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Cardiovascular Research 2006 71(2):195-207; doi:10.1016/j.cardiores.2006.04.008
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Copyright © 2006, European Society of Cardiology

The good, the bad and the ugly in oxygen-sensing: ROS, cytochromes and prolyl-hydroxylases

Till Ackera, Joachim Fandreyb and Helmut Ackerb,*

aNeurologisches Institut (Edinger Institut), Klinikum der J.W. Goethe Universität Frankfurt am Main, Deutschordenstr. 46, D-60528 Frankfurt, Germany
bInstitut für Physiologie, Universität Duisburg-Essen, Hufelandstr. 55 IG1, D-45147 Essen, Germany

* Corresponding author. Email address: helmut.acker{at}uni-essen.de

Current concepts of cellular oxygen-sensing include an isoform of the neutrophil NADPH oxidase, different electron carrier units of the mitochondrial electron transport chain (ETC), heme oxygenase-2 (HO-2), and a subfamily of 2-oxoglutarate dependent dioxygenases termed HIF (hypoxia inducible factor) prolyl hydroxylases (PHDs) and HIF asparagyl hydroxylase FIH-1 (factor-inhibiting HIF). Different oxygen sensitivities, cell-specific distribution and subcellular localization of specific oxygen-sensing cascades involving reactive oxygen species (ROS) as second messengers may help to tailor various adaptive responses according to differences in tissue oxygen availability. Herein, we propose an integrated model for these various oxygen-sensing mechanisms that very efficiently regulate HIF-{alpha} activity and plasma membrane potassium-channel (PMPC) conductivity.

KEYWORDS ROS; HIF; PHD; Cytochromes; Ion channels; Oxygen-sensing

Time for primary review 23 days


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