FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Published as doi: 10.1096/fj.06-7489com.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
fj.06-7489comv1
21/4/1137    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Beck, V.
Right arrow Articles by Pohl, E. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Beck, V.
Right arrow Articles by Pohl, E. E.
(The FASEB Journal. 2007;21:1137-1144.)
© 2007 FASEB

Polyunsaturated fatty acids activate human uncoupling proteins 1 and 2 in planar lipid bilayers

Valeri Beck*, Martin Jaburek{dagger}, Tatiana Demina*,1, Anne Rupprecht*, Richard K. Porter{ddagger}, Petr Jezek{dagger} and Elena E. Pohl*,2

* Institute of Cell Biology and Neurobiology, Centre for Anatomy, Charité Universitätsmedizin, Berlin, Germany;

{dagger} Department of Membrane Transport Biophysics, Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic; and

{ddagger} School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland

2Correspondence: Institute of Cell Biology and Neurobiology, Charité Universitätsmedizin, Charitéplatz 1, 10117 Berlin, Germany. E-mail: elena.pohl{at}charite.de

Uncoupling proteins 1 (UCP1) and 2 (UCP2) belong to the family of mitochondrial anion transporters and share 59% sequence identity with each other. Whereas UCP1 was shown to be responsible for the rapid production of heat in brown adipose tissue, the primary function and transport properties of ubiquitously expressed UCP2 are controversially discussed. Here, for the first time, the activation pattern of the recombinant human UCP2 in comparison to the recombinant human UCP1 are studied using a well-defined system of planar lipid bilayers. It is shown that despite apparently different physiological functions, hUCP2 exhibited its protonophoric function similar to hUCP1—exclusively in the presence of long-chain fatty acids (FA). The calculated hUCP2 transport rate of 4.5 s–1 is the same order of magnitude, as shown previously for UCP1. It leads to the conclusion that the differences in the activity of both proteins in living mitochondria are based exclusively on their different expression level. Both proteins are activated much more effectively by polyunsaturated than by saturated FA. The proton and total membrane conductances increased in the range palmitic < oleic < eicosatrienoic < linoleic < retinoic < arachidonic acids. The higher uncoupling protein (UCP)—dependent conductance in the presence of polyunsaturated FA is explained on the basis of the FA cycling hypothesis.—Beck, V., Jaburek, M., Demina, T., Rupprecht, A., Porter, R. K., Jezek, P., Pohl, E. E. Polyunsaturated fatty acids activate human uncoupling proteins 1 and 2 in planar lipid bilayers.


Key Words: mitochondria • anion transporter • proton transport • artificial bilayer membranes • reactive oxygen species




This article has been cited by other articles:


Home page
Am. J. Physiol. Endocrinol. Metab.Home page
N. Tsuboyama-Kasaoka, K. Sano, C. Shozawa, T. Osaka, and O. Ezaki
Studies of UCP2 transgenic and knockout mice reveal that liver UCP2 is not essential for the antiobesity effects of fish oil
Am J Physiol Endocrinol Metab, March 1, 2008; 294(3): E600 - E606.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2007 by The Federation of American Societies for Experimental Biology.