Related ArticlesAssessment of mitochondrial energy coupling in vivo by 13C/31P NMR.
Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6880-4
Authors: Jucker BM, Dufour S, Ren J, Cao X, Previs SF, Underhill B, Cadman KS, Shulman GI
The recently cloned uncoupling protein homolog UCP3 is expressed primarily in muscle and therefore may play a significant role in the regulation of energy expenditure and body weight. However, investigation into the regulation of uncoupling protein has been hampered by the inability to assess its activity in vivo. In this report, we demonstrate the use of a noninvasive NMR technique to assess mitochondrial energy uncoupling in skeletal muscle of awake rats by combining (13)C NMR to measure rates of mitochondrial substrate oxidation with (31)P NMR to assess unidirectional ATP synthesis flux. These combined (31)P/(13)C NMR measurements were performed in control, 10-day triiodo-l-thyronine (T(3))-treated (model of increased UCP3 expression), and acute 2,4-dinitrophenol (DNP)-treated (protonophore and mitochondrial uncoupler) rats. UCP3 mRNA and protein levels increased 8.1-fold (+/- 1.1) and 2.8-fold (+/- 0.8), respectively, in the T(3)-treated vs. control rat gastrocnemius muscle. (13)C NMR measurements of tricarboxylic acid cycle flux as an index of mitochondrial substrate oxidation were 61 +/- 21, 148 +/- 25, and 310 +/- 48 nmol/g per min in the control, T(3), and DNP groups, respectively. (31)P NMR saturation transfer measurements of unidirectional ATP synthesis flux were 83 +/- 14, 84 +/- 14, and 73 +/- 7 nmol/g per s in the control, T(3), and DNP groups, respectively. Together, these flux measurements, when normalized to the control group, suggest that acute administration of DNP (mitochondrial uncoupler) and chronic administration of T(3) decrease energy coupling by approximately 80% and approximately 60%, respectively, and that the latter treatment correlates with an increase in UCP3 mRNA and protein expression. This NMR approach could prove useful for exploring the regulation of uncoupling protein activity in vivo and elucidating its role in energy metabolism and obesity.
[NMR paper] NMR identification of the Tom20 binding segment in mitochondrial presequences.
NMR identification of the Tom20 binding segment in mitochondrial presequences.
Related Articles NMR identification of the Tom20 binding segment in mitochondrial presequences.
J Mol Biol. 2001 Feb 16;306(2):137-43
Authors: Muto T, Obita T, Abe Y, Shodai T, Endo T, Kohda D
Many mitochondrial proteins are synthesized in the cytosol as precursors with N-terminal presequences, and are imported into mitochondria with the aid of translocator protein complexes containing presequence-binding proteins. Tom20, a receptor protein which functions in an...
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[NMR paper] 13C/31P NMR assessment of mitochondrial energy coupling in skeletal muscle of awake f
13C/31P NMR assessment of mitochondrial energy coupling in skeletal muscle of awake fed and fasted rats. Relationship with uncoupling protein 3 expression.
Related Articles 13C/31P NMR assessment of mitochondrial energy coupling in skeletal muscle of awake fed and fasted rats. Relationship with uncoupling protein 3 expression.
J Biol Chem. 2000 Dec 15;275(50):39279-86
Authors: Jucker BM, Ren J, Dufour S, Cao X, Previs SF, Cadman KS, Shulman GI
To examine the relationship between mitochondrial energy coupling in skeletal muscle and change in...
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[NMR paper] Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied b
Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied by spin-label ESR and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied by spin-label ESR and NMR spectroscopy.
Eur J Biochem. 1992 Oct 1;209(1):423-30
Authors: Hayer-Hartl M, Schägger H, von Jagow G, Beyer K
Protein/phospholipid interactions in the...
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[NMR paper] Conformational analysis of a mitochondrial presequence derived from the F1-ATPase bet
Conformational analysis of a mitochondrial presequence derived from the F1-ATPase beta-subunit by CD and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Conformational analysis of a mitochondrial presequence derived from the F1-ATPase beta-subunit by CD and NMR spectroscopy.
Biochim Biophys Acta. 1992 Sep 4;1159(1):81-93
Authors: Bruch MD, Hoyt DW
Previous studies on mitochondrial targeting presequences have indicated that formation of an amphiphillic...
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[NMR paper] A 31P NMR study of mitochondrial inorganic phosphate visibility: effects of Ca2+, Mn2
A 31P NMR study of mitochondrial inorganic phosphate visibility: effects of Ca2+, Mn2+, and the pH gradient.
Related Articles A 31P NMR study of mitochondrial inorganic phosphate visibility: effects of Ca2+, Mn2+, and the pH gradient.
Biochemistry. 1992 Feb 11;31(5):1322-30
Authors: Hutson SM, Williams GD, Berkich DA, LaNoue KF, Briggs RW
The effects of external pH, temperature, and Ca2+ and Mn2+ concentrations on the compartmentation and NMR visibility of inorganic phosphate (Pi) were studied in isolated rat liver mitochondria respiring on...
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[NMR paper] 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenin
31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Related Articles 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Biochemistry. 1991 Aug 27;30(34):8351-7
Authors: Masiakos PT, Williams GD, Berkich DA, Smith MB, LaNoue KF
The exchange of intramitochondrial ATP (ATP(in)) for extramitochondrial ATP (ATP(out)) was measured by using 31P NMR spectroscopy over a range of temperatures in isolated rat liver mitochondria oxidizing...
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Assessment of GABARAP self-association by its diffusion properties
Abstract Gamma-aminobutyric acid type A receptor-associated protein (GABARAP) belongs to a family of small ubiquitin-like adaptor proteins implicated in intracellular vesicle trafficking and autophagy. We have used diffusion-ordered nuclear magnetic resonance spectroscopy to study the temperature and concentration dependence of the diffusion properties of GABARAP. Our data suggest the presence of distinct conformational states and provide support for self-association of GABARAP molecules. Assuming a monomerâ??dimer equilibrium, a temperature-dependent dissociation constant could be derived....
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NMR RPF: new NMR quality assessment scores
Protein NMR recall, precision, and F-measure scores (RPF scores): structure quality assessment measures based on information retrieval statistics.
Huang YJ, Powers R, Montelione GT.
Center for Advanced Biotechnology and Medicine and Department of Molecular Biology and Biochemistry, Rutgers University, Northeast Structural Genomics Consortium, and Robert Wood Johnson Medical School, Piscataway, New Jersey 08854-5368, USA.
J Am Chem Soc. 2005 Feb 16;127(6):1665-74.
Abstract:
Assessment of mitochondrial energy coupling in vivo by 13C/31P NMR.
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