  
Peptidic Inhibitors ◽  
Orally Active

Active amino acids of the Kell blood group protein and model of the ectodomain based on the structure of neutral endopeptidase 24.11

Blood ◽  
2003 ◽  
Vol 102 (8) ◽  
pp. 3028-3034 ◽  
Author(s):  
Soohee Lee ◽  
Asim K. Debnath ◽  
Colvin M. Redman
Keyword(s):  
Amino Acids ◽  
Blood Group ◽  
Active Site ◽  
Neutral Endopeptidase ◽  
Site Directed Mutagenesis ◽  
Peptide Hydrolysis ◽  
Enzyme Active Site ◽  
Endopeptidase 24.11 ◽  
Outer Domain ◽  
Group Protein

Abstract In addition to its importance in transfusion, Kell protein is a member of the M13 family of zinc endopeptidases and functions as an endothelin-3–converting enzyme. To obtain information on the structure of Kell protein we built a model based on the crystal structure of the ectodomain of neutral endopeptidase 24.11 (NEP). Similar to NEP, the Kell protein has 2 globular domains consisting mostly of α-helical segments. The domain situated closest to the membrane contains both the N- and C-terminal sequences and the enzyme-active site. The outer domain contains all of the amino acids whose substitutions lead to different Kell blood group phenotypes. In the model, the zinc peptidase inhibitor, phosphoramidon, was docked in the active site. Site-directed mutagenesis of amino acids in the active site was performed and the enzymatic activities of expressed mutant Kell proteins analyzed and compared with NEP. Our studies indicate that Kell and NEP use the same homologous amino acids in the coordination of zinc and in peptide hydrolysis. However, Kell uses different amino acids than NEP in substrate binding and appears to have more flexibility in the composition of amino acids allowed in the active site.

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