Am J Physiol Cell Physiol Add DOIs to your references at manuscript stage!
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Cell Physiol 291: C1172-C1182, 2006. First published June 28, 2006; doi:10.1152/ajpcell.00195.2006
0363-6143/06 $8.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
291/6/C1172    most recent
00195.2006v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Benard, G.
Right arrow Articles by Rossignol, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Benard, G.
Right arrow Articles by Rossignol, R.

MITOCHONDRIAL MODELING AND FUNCTION

Physiological diversity of mitochondrial oxidative phosphorylation

G. Benard,1 B. Faustin,1 E. Passerieux,1 A. Galinier,2 C. Rocher,1 N. Bellance,1 J.-P. Delage,1 L. Casteilla,2 T. Letellier,1 and R. Rossignol1

1INSERM, U688 Physiopathologie Mitochondriale, Université Victor Segalen-Bordeaux 2, Bordeaux, France; and 2IFR 31, Institut Louis Bugnard, BP 84225, UMR 5018 CNRS UPS, Toulouse, France

Submitted 20 April 2006 ; accepted in final form 7 June 2006

To investigate the physiological diversity in the regulation and control of mitochondrial oxidative phosphorylation, we determined the composition and functional features of the respiratory chain in muscle, heart, liver, kidney, and brain. First, we observed important variations in mitochondrial content and infrastructure via electron micrographs of the different tissue sections. Analyses of respiratory chain enzyme content by Western blot also showed large differences between tissues, in good correlation with the expression level of mitochondrial transcription factor A and the activity of citrate synthase. On the isolated mitochondria, we observed a conserved molar ratio between the respiratory chain complexes and a variable stoichiometry for coenzyme Q and cytochrome c, with typical values of [1–1.5]:[30–135]:[3]:[9–35]:[6.5–7.5] for complex II:coenzyme Q:complex III:cytochrome c:complex IV in the different tissues. The functional analysis revealed important differences in maximal velocities of respiratory chain complexes, with higher values in heart. However, calculation of the catalytic constants showed that brain contained the more active enzyme complexes. Hence, our study demonstrates that, in tissues, oxidative phosphorylation capacity is highly variable and diverse, as determined by different combinations of 1) the mitochondrial content, 2) the amount of respiratory chain complexes, and 3) their intrinsic activity. In all tissues, there was a large excess of enzyme capacity and intermediate substrate concentration, compared with what is required for state 3 respiration. To conclude, we submitted our data to a principal component analysis that revealed three groups of tissues: muscle and heart, brain, and liver and kidney.

respiratory chain; tissues; stoichiometry; cytochrome c; coenzyme Q



Address for reprint requests and other correspondence: R. Rossignol, INSERM U688, Physiopathologie mitochondriale, Université Victor Segalen-Bordeaux 2, 146 rue Léo-Saignat, F-33076 Bordeaux Cedex, France (e-mail: rossig{at}u-bordeaux2.fr)




This article has been cited by other articles:


Home page
QJMHome page
A.M. Hall, R.J. Unwin, M.G. Hanna, and M.R. Duchen
Renal function and mitochondrial cytopathy (MC): more questions than answers?
QJM, October 1, 2008; 101(10): 755 - 766.
[Abstract] [Full Text] [PDF]


Home page
Clin. Cancer Res.Home page
J. A. Mayr, D. Meierhofer, F. Zimmermann, R. Feichtinger, C. Kogler, M. Ratschek, N. Schmeller, W. Sperl, and B. Kofler
Loss of Complex I due to Mitochondrial DNA Mutations in Renal Oncocytoma
Clin. Cancer Res., April 15, 2008; 14(8): 2270 - 2275.
[Abstract] [Full Text] [PDF]


Home page
JEMHome page
T. Trian, G. Benard, H. Begueret, R. Rossignol, P.-O. Girodet, D. Ghosh, O. Ousova, J.-M. Vernejoux, R. Marthan, J.-M. Tunon-de-Lara, et al.
Bronchial smooth muscle remodeling involves calcium-dependent enhanced mitochondrial biogenesis in asthma
J. Exp. Med., December 24, 2007; 204(13): 3173 - 3181.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
G. Benard, N. Bellance, D. James, P. Parrone, H. Fernandez, T. Letellier, and R. Rossignol
Mitochondrial bioenergetics and structural network organization
J. Cell Sci., March 1, 2007; 120(5): 838 - 848.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2006 by the American Physiological Society.