Frex and frexH: Indicators of metabolic states in living cells

Bioengineered Bugs

Volumn 3, Issue 3, 2012, Pages 181-188

  Zhao, Yuzheng ^a   Yang, Yi ^a  

^a UNIVERSITY OF SHANGHAI FOR SCIENCE AND TECHNOLOGY   (China)

Author keywords

Electron transport chain; Genetically encoded sensor; Glucose; Hypoxia; Metabolic state; Reduced nicotinamide adenine dinucleotide (NADH); Subcellular distribution

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; BIOSENSOR; CELL COMPARTMENTALIZATION; CELL NUCLEUS; CONFOCAL MICROSCOPY; CYTOSOL; FLOW CYTOMETRY; FLUORESCENCE; FLUORESCENCE MICROSCOPY; GLUCOSE METABOLISM; GLYCOLYSIS; HUMAN; LIVER MITOCHONDRION; MAMMAL CELL; METABOLISM; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE PHOSPHORYLATION; QUANTITATIVE ANALYSIS; SENSITIVITY AND SPECIFICITY;

BIOSENSING TECHNIQUES; ELECTRON TRANSPORT; FLUORESCENCE; NAD;

EID: 84862747135     PISSN: 19491018     EISSN: 19491026     Source Type: Journal    
DOI: 10.4161/bbug.19769     Document Type: Article

References (35)

1. Wang H, Nakata E, Hamachi I. Recent progress in strategies for the creation of protein-based fluorescent biosensors. Chembiochem 2009; 10:2560-2577; PMID: 19693761; http://dx.doi.org/10.1002/cbic.200900249
2. Sakaue-Sawano A, Kurokawa H, Morimura T, Hanyu A, Hama H, Osawa H, et al. Visualizing spatiotemporal dynamics of multicellular cell-cycle progression. Cell 2008; 132:487-498; PMID:18267078; http://dx.doi.org/10.1016/j.cell.2007.12.033
3. Zhao Y, Araki S, Wu J, Teramoto T, Chang YF, Nakano M, et al. An expanded palette of genetically encoded Ca2 indicators. Science 2011; 333:1888-1891; PMID:21903779; http://dx.doi.org/10.1126/science. 1208592
4. Tsou P, Zheng B, Hsu CH, Sasaki AT, Cantley LC. A fluorescent reporter of AMPK activity and cellular energy stress. Cell Metab 2011; 13:476-486; PMID: 21459332; http://dx.doi.org/10.1016/j.cmet.2011.03.006
5. Arosio D, Ricci F, Marchetti L, Gualdani R, Albertazzi L, Beltram F. Simultaneous intracellular chloride and pH measurements using a GFP-based sensor. Nat Methods 2010; 7:516-518; PMID:20581829; http://dx.doi.org/10.1038/nmeth.1471
6. Imamura H, Nhat KP, Togawa H, Saito K, Iino R, Kato-Yamada Y, et al. Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators. Proc Natl Acad Sci U S A 2009; 106:15651-1566; PMID: 19720993; http://dx.doi.org/10.1073/pnas.0904764106
7. Kasischke KA, Vishwasrao HD, Fisher PJ, Zipfel WR, Webb WW. Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis. Science 2004; 305:99-103; PMID:15232110; http://dx.doi.org/10.1126/science.1096485
8. Eto K, Tsubamoto Y, Terauchi Y, Sugiyama T, Kishimoto T, Takahashi N, et al. Role of NADH shuttle system in glucose-induced activation of mitochondrial metabolism and insulin secretion. Science 1999; 283:981-985; PMID:9974390; http://dx.doi.org/10.1126/science.283.5404.981
9. Patterson GH, Knobel SM, Arkhammar P, Thastrup O, Piston DW. Separation of the glucose-stimulated cytoplasmic and mitochondrial NAD(P)H responses in pancreatic islet beta cells. Proc Natl Acad Sci U S A 2000; 97:5203-5207; PMID:10792038; http://dx.doi.org/10.1073/pnas.090098797
10. Rubi B, del Arco A, Bartley C, Sstrustegui J, Maechler P. The malate-aspartate NADH shuttle member Aralar1 determines glucose metabolic fate, mitochondrial activity, and insulin secretion in beta cells. J Biol Chem 2004; 279:55659-55666; PMID:15494407; http://dx.doi.org/10.1074/jbc.M409303200
11. Zhao Y, Jin J, Hu Q, Zhou HM, Yi J, Yu Z, et al. Genetically encoded fluorescent sensors for intracellular NADH detection. Cell Metab 2011; 14:555-566; PMID:21982715; http://dx.doi.org/10.1016/j.cmet.2011.09.004
12. McLaughlin KJ, Strain-Damerell CM, Xie K, Brekasis D, Soares AS, Paget MS, et al. Structural basis for NADH/NAD+ redox sensing by a Rex family repressor. Mol Cell 2010; 38:563-575; PMID:20513431; http://dx.doi.org/10.1016/j.molcel.2010.05.006
13. Mayevsky A. Mitochondrial function and energy metabolism in cancer cells: past overview and future perspectives. Mitochondrion 2009; 9:165-179; PMID: 19460294; http://dx.doi.org/10.1016/j.mito.2009.01.009
14. Joubert F, Fales HM, Wen H, Combs CA, Balaban RS. NADH enzyme-dependent fluorescence recovery after photobleaching (ED-FRAP): applications to enzyme and mitochondrial reaction kinetics, in vitro. Biophys J 2004; 86:629-645; PMID:14695307; http://dx.doi.org/10.1016/S0006-3495(04)74141-7
15. Yang H, Yang T, Baur JA, Perez E, Matsui T, Carmona JJ, et al. Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival. Cell 2007; 130:1095-1107; PMID:17889652; http://dx.doi.org/10.1016/j.cell.2007.07.035
16. Kasimova MR, Grigiene J, Krab K, Hagedorn PH, Flyvbjerg H, Andersen PE, et al. The free NADH concentration is kept constant in plant mitochondria under different metabolic conditions. Plant Cell 2006; 18:688-698; PMID:16461578; http://dx.doi.org/10.1105/tpc.105.039354
17. Henley KS, Laughrey EG. The redox state of the mitochondrial NAD system in cirrhosis of the liver and in chronic quantitative undernutrition in the rat. Biochim Biophys Acta 1970; 201:9-12; PMID: 4312780; http://dx.doi.org/10.1016/0304-4165(70) 90003-6
18. Williamson DH, Lund P, Krebs HA. The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 1967; 103:514-527; PMID:4291787
19. Zhang Q, Piston DW, Goodman RH. Regulation of corepressor function by nuclear NADH. Science 2002; 295:1895-7; PMID:11847309
20. Blinova K, Carroll S, Bose S, Smirnov AV, Harvey JJ, Knutson JR, et al. Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions. Biochemistry 2005; 44: 2585-94; PMID:15709771; http://dx.doi.org/10.1021/bi0485124
21. Yu Q, Heikal AA. Two-photon autofluorescence dynamics imaging reveals sensitivity of intracellular NADH concentration and conformation to cell physiology at the single-cell level. J Photochem Photobiol B 2009; 95:46-57; PMID:19179090; http://dx.doi.org/10.1016/j.jphotobiol.2008.12.010
22. Vishwasrao HD, Heikal AA, Kasischke KA, Webb WW. Conformational dependence of intracellular NADH on metabolic state revealed by associated fluorescence anisotropy. J Biol Chem 2005; 280:25119-25126; PMID:15863500; http://dx.doi.org/10.1074/jbc.M502475200
23. Wakita M, Nishimura G, Tamura M. Some characteristics of the fluorescence lifetime of reduced pyridine nucleotides in isolated mitochondria, isolated hepatocytes, and perfused rat liver in situ. J Biochem 1995; 118:1151-1160; PMID:8720129
24. Corcoran JA, Saffran HA, Duguay BA, Smiley JR. Herpes simplex virus UL12.5 targets mitochondria through a mitochondrial localization sequence proximal to the N terminus. J Virol 2009; 83:2601-2610; PMID: 19129438; http://dx.doi.org/10.1128/JVI.02087-08
25. Ying W, Sevigny MB, Chen Y, Swanson RA. Poly (ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death. Proc Natl Acad Sci U S A 2001; 98:12227-12232; PMID:11593040; http://dx.doi.org/10.1073/pnas.211202598
26. Szabó C, Zingarelli B, O'Connor M, Salzman AL. DNA strand breakage, activation of poly (ADP-ribose) synthetase, and cellular energy depletion are involved in the cytotoxicity of macrophages and smooth muscle cells exposed to peroxynitrite. Proc Natl Acad Sci U S A 1996; 93:1753-1758; PMID:8700830; http://dx.doi.org/10.1073/pnas.93.5.1753
27. Thornburg JM, Nelson KK, Clem BF, Lane AN, Arumugam S, Simmons A, et al. Targeting aspartate aminotransferase in breast cancer. Breast Cancer Res 2008; 10:R84; PMID:18922152; http://dx.doi.org/10.1186/bcr2154
28. Ying W. NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences. Antioxid Redox Signal 2008; 10:179-206; PMID:18020963; http://dx.doi.org/10.1089/ars.2007.1672
29. Lu H, Burns D, Garnier P, Wei G, Zhu K, Ying W. P2X7 receptors mediate NADH transport across the plasma membranes of astrocytes. Biochem Biophys Res Commun 2007; 362:946-950; PMID:17803959; http://dx.doi.org/10.1016/j.bbrc.2007.08.095
30. Chance B, Williams GR. Respiratory enzymes in oxidative phosphorylation. III. The steady state. J Biol Chem 1955; 217:409-427; PMID:13271404
31. Mayevsky A, Rogatsky GG. Mitochondrial function in vivo evaluated by NADH fluorescence: from animal models to human studies. Am J Physiol Cell Physiol 2007; 292:C615-40; PMID:16943239; http://dx.doi.org/10.1152/ajpcell.00249.2006
32. Zhang Q, Wang SY, Nottke AC, Rocheleau JV, Piston DW, Goodman RH. Redox sensor CtBP mediates hypoxia-induced tumor cell migration. Proc Natl Acad Sci U S A 2006; 103:9029-9033; PMID:16740659; http://dx.doi.org/10.1073/pnas.0603269103
33. Crawford RM, Jovanović S, Budas GR, Davies AM, Lad H, Wenger RH, et al. Chronic mild hypoxia protects heart-derived H9c2 cells against acute hypoxia/reoxygenation by regulating expression of the SUR2A subunit of the ATP-sensitive K+ channel. J Biol Chem 2003; 278:31444-31455; PMID:12791696; http://dx.doi.org/10.1074/jbc.M303051200
34. Hung YP, Albeck JG, Tantama M, Yellen G. Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor. Cell Metab 2011; 14:545-554; PMID:21982714; http://dx.doi.org/10.1016/j.cmet.2011.08.012
35. Berg J, Hung YP, Yellen G. A genetically encoded fluorescent reporter of ATP:ADP ratio. Nat Methods 2009; 6:161-166; PMID:19122669; http://dx.doi.org/10.1038/nmeth.1288