Related ArticlesFutile cycling of lactate through the plasma membrane of C6 glioma cells as detected by (13C, 2H) NMR.
J Neurosci Res. 2005 Jan 1-15;79(1-2):119-27
Authors: Rodrigues TB, Gray HL, Benito M, Garrido S, Sierra A, Geraldes CF, Ballesteros P, Cerdán S
We report a novel ((13)C, (2)H) nuclear magnetic resonance (NMR) procedure to investigate lactate recycling through the monocarboxylate transporter of the plasma membrane of cells in culture. C6 glioma cells were incubated with [3-(13)C]lactate in Krebs-Henseleit Buffer containing 50% (2)H(2)O (vol/vol) for up to 30 hr. (13)C NMR analysis of aliquots progressively taken from the medium, showed: (1) a linearly decreasing singlet at approximately 20.85 parts per million (ppm; -0.119 micromol/mg protein/hr) derived from the methyl carbon of [3-(13)C]lactate; and (2) an exponentially increasing shifted singlet at approximately 20.74 ppm (0.227 micromol/ mg protein/hr) from the methyl carbon of [3-(13)C, 2-(2)H]lactate. The shifted singlet appears because during its transit through the cytosol, [3-(13)C]lactate generates [3-(13)C, 2-(2)H]lactate in the lactate dehydrogenase (LDH) equilibrium, which may return to the incubation medium through the reversible monocarboxylate carrier. The methyl group of [3-(13)C, 2-(2)H]lactate is shifted -0.11 ppm with respect to that of [3-(13)C]lactate, making it possible to distinguish between both molecules by (13)C NMR. During incubations with 2.5 mM [1-(13)C]glucose and 3.98 mM [U-(13)C(3)]lactate or with 2.5 mM [1-(13)C]glucose and 3.93 mM [2-(13)C]pyruvate, C2-deuterated lactate was produced only from [1-(13)C]glucose or [U-(13)C(3)]lactate, revealing that this deuteration process is redox sensitive. When [1-(13)C]glucose and [U-(13)C(3)]lactate were used as substrates, no significant [3-(13)C]lactate production from [1-(13)C]glucose was detected, suggesting that glycolytic lactate production may be stopped under the high lactate concentrations prevailing under mild hypoxic or ischemic episodes or during cerebral activation.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 20;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
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Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 14;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
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[NMR paper] Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Related Articles Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
J Am Chem Soc. 2005 Sep 7;127(35):12263-72
Authors: Vogel A, Katzka CP, Waldmann H, Arnold K, Brown MF, Huster D
The human N-ras protein binds to cellular membranes by insertion of two covalently bound posttranslational lipid modifications, which is crucial for its...
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[NMR paper] PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from b
PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from bilayer mixtures with phosphatidylcholine: a (2)H-NMR study.
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Biophys J. 2000 Nov;79(5):2624-31
Authors: Roux M, Beswick V, Coïc YM, Huynh-Dinh T, Sanson A, Neumann JM
PMP1 is a 38-residue plasma membrane protein of the yeast Saccharomyces cerevisiae that regulates the activity of the H(+)-ATPase. The...
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[NMR paper] Glucose and glutamine metabolism in C6 glioma cells studied by carbon 13 NMR.
Glucose and glutamine metabolism in C6 glioma cells studied by carbon 13 NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Glucose and glutamine metabolism in C6 glioma cells studied by carbon 13 NMR.
Biochimie. 1996;78(3):155-64
Authors: Portais JC, Voisin P, Merle M, Canioni P
The question as to whether glutamine and glucose are both required for optimal growth of glioma cells is studied through the role of these substrates on the metabolism of the cells. C6 rat...
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[NMR paper] A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydro
A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
Biochemistry. 1996 Dec 24;35(51):16502-9
Authors: Sun ZY, Pratt EA, Simplaceanu V, Ho C
Partially folded protein intermediates have been observed by 19F-NMR spectroscopy during the equilibrium unfolding of the...
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[NMR paper] A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escheric
A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
Protein Sci. 1993 Nov;2(11):1938-47
Authors: Sun ZY, Truong HT, Pratt EA, Sutherland DC,...
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[NMR paper] Transduction of reducing power across the plasma membrane by reduced glutathione. A 1
Transduction of reducing power across the plasma membrane by reduced glutathione. A 1H-NMR spin-echo study of intact human erythrocytes.
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 Transduction of reducing power across the plasma membrane by reduced glutathione. A 1H-NMR spin-echo study of intact human erythrocytes.
Eur J Biochem. 1993 Aug 1;215(3):711-8
Authors: Ciriolo MR, Paci M, Sette M, De Martino A, Bozzi A, Rotilio G
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Futile cycling of lactate through the plasma membrane of C6 glioma cells as detected
Linear Mode
