메뉴 건너뛰기




Volumn 178, Issue 2, 2007, Pages 869-876

HIV-1 trans activator of transcription protein elicits mitochondrial hyperpolarization and respiratory deficit, with dysregulation of complex IV and nicotinamide adenine dinucleotide homeostasis in cortical neurons

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALMODULIN; CYTOCHROME C OXIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RHODAMINE 123; TRANSACTIVATOR PROTEIN; YELLOW FLUORESCENT PROTEIN;

EID: 33846230605     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.178.2.869     Document Type: Article
Times cited : (74)

References (50)
  • 1
    • 9644272621 scopus 로고    scopus 로고
    • HIV dementia: An evolving disease
    • McArthur, J. C. 2004. HIV dementia: an evolving disease. J. Neuroimmunol. 157: 3-10.
    • (2004) J. Neuroimmunol , vol.157 , pp. 3-10
    • McArthur, J.C.1
  • 2
    • 0035400121 scopus 로고    scopus 로고
    • Dissipation of potassium and proton gradients inhibits mitochondrial hyperpolarization and cytochrome c release during neural apoptosis
    • Poppe, M., C. Reimertz, H. Dussmann, A. J. Krohn, C. M. Luetjens, D. Bockelmann, A. L. Nieminen, D. Kogel, and J. H. Prehn. 2001. Dissipation of potassium and proton gradients inhibits mitochondrial hyperpolarization and cytochrome c release during neural apoptosis. J. Neurosci. 21: 4551-4563.
    • (2001) J. Neurosci , vol.21 , pp. 4551-4563
    • Poppe, M.1    Reimertz, C.2    Dussmann, H.3    Krohn, A.J.4    Luetjens, C.M.5    Bockelmann, D.6    Nieminen, A.L.7    Kogel, D.8    Prehn, J.H.9
  • 3
    • 22244484446 scopus 로고    scopus 로고
    • Molecular mechanisms of HIV-1 associated neurodegeneration
    • Ozdener, H. 2005. Molecular mechanisms of HIV-1 associated neurodegeneration. J. Biosci. 30: 391-405.
    • (2005) J. Biosci , vol.30 , pp. 391-405
    • Ozdener, H.1
  • 4
    • 0037000758 scopus 로고    scopus 로고
    • Interactions of human immunodeficiency virus-1 proteins with neurons: Possible role in the development of human immunodeficiency virus-1-associated dementia
    • Van de Bovenkamp, M., H. S. Nottet, and C. F. Pereira. 2002. Interactions of human immunodeficiency virus-1 proteins with neurons: possible role in the development of human immunodeficiency virus-1-associated dementia. Eur. J. Clin. Invest. 32: 619-627.
    • (2002) Eur. J. Clin. Invest , vol.32 , pp. 619-627
    • Van de Bovenkamp, M.1    Nottet, H.S.2    Pereira, C.F.3
  • 5
    • 0025344596 scopus 로고
    • Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients
    • Ensoli, B., G. Barillari, S. Z. Salahuddin, R. C. Gallo, and F. Wong-Staal. 1990. Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients. Nature 345: 84-86.
    • (1990) Nature , vol.345 , pp. 84-86
    • Ensoli, B.1    Barillari, G.2    Salahuddin, S.Z.3    Gallo, R.C.4    Wong-Staal, F.5
  • 6
    • 0348087031 scopus 로고    scopus 로고
    • HIV Tat, its TARgets and the control of viral gene expression
    • Brigati, C., M. Giacca, D. M. Noonan, and A. Albini. 2003. HIV Tat, its TARgets and the control of viral gene expression. FEMS Microbiol. Lett. 220: 57-65.
    • (2003) FEMS Microbiol. Lett , vol.220 , pp. 57-65
    • Brigati, C.1    Giacca, M.2    Noonan, D.M.3    Albini, A.4
  • 8
    • 0026709499 scopus 로고
    • Human immunodeficiency virus type 1-infected monocytic cells can destroy human neural cells after cell-to-cell adhesion
    • Tardieu, M., C. Hery, S. Peudenier, O. Boespflug, and L. Montagnier. 1992. Human immunodeficiency virus type 1-infected monocytic cells can destroy human neural cells after cell-to-cell adhesion. Ann. Neurol. 32: 11-17.
    • (1992) Ann. Neurol , vol.32 , pp. 11-17
    • Tardieu, M.1    Hery, C.2    Peudenier, S.3    Boespflug, O.4    Montagnier, L.5
  • 9
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel, A. D., and C. O. Pabo. 1988. Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55: 1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 10
    • 0025797055 scopus 로고
    • Endocytosis and targeting of exogenous HIV-1 Tat protein
    • Mann, D. A., and A. D. Frankel. 1991. Endocytosis and targeting of exogenous HIV-1 Tat protein. EMBO J. 10: 1733-1739.
    • (1991) EMBO J , vol.10 , pp. 1733-1739
    • Mann, D.A.1    Frankel, A.D.2
  • 11
    • 0034909804 scopus 로고    scopus 로고
    • HTV-1 Tat through phosphorylation of NMDA receptors potentiates glutamate excitotoxicity
    • Haughey, N. J., A. Nath, M. P. Mattson, J. T. Slevin, and J. D. Geiger. 2001. HTV-1 Tat through phosphorylation of NMDA receptors potentiates glutamate excitotoxicity. J. Neurochem. 78: 457-467.
    • (2001) J. Neurochem , vol.78 , pp. 457-467
    • Haughey, N.J.1    Nath, A.2    Mattson, M.P.3    Slevin, J.T.4    Geiger, J.D.5
  • 12
    • 22744440922 scopus 로고    scopus 로고
    • Cell death in HIV dementia
    • Mattson, M. P., N. J. Haughey, and A. Nath. 2005. Cell death in HIV dementia. Cell Death Differ. 12(Suppl. 1): 893-904.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 1 , pp. 893-904
    • Mattson, M.P.1    Haughey, N.J.2    Nath, A.3
  • 13
    • 0032504151 scopus 로고    scopus 로고
    • HIV-1 Tat induces neuronal death via tumor necrosis factor-α and activation of non-N-methyl-D-aspartate receptors by a NFκB-independent mechanism
    • New, D. R., S. B. Maggirwar, L. G. Epstein, S. Dewhurst, and H. A. Gelbard. 1998. HIV-1 Tat induces neuronal death via tumor necrosis factor-α and activation of non-N-methyl-D-aspartate receptors by a NFκB-independent mechanism. J. Biol. Chem. 273: 17852-17858.
    • (1998) J. Biol. Chem , vol.273 , pp. 17852-17858
    • New, D.R.1    Maggirwar, S.B.2    Epstein, L.G.3    Dewhurst, S.4    Gelbard, H.A.5
  • 17
    • 0030889331 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Tat protein induces death by apoptosis in primary human neuron cultures
    • New, D. R., M. Ma, L. G. Epstein, A. Nath, and H. A. Gelbard. 1997. Human immunodeficiency virus type 1 Tat protein induces death by apoptosis in primary human neuron cultures. J. Neurovirol. 3: 168-173.
    • (1997) J. Neurovirol , vol.3 , pp. 168-173
    • New, D.R.1    Ma, M.2    Epstein, L.G.3    Nath, A.4    Gelbard, H.A.5
  • 22
    • 0013198976 scopus 로고    scopus 로고
    • Mitochondria in cell death: Novel targets for neuroprotection and cardioprotection
    • Mattson, M. P., and G. Kroemer. 2003. Mitochondria in cell death: novel targets for neuroprotection and cardioprotection. Trends Mol. Med. 9: 196-205.
    • (2003) Trends Mol. Med , vol.9 , pp. 196-205
    • Mattson, M.P.1    Kroemer, G.2
  • 23
    • 0014018142 scopus 로고
    • Synthesis of adenosine triphosphate by a protonmotive force in rat liver mitochondria
    • Reid, R. A., J. Moyle, and P. Mitchell. 1966. Synthesis of adenosine triphosphate by a protonmotive force in rat liver mitochondria. Nature 212: 257-258.
    • (1966) Nature , vol.212 , pp. 257-258
    • Reid, R.A.1    Moyle, J.2    Mitchell, P.3
  • 24
    • 0034176843 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and neuronal glutamate excitotoxicity: Mortality and millivolts
    • Nicholls, D. G., and M. W. Ward. 2000. Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts. Trends Neurosci. 23: 166-174.
    • (2000) Trends Neurosci , vol.23 , pp. 166-174
    • Nicholls, D.G.1    Ward, M.W.2
  • 25
    • 0036830474 scopus 로고    scopus 로고
    • Mitochondrial function and dysfunction in the cell: Its relevance to aging and aging-related disease
    • Nicholls, D. G. 2002. Mitochondrial function and dysfunction in the cell: its relevance to aging and aging-related disease. Int. J. Biochem. Cell Biol. 34: 1372-1381.
    • (2002) Int. J. Biochem. Cell Biol , vol.34 , pp. 1372-1381
    • Nicholls, D.G.1
  • 27
    • 0034668946 scopus 로고    scopus 로고
    • Mitochondria as all-round players of the calcium game
    • Rizzuto, R., P. Bernardi, and T. Pozzan. 2000. Mitochondria as all-round players of the calcium game. J. Physiol. 529: 37-47.
    • (2000) J. Physiol , vol.529 , pp. 37-47
    • Rizzuto, R.1    Bernardi, P.2    Pozzan, T.3
  • 28
    • 0035797119 scopus 로고    scopus 로고
    • Mitochondria make a comeback
    • Scheffler, I. E. 2001. Mitochondria make a comeback. Adv. Drug Delivery Rev. 49: 3-26.
    • (2001) Adv. Drug Delivery Rev , vol.49 , pp. 3-26
    • Scheffler, I.E.1
  • 29
    • 15444370727 scopus 로고    scopus 로고
    • HIV-1 transactivator of transcription protein induces mitochondrial hyperpolarization and synaptic stress leading to apoptosis
    • Perry, S. W., J. P. Norman, A. Litzburg, D. Zhang, S. Dewhurst, and H. A. Gelbard. 2005. HIV-1 transactivator of transcription protein induces mitochondrial hyperpolarization and synaptic stress leading to apoptosis. J. Immunol. 174: 4333-4344.
    • (2005) J. Immunol , vol.174 , pp. 4333-4344
    • Perry, S.W.1    Norman, J.P.2    Litzburg, A.3    Zhang, D.4    Dewhurst, S.5    Gelbard, H.A.6
  • 30
    • 0038620230 scopus 로고    scopus 로고
    • Mitochondrial membrane hyperpolarization hijacks activated T lymphocytes toward the apoptotic-prone phenotype: Homeostatic mechanisms of HIV protease inhibitors
    • Matarrese, P., L. Gambardella, A. Cassone, S. Vella, R. Cauda, and W. Malorni. 2003. Mitochondrial membrane hyperpolarization hijacks activated T lymphocytes toward the apoptotic-prone phenotype: homeostatic mechanisms of HIV protease inhibitors. J. Immunol. 170: 6006-6015.
    • (2003) J. Immunol , vol.170 , pp. 6006-6015
    • Matarrese, P.1    Gambardella, L.2    Cassone, A.3    Vella, S.4    Cauda, R.5    Malorni, W.6
  • 31
    • 0242663915 scopus 로고    scopus 로고
    • 2+- and redox-dependent production of nitric oxide
    • 2+- and redox-dependent production of nitric oxide. J. Immunol. 171: 5188-5197.
    • (2003) J. Immunol , vol.171 , pp. 5188-5197
    • Nagy, G.1    Koncz, A.2    Perl, A.3
  • 32
    • 2942635457 scopus 로고    scopus 로고
    • Mitochondrial hyperpolarization: A checkpoint of T-cell life, death and autoimmunity
    • Perl, A., P. Gergely, Jr., G. Nagy, A. Koncz, and K. Banki. 2004. Mitochondrial hyperpolarization: a checkpoint of T-cell life, death and autoimmunity. Trends Immunol. 25: 360-367.
    • (2004) Trends Immunol , vol.25 , pp. 360-367
    • Perl, A.1    Gergely Jr., P.2    Nagy, G.3    Koncz, A.4    Banki, K.5
  • 33
    • 0030068995 scopus 로고    scopus 로고
    • Identification of a human immunodeficiency virus type 1 Tat epitope that is neuroexcitatory and neurotoxic
    • Nath, A., K. Psooy, C. Martin, B. Knudsen, D. S. Magnuson, N. Haughey, and J. D. Geiger. 1996. Identification of a human immunodeficiency virus type 1 Tat epitope that is neuroexcitatory and neurotoxic. J. Virol. 70: 1475-1480.
    • (1996) J. Virol , vol.70 , pp. 1475-1480
    • Nath, A.1    Psooy, K.2    Martin, C.3    Knudsen, B.4    Magnuson, D.S.5    Haughey, N.6    Geiger, J.D.7
  • 34
    • 0035800813 scopus 로고    scopus 로고
    • 2+ to the endoplasmic reticulum and prevent the depletion of neighboring endoplasmic reticulum regions
    • 2+ to the endoplasmic reticulum and prevent the depletion of neighboring endoplasmic reticulum regions. J. Biol. Chem. 276: 29430-29439.
    • (2001) J. Biol. Chem , vol.276 , pp. 29430-29439
    • Arnaudeau, S.1    Kelley, W.L.2    Walsh Jr., J.V.3    Demaurex, N.4
  • 35
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein: Mechanism and applications
    • Griesbeck, O., G. S. Baird, R. E. Campbell, D. A. Zacharias, and R. Y. Tsien. 2001. Reducing the environmental sensitivity of yellow fluorescent protein: mechanism and applications. J. Biol. Chem. 276: 29188-29194.
    • (2001) J. Biol. Chem , vol.276 , pp. 29188-29194
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3    Zacharias, D.A.4    Tsien, R.Y.5
  • 36
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • Brewer, G. J., J. R. Torricelli, E. K. Evege, and P. J. Price. 1993. Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35: 567-576.
    • (1993) J. Neurosci. Res , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 39
    • 0007574262 scopus 로고
    • Localization of mitochondria in living cells with rhodamine 123
    • Johnson, L. V., M. L. Walsh, and L. B. Chen. 1980. Localization of mitochondria in living cells with rhodamine 123. Proc. Natl. Acad. Sci. USA 77: 990-994.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 990-994
    • Johnson, L.V.1    Walsh, M.L.2    Chen, L.B.3
  • 42
    • 3042793425 scopus 로고    scopus 로고
    • Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis
    • Kasischke, K. A., H. D. Vishwasrao, P. J. Fisher, W. R. Zipfel, and W. W. Webb. 2004. Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis. Science 305: 99-103.
    • (2004) Science , vol.305 , pp. 99-103
    • Kasischke, K.A.1    Vishwasrao, H.D.2    Fisher, P.J.3    Zipfel, W.R.4    Webb, W.W.5
  • 44
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • Belevich, I., M. I. Verkhovsky, and M. Wikstrom. 2006. Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase. Nature 440: 829-832.
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikstrom, M.3
  • 46
    • 33746329868 scopus 로고    scopus 로고
    • Energy Converting NADH: Quinone oxidoreductase complex I
    • Brandt, U. 2006. Energy Converting NADH: quinone oxidoreductase complex I. Annu. Rev. Biochem. 75: 69-92.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 69-92
    • Brandt, U.1
  • 47
    • 0023653390 scopus 로고
    • Respiratory control in the glucose perfused heart: A 31P NMR and NADH fluorescence study
    • Katz, L. A., A. P. Koretsky, and R. S. Balaban. 1987. Respiratory control in the glucose perfused heart: a 31P NMR and NADH fluorescence study. FEBS Lett. 221: 270-276.
    • (1987) FEBS Lett , vol.221 , pp. 270-276
    • Katz, L.A.1    Koretsky, A.P.2    Balaban, R.S.3
  • 48
    • 0033198273 scopus 로고    scopus 로고
    • Mitochondrial depolarization is not required for neuronal apoptosis
    • Krohn, A. J., T. Wahlbrink, and J. H. Prehn. 1999. Mitochondrial depolarization is not required for neuronal apoptosis. J. Neurosci. 19: 7394-7404.
    • (1999) J. Neurosci , vol.19 , pp. 7394-7404
    • Krohn, A.J.1    Wahlbrink, T.2    Prehn, J.H.3
  • 50
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze, S. R., A. Ho, A. Vocero-Akbani, and S. F. Dowdy. 1999. In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 285: 1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.