Am J Physiol Cell Physiol AJP: Endocrinology and Metabolism
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Cell Physiol 279: C1704-C1709, 2000;
0363-6143/00 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Web of Science
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 Web of Science (8)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Griffin, J. L.
Right arrow Articles by Lewandowski, E. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Griffin, J. L.
Right arrow Articles by Lewandowski, E. D.
Vol. 279, Issue 6, C1704-C1709, December 2000

Postnatal expression and activity of the mitochondrial 2-oxoglutarate-malate carrier in intact hearts

J. L. Griffin1, J. M. O'Donnell1, L. T. White1, R. J. Hajjar2, and E. D. Lewandowski1,2

Metabolic Research Laboratory, 1 Departments of Radiology and 2 Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts

This study examines the functional implications of postnatal changes in the expression of the mitochondrial transporter protein, 2-oxoglutarate-malate carrier (OMC). Online 13C nuclear magnetic resonance (13C NMR) measurements of isotope kinetics in hearts from neonate (3-4 days) and adult rabbits provided tricarboxylic acid cycle flux rates and flux rates through OMC. Neonate and adult hearts oxidizing 2.5 mM [2,4-13C2]butyrate were subjected to either normal or high cytosolic redox state (2.5 mM lactate) conditions to evaluate the recruitment of malate-aspartate activity and the resulting OMC flux. During development from neonate (3-4 days) to adult, mitochondrial protein density in the heart increased from 19 ± 3% to 31 ± 2%, whereas OMC expression decreased by 65% per mitochondrial protein content (P < 0.05). Correspondingly, OMC flux was lower in adults hearts than in neonates by 73% (neonate = 7.4 ± 0.4, adult = 2.0 ± 0.1 µmol/min per 100 mg mitochondrial protein; P < 0.05). Despite clear changes in OMC content and flux, the responsiveness of the malate-aspartate shuttle to increased cytosolic NADH was similar in both adults and neonates with an approximate threefold increase in OMC flux (in densitometric units/100 mg mitochondrial protein: neonate = 25.8 ± 2.5, adult = 6.0 ± 0.2; P < 0.05). The 13C NMR data demonstrate that OMC activity is a principal component of the rate of labeling of glutamate.

functional expression; tricarboxylic acid cycle; nuclear magnetic resonance spectroscopy; mitochondria; metabolism


This article has been cited by other articles:


Home page
NeoReviewsHome page
T. D. Scholz and J. L. Segar
Cardiac Metabolism in the Fetus and Newborn
NeoReviews, March 1, 2008; 9(3): e109 - e118.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
E. D. Lewandowski, J. M. O'Donnell, T. D. Scholz, N. Sorokina, and P. M. Buttrick
Recruitment of NADH shuttling in pressure-overloaded and hypertrophic rat hearts
Am J Physiol Cell Physiol, May 1, 2007; 292(5): C1880 - C1886.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. Contreras, P. Gomez-Puertas, M. Iijima, K. Kobayashi, T. Saheki, and J. Satrustegui
Ca2+ Activation Kinetics of the Two Aspartate-Glutamate Mitochondrial Carriers, Aralar and Citrin: ROLE IN THE HEART MALATE-ASPARTATE NADH SHUTTLE
J. Biol. Chem., March 9, 2007; 282(10): 7098 - 7106.
[Abstract] [Full Text] [PDF]


Home page
Physiol. Rev.Home page
J. Satrustegui, B. Pardo, and A. del Arco
Mitochondrial Transporters as Novel Targets for Intracellular Calcium Signaling
Physiol Rev, January 1, 2007; 87(1): 29 - 67.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
J. M. O'Donnell, R. K. Kudej, K. F. LaNoue, S. F. Vatner, and E. D. Lewandowski
Limited transfer of cytosolic NADH into mitochondria at high cardiac workload
Am J Physiol Heart Circ Physiol, June 1, 2004; 286(6): H2237 - H2242.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. L. Garcia-Martin, M. A. Garcia-Espinosa, P. Ballesteros, M. Bruix, and S. Cerdan
Hydrogen Turnover and Subcellular Compartmentation of Hepatic [2-13C]Glutamate and [3-13C]Aspartate as Detected by 13C NMR
J. Biol. Chem., March 1, 2002; 277(10): 7799 - 7807.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online