Malondialdehyde inhibits an AMPK-mediated nuclear translocation and repression activity of ALDH2 in transcription

Biochemical and Biophysical Research Communications

Volumn 404, Issue 1, 2011, Pages 400-406

  Choi, Ji Woong ^a   Kim, Jae Hwan ^a   Cho, Sung Chun ^a   Ha, Moon Kyung ^a   Song, Kye Yong ^b   Youn, Hong Duk ^a   Park, Sang Chul ^a  

^a Seoul National University College of Medicine   (South Korea)

^b Chung Ang University College of Medicine   (South Korea)

Author keywords

Aging; Aldehyde dehydrogenase 2 (ALDH2); AMP activated protein kinase (AMPK); Histone deacetylase (HDAC); Malondialdehyde (MDA)

Indexed keywords

ADENYLATE KINASE; ALDEHYDE DEHYDROGENASE ISOENZYME 2; MALONALDEHYDE;

AGING; ANIMAL TISSUE; ARTICLE; CELL NUCLEUS; CELL STRAIN HEK293; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; FEMALE; IN VITRO STUDY; KIDNEY; NONHUMAN; PRIORITY JOURNAL; RAT;

ACTIVE TRANSPORT, CELL NUCLEUS; AGING; ALDEHYDE DEHYDROGENASE; AMP-ACTIVATED PROTEIN KINASES; ANIMALS; CELL NUCLEUS; FEMALE; GENE EXPRESSION REGULATION; HISTONE DEACETYLASES; MALONDIALDEHYDE; MITOCHONDRIAL PROTEINS; OXIDATIVE STRESS; RATS; RATS, SPRAGUE-DAWLEY; REPRESSOR PROTEINS; TRANSCRIPTION, GENETIC;

RATTUS;

EID: 78650922762     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.11.131     Document Type: Article

References (26)

1. Harman D. Free radical theory of aging. Antioxid. Redox Signal. 2004, 5:557-561.
2. Gómez-Sánchez A., Hermosín I., Maya I. Cleavage and oligomerization of malondialdehyde under physiological conditions. Tetrahedron Lett. 1990, 31:4077-4080.
3. Hurley T.D., Edenberg H.J., Li T.K. Pharmacogenomics: The Search for Individualized Therapies. Culinary and Hospitality Industry Publications Services 2002, 417-441. Weinheim, Germany. J. Licinio, M.L. Wong (Eds.).
4. Yoshida A. Genetic polymorphisms of alcohol metabolizing enzymes related to alcohol sensitivity and alcoholic diseases. Alcohol Alcohol. 1994, 29:693-696.
5. Kitagawa K., Kawamoto T., Kunugita N., Tsukiyama T., Okamoto K., Yoshida A., Nakayama K., Nakayama K.I. Aldehyde dehydrogenase (ALDH) 2 associates with oxidation of methoxyacetaldehyde; in vitro analysis with liver subcellular fraction derived from human and Aldh2 gene targeting mouse. FEBS Lett. 2000, 476:306-311.
6. Chen J.J., Yu B.P. Detoxication of reactive aldehydes in mitochondria: effect of age and dietary restriction. Aging 1996, 8:334-340.
7. Corton J.M., Gillespie J.G., Hardie D.G. Role of the AMP-activated protein kinase in the cellular stress response. Curr. Biol. 1994, 4:315-324.
8. Hardie D.G., Carling D. The AMP-activated protein kinase: fuel gauge of the mammalian cell. Eur. J. Biochem. 1997, 246:259-273.
9. Hardie D.G., Carling D., Carlson M. The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell?. Annu. Rev. Biochem. 1998, 67:821-855.
10. Hardie D.G., Scott J.W., Pan D.A., Hudson E.R. Management of cellular energy by the AMP-activated protein kinase system. FEBS Lett. 2003, 546:113-120.
11. Kemp B.E., Mitchelhill K.I., Stapleton D., Michell B.J., Chen Z.P., Witters L.A. Dealing with energy demand: the AMP-activated protein kinase. Trends Biochem. Sci. 1999, 24:22-25.
12. Foretz M., Carling D., Guichard C., Ferre P., Foufelle F. AMP-activated protein kinase inhibits the glucose-activated expression of fatty acid synthase gene in rat hepatocytes. J. Biol. Chem. 1998, 273:14767-14771.
13. Leclerc I., Kahn A., Doiron B. The AMP-activated protein kinase inhibits the transcriptional stimulation by glucose in liver cells acting through the glucose response complex. FEBS Lett. 1998, 431:180-184.
14. Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T. Regulation of transcription by AMP-activated protein kinase. J. Biol. Chem. 2001, 276:38341-38344.
15. Winder W.W., Holmes B.F., Rubink D.S., Jensen E.B., Chen M., Holloszy J.O. Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle. J. Appl. Physiol. 2000, 88:2219-2226.
16. Fryer L.G., Foufelle F., Barnes K., Baldwin S.A., Woods A., Carling D. Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle. Biochem. J. 2002, 363:167-174.
17. Choi J.W., Kim D.J., Rhim J.H., Chung J.H., Chung H.K. Generation and characterization of IgG monoclonal antibodies specific for malondialdehyde. Hybrid. Hybridomics 2003, 22:259-262.
18. Lage R., Dieguesz C., Vidal-Puig A., Lopez M. AMPK: a metabolic gauge regulating whole-body energy homeostasis. Trends Mol. Med. 2009, 14:539-549.
19. You M., Fischer M., Cho W.K., Crabb D. Transcriptional control of the human aldehyde dehydrogenase 2 promoter by hepatocyte nuclear factor 4: inhibition by cyclic AMP and COUP transcription factors. Arch. Biochem. Biophys. 2002, 389:79-86.
20. Berry M.D., Boulton A.A. Glyceraldehyde-3-phosphate dehydrogenase and apoptosis. J. Neurosci. Res. 2000, 60:150-154.
21. Zheng L., Roeder R.G., Luo Y. S phase activation of the histone H2B promoter by OCA-S a coactivator complex that contains GAPDH as a key component. Cell 2003, 114:255-266.
22. Zhong X.H., Howard B.D. Phosphotyrosine-containing lactate dehydrogenase is restricted to the nuclei of PC12 pheochromocytoma cells. Mol. Cell. Biol. 1990, 10:770-776.
23. Lee S.M., Kim J.H., Cho E.J., Youn H.D. A nucleocytoplasmic malate dehydrogenase regulates p53 transcriptional activity in response to metabolic stress. Cell Death Differ. 2009, 16:738-748.
24. Mukhopadhyay A., Heard T.S., Wen X., Hammen P.K., Weiner H. Location of the actual signal in the negatively charged leader sequence involved in the import into the mitochondrial matrix space. J. Biol. Chem. 2003, 278:13712-13718.
25. Daugas E., Susin S.A., Zamzami N., Ferri K.F., Irinopoulou T., Larochette N., Prévost M.C., Leber B., Andrews D., Penninger J., Kroemer G. Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis. FASEB J. 2000, 14:729-739.
26. Dawson V.L., Dawson T.M. Deadly conversations: nuclear-mitochondrial cross-talk. J. Bioenerg. Biomembr. 2004, 36:287-294.