Jump to ContentJump to Main Navigation
Show Summary Details

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

249,00 € / $374.00 / £187.00*

See all formats and pricing



Select Volume and Issue
Loading journal volume and issue information...

Signal transduction in CHO cells stably transfected with domain-selective forms of murine ACE

Xiaoou Sun1, 2 / Brit Rentzsch3 / Maolian Gong3 / Jenny Eichhorst1 / Kristin Pankow1, 2 / Gisela Papsdorf1 / Björn Maul1 / Michael Bader3 / Wolf-Eberhard Siems1

1Leibniz-Institut für Molekulare Pharmakologie, D-13125 Berlin, Germany

2Charité, Universitätsmedizin Berlin, D-13353 Berlin, Germany

3Max-Delbrück Center for Molecular Medicine, D-13125 Berlin, Germany

Corresponding author

Citation Information: Biological Chemistry. Volume 391, Issue 2/3, Pages 235–244, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/bc.2010.020, December 2009

Publication History

Published Online:


Membrane-bound human angiotensin-converting enzyme (ACE) has been reported to initiate intracellular signaling after interaction with substrates or inhibitors. Somatic ACE is known to contain two distinct, extracellular catalytic centers. We analyzed the signal transduction mechanisms in cells transfected with different forms of murine ACE (mACE) and investigated whether the two domains are similarly involved in these processes. For this purpose, CHO cells were stably transfected with mACE or with its domain-selective mutants. In addition to these modified cellular models, human umbilical vein endothelial cells were used in this study. Signal transduction molecules such as JNK and c-Jun were analyzed after activation of cells with several ACE substrates and inhibitors. ACE-targeting compounds such as substrates, inhibitors, or even the ACE product angiotensin-II induce in mACE-expressing cells a signal transduction response. These processes are also evoked by partially inactivated forms of mACE and finally result in an enhanced cyclooxygenase-2 transcription. Surprisingly, the membrane-bound ACE activity is also influenced by ACE-targeted interventions. Our data suggest that the two catalytic domains of mACE do not function independently but that the signal transduction is influenced by negative cooperativity of the two catalytic domains. This study underlines that ACE indeed has receptor-like properties which occur in a species-specific manner.

Keywords: ACE domains; angiotensin-converting enzyme; CHO cells; c-Jun; HUVEC cells; JNK

Comments (0)

Please log in or register to comment.