메뉴 건너뛰기




Volumn 147, Issue 3, 2007, Pages 674-679

Acrolein induces selective protein carbonylation in synaptosomes

Author keywords

[No Author keywords available]

Indexed keywords

ACROLEIN; BETA ACTIN; ELONGATION FACTOR; TROPOMYOSIN; TROPOMYOSIN 3 GAMMA ISOFORM 2; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 34250834295     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2007.04.003     Document Type: Article
Times cited : (62)

References (46)
  • 1
    • 0027227808 scopus 로고
    • Acrolein-induced oxygen radical formation
    • Adams Jr. J.D., and Klaidman L.K. Acrolein-induced oxygen radical formation. Free Radic Biol Med 15 (1993) 187-193
    • (1993) Free Radic Biol Med , vol.15 , pp. 187-193
    • Adams Jr., J.D.1    Klaidman, L.K.2
  • 3
    • 0029905387 scopus 로고    scopus 로고
    • The spectrin-based membrane skeleton as a membrane protein-sorting machine
    • Beck K.A., and Nelson W.J. The spectrin-based membrane skeleton as a membrane protein-sorting machine. Am J Physiol 270 (1996) C1263-C1270
    • (1996) Am J Physiol , vol.270
    • Beck, K.A.1    Nelson, W.J.2
  • 4
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., and Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272 (1997) 20313-20316
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 6
    • 0141767139 scopus 로고    scopus 로고
    • Proteomics in Alzheimer's disease: insights into potential mechanisms of neurodegeneration
    • Butterfield D.A., Boyd-Kimball D., and Castegna A. Proteomics in Alzheimer's disease: insights into potential mechanisms of neurodegeneration. J Neurochem 86 (2003) 1313-1327
    • (2003) J Neurochem , vol.86 , pp. 1313-1327
    • Butterfield, D.A.1    Boyd-Kimball, D.2    Castegna, A.3
  • 7
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • Butterfield D.A., Castegna A., Lauderback C.M., and Drake J. Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death. Neurobiol Aging 23 (2002) 655-664
    • (2002) Neurobiol Aging , vol.23 , pp. 655-664
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 9
    • 0032905632 scopus 로고    scopus 로고
    • Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease
    • Calingasan N.Y., Uchida K., and Gibson G.E. Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease. J Neurochem 72 (1999) 751-756
    • (1999) J Neurochem , vol.72 , pp. 751-756
    • Calingasan, N.Y.1    Uchida, K.2    Gibson, G.E.3
  • 10
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., and Butterfield D.A. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic Biol Med 33 (2002) 562-571
    • (2002) Free Radic Biol Med , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 11
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A., Aksenov M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., and Butterfield D.A. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 82 (2002) 1524-1532
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 12
    • 0025915662 scopus 로고
    • Glutathione depletion: its effects on other antioxidant systems and hepatocellular damage
    • Comporti M., Maellaro E., Del Bello B., and Casini A.F. Glutathione depletion: its effects on other antioxidant systems and hepatocellular damage. Xenobiotica 21 (1991) 1067-1076
    • (1991) Xenobiotica , vol.21 , pp. 1067-1076
    • Comporti, M.1    Maellaro, E.2    Del Bello, B.3    Casini, A.F.4
  • 13
  • 14
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 11 (1991) 81-128
    • (1991) Free Radic Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 15
    • 0027359981 scopus 로고
    • Effect of oxidative stress on excitatory amino acid release by cerebral cortical synaptosomes
    • Gilman S.C., Bonner M.J., and Pellmar T.C. Effect of oxidative stress on excitatory amino acid release by cerebral cortical synaptosomes. Free Radic Biol Med 15 (1993) 671-675
    • (1993) Free Radic Biol Med , vol.15 , pp. 671-675
    • Gilman, S.C.1    Bonner, M.J.2    Pellmar, T.C.3
  • 16
    • 73049155988 scopus 로고
    • The isolation of nerve endings from brain: an electron-microscopic study of cell fragments derived by homogenization and centrifugation
    • Gray E.G., and Whittaker V.P. The isolation of nerve endings from brain: an electron-microscopic study of cell fragments derived by homogenization and centrifugation. J Anat 96 (1962) 79-88
    • (1962) J Anat , vol.96 , pp. 79-88
    • Gray, E.G.1    Whittaker, V.P.2
  • 18
    • 0037312691 scopus 로고    scopus 로고
    • Actin in a supporting role
    • Halpain S. Actin in a supporting role. Nat Neurosci 6 (2003) 101-102
    • (2003) Nat Neurosci , vol.6 , pp. 101-102
    • Halpain, S.1
  • 19
    • 0027936618 scopus 로고
    • Electron paramagnetic resonance investigations of free radical-induced alterations in neocortical synaptosomal membrane protein infrastructure
    • Hensley K., Carney J., Hall N., Shaw W., and Butterfield D.A. Electron paramagnetic resonance investigations of free radical-induced alterations in neocortical synaptosomal membrane protein infrastructure. Free Radic Biol Med 17 (1994) 321-331
    • (1994) Free Radic Biol Med , vol.17 , pp. 321-331
    • Hensley, K.1    Carney, J.2    Hall, N.3    Shaw, W.4    Butterfield, D.A.5
  • 20
    • 0030796956 scopus 로고    scopus 로고
    • Relationships between cell density, glutathione and proliferation of A549 human lung adenocarcinoma cells treated with acrolein
    • Horton N.D., Mamiya B.M., and Kehrer J.P. Relationships between cell density, glutathione and proliferation of A549 human lung adenocarcinoma cells treated with acrolein. Toxicology 122 (1997) 111-122
    • (1997) Toxicology , vol.122 , pp. 111-122
    • Horton, N.D.1    Mamiya, B.M.2    Kehrer, J.P.3
  • 21
    • 0033864802 scopus 로고    scopus 로고
    • The molecular effects of acrolein
    • Kehrer J.P., and Biswal S.S. The molecular effects of acrolein. Toxicol Sci 57 (2000) 6-15
    • (2000) Toxicol Sci , vol.57 , pp. 6-15
    • Kehrer, J.P.1    Biswal, S.S.2
  • 22
    • 29344468832 scopus 로고    scopus 로고
    • Voltage-dependent anion channel (VDAC) as mitochondrial governator: thinking outside the box
    • Lemasters J.J., and Holmuhamedov E. Voltage-dependent anion channel (VDAC) as mitochondrial governator: thinking outside the box. Biochim Biophys Acta 1762 (2006) 181-190
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 181-190
    • Lemasters, J.J.1    Holmuhamedov, E.2
  • 23
    • 0034667741 scopus 로고    scopus 로고
    • Acrolein, a product of lipid peroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures
    • Lovell M.A., Xie C., and Markesbery W.R. Acrolein, a product of lipid peroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures. Free Radic Biol Med 29 (2000) 714-720
    • (2000) Free Radic Biol Med , vol.29 , pp. 714-720
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 24
    • 0035112495 scopus 로고    scopus 로고
    • Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures
    • Lovell M.A., Xie C., and Markesbery W.R. Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures. Neurobiol Aging 22 (2001) 187-194
    • (2001) Neurobiol Aging , vol.22 , pp. 187-194
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 25
    • 21144451431 scopus 로고    scopus 로고
    • Accumulation of acrolein-protein adducts after traumatic spinal cord injury
    • Luo J., Uchida K., and Shi R. Accumulation of acrolein-protein adducts after traumatic spinal cord injury. Neurochem Res 30 (2005) 291-295
    • (2005) Neurochem Res , vol.30 , pp. 291-295
    • Luo, J.1    Uchida, K.2    Shi, R.3
  • 26
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide
    • Mark R.J., Lovell M.A., Markesbery W.R., Uchida K., and Mattson M.P. A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide. J Neurochem 68 (1997) 255-264
    • (1997) J Neurochem , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 27
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery W.R., and Lovell M.A. Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol Aging 19 (1998) 33-36
    • (1998) Neurobiol Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 29
    • 0027442066 scopus 로고
    • Acrolein-induced injury to cultured pulmonary artery endothelial cells
    • Patel J.M., and Block E.R. Acrolein-induced injury to cultured pulmonary artery endothelial cells. Toxicol Appl Pharmacol 122 (1993) 46-53
    • (1993) Toxicol Appl Pharmacol , vol.122 , pp. 46-53
    • Patel, J.M.1    Block, E.R.2
  • 30
    • 1342306400 scopus 로고    scopus 로고
    • Acrolein inhibits NADH-linked mitochondrial enzyme activity: implications for Alzheimer's disease
    • Pocernich C.B., and Butterfield D.A. Acrolein inhibits NADH-linked mitochondrial enzyme activity: implications for Alzheimer's disease. Neurotox Res 5 (2003) 515-520
    • (2003) Neurotox Res , vol.5 , pp. 515-520
    • Pocernich, C.B.1    Butterfield, D.A.2
  • 31
    • 0034988283 scopus 로고    scopus 로고
    • Glutathione elevation and its protective role in acrolein-induced protein damage in synaptosomal membranes: relevance to brain lipid peroxidation in neurodegenerative disease
    • Pocernich C.B., Cardin A.L., Racine C.L., Lauderback C.M., and Butterfield D.A. Glutathione elevation and its protective role in acrolein-induced protein damage in synaptosomal membranes: relevance to brain lipid peroxidation in neurodegenerative disease. Neurochem Int 39 (2001) 141-149
    • (2001) Neurochem Int , vol.39 , pp. 141-149
    • Pocernich, C.B.1    Cardin, A.L.2    Racine, C.L.3    Lauderback, C.M.4    Butterfield, D.A.5
  • 32
    • 23744513820 scopus 로고    scopus 로고
    • Abeta-polyacrolein aggregates: novel mechanism of plastic formation in senile plaques
    • Seidler N.W., and Squire T.J. Abeta-polyacrolein aggregates: novel mechanism of plastic formation in senile plaques. Biochem Biophys Res Commun 335 (2005) 501-504
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 501-504
    • Seidler, N.W.1    Squire, T.J.2
  • 33
    • 2942678692 scopus 로고    scopus 로고
    • Albumin-bound polyacrolein: implications for Alzheimer's disease
    • Seidler N.W., and Yeargans G.S. Albumin-bound polyacrolein: implications for Alzheimer's disease. Biochem Biophys Res Commun 320 (2004) 213-217
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 213-217
    • Seidler, N.W.1    Yeargans, G.S.2
  • 34
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S., Narita M., and Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399 (1999) 483-487
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 35
    • 3342931462 scopus 로고    scopus 로고
    • Aberrant neuronal and mitochondrial proteins in hippocampus of transgenic mice overexpressing human Cu/Zn superoxide dismutase 1
    • Shin J.H., London J., Le Pecheur M., Hoger H., Pollak D., and Lubec G. Aberrant neuronal and mitochondrial proteins in hippocampus of transgenic mice overexpressing human Cu/Zn superoxide dismutase 1. Free Radic Biol Med 37 (2004) 643-653
    • (2004) Free Radic Biol Med , vol.37 , pp. 643-653
    • Shin, J.H.1    London, J.2    Le Pecheur, M.3    Hoger, H.4    Pollak, D.5    Lubec, G.6
  • 36
    • 0942297436 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death
    • Shoshan-Barmatz V., and Gincel D. The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death. Cell Biochem Biophys 39 (2003) 279-292
    • (2003) Cell Biochem Biophys , vol.39 , pp. 279-292
    • Shoshan-Barmatz, V.1    Gincel, D.2
  • 38
    • 33644913675 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta (1-42)
    • Sultana R., Perluigi M., and Butterfield D.A. Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta (1-42). J Chromatogr B Analyt Technol Biomed Life Sci 833 (2006) 3-11
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.833 , pp. 3-11
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 40
    • 0033113321 scopus 로고    scopus 로고
    • Carbonyl stress in the pathogenesis of diabetic nephropathy
    • Suzuki D., and Miyata T. Carbonyl stress in the pathogenesis of diabetic nephropathy. Intern Med 38 (1999) 309-314
    • (1999) Intern Med , vol.38 , pp. 309-314
    • Suzuki, D.1    Miyata, T.2
  • 41
    • 23944478337 scopus 로고    scopus 로고
    • Oxidative metabolites are involved in polyamine-induced microglial cell death
    • Takano K., Ogura M., Yoneda Y., and Nakamura Y. Oxidative metabolites are involved in polyamine-induced microglial cell death. Neuroscience 134 (2005) 1123-1131
    • (2005) Neuroscience , vol.134 , pp. 1123-1131
    • Takano, K.1    Ogura, M.2    Yoneda, Y.3    Nakamura, Y.4
  • 42
    • 33748961353 scopus 로고    scopus 로고
    • Mitochondrial membrane permeability transition and cell death
    • Tsujimoto Y., Nakagawa T., and Shimizu S. Mitochondrial membrane permeability transition and cell death. Biochim Biophys Acta 1757 (2006) 1297-1300
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 1297-1300
    • Tsujimoto, Y.1    Nakagawa, T.2    Shimizu, S.3
  • 43
    • 0036479011 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: an essential player in apoptosis
    • Tsujimoto Y., and Shimizu S. The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84 (2002) 187-193
    • (2002) Biochimie , vol.84 , pp. 187-193
    • Tsujimoto, Y.1    Shimizu, S.2
  • 44
    • 0033452913 scopus 로고    scopus 로고
    • Current status of acrolein as a lipid peroxidation product
    • Uchida K. Current status of acrolein as a lipid peroxidation product. Trends Cardiovasc Med 9 (1999) 109-113
    • (1999) Trends Cardiovasc Med , vol.9 , pp. 109-113
    • Uchida, K.1
  • 46
    • 4544233514 scopus 로고    scopus 로고
    • Effect of acrolein and glutathione depleting agents on thioredoxin
    • Yang X., Wu X., Choi Y.E., Kern J.C., and Kehrer J.P. Effect of acrolein and glutathione depleting agents on thioredoxin. Toxicology 204 (2004) 209-218
    • (2004) Toxicology , vol.204 , pp. 209-218
    • Yang, X.1    Wu, X.2    Choi, Y.E.3    Kern, J.C.4    Kehrer, J.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.