메뉴 건너뛰기




Volumn 1369, Issue , 2011, Pages 184-193

Subcellular compartmentalization of proteolytic enzymes in brain regions and the effects of chronic β-amyloid treatment

Author keywords

Amyloid peptide; Brain regions; Proteases; Subcellular structures

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; BETA GALACTOSIDASE; CALPAIN 1; CALPAIN 2; CASPASE 3; CASPASE 9; CATHEPSIN B; CATHEPSIN D; PROTEINASE;

EID: 78651078114     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2010.10.078     Document Type: Article
Times cited : (12)

References (63)
  • 1
    • 0036934648 scopus 로고    scopus 로고
    • Calpain activation in neurodegenerative diseases: Confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2
    • E. Adamec, P. Mohan, J.P. Vonsattel, and R.A. Nixon Calpain activation in neurodegenerative diseases: confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2 Acta Neuropathol. (Berl) 104 2002 92 104
    • (2002) Acta Neuropathol. (Berl) , vol.104 , pp. 92-104
    • Adamec, E.1    Mohan, P.2    Vonsattel, J.P.3    Nixon, R.A.4
  • 2
    • 26444588771 scopus 로고    scopus 로고
    • Gradual alteration of mitochondrial structure and function by beta-amyloids: Importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release
    • A.M. Aleardi, G. Benard, O. Augereau, M. Madat, J.C. Talbot, J.P. Mazat, T. Letellier, J. Dachary-Prigent, G.C. Solaini, and R. Rossignol Gradual alteration of mitochondrial structure and function by beta-amyloids: importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release J. Bioenerg. Biomembr. 37 2005 207 225
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 207-225
    • Aleardi, A.M.1    Benard, G.2    Augereau, O.3    Madat, M.4    Talbot, J.C.5    Mazat, J.P.6    Letellier, T.7    Dachary-Prigent, J.8    Solaini, G.C.9    Rossignol, R.10
  • 6
    • 33845337981 scopus 로고    scopus 로고
    • Calpain 10: A mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction
    • D. Arrington, T. Van Vleet, and R. Schnellmann Calpain 10: a mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction Am. J. Physiol. Cell Physiol. 291 2006 C1159 C1171
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291
    • Arrington, D.1    Van Vleet, T.2    Schnellmann, R.3
  • 7
    • 0019421831 scopus 로고
    • Purification and characterization of human alpha-galactosidase isozymes: Comparison of tissue and plasma forms and evaluation of purification methods
    • D.F. Bishop, K.J. Dean, C.C. Sweeley, and R.J. Desnick Purification and characterization of human alpha-galactosidase isozymes: comparison of tissue and plasma forms and evaluation of purification methods Birth Defects Orig. Artic. Ser. 16 1980 17 32
    • (1980) Birth Defects Orig. Artic. Ser. , vol.16 , pp. 17-32
    • Bishop, D.F.1    Dean, K.J.2    Sweeley, C.C.3    Desnick, R.J.4
  • 8
    • 0037216189 scopus 로고    scopus 로고
    • Beta-Amyloid (1-40)-induced apoptosis of cultured cortical neurons involves calpain-mediated cleavage of poly-ADP-ribose polymerase
    • B. Boland, and V. Campbell beta-Amyloid (1-40)-induced apoptosis of cultured cortical neurons involves calpain-mediated cleavage of poly-ADP-ribose polymerase Neurobiol. Aging 24 2003 179 186
    • (2003) Neurobiol. Aging , vol.24 , pp. 179-186
    • Boland, B.1    Campbell, V.2
  • 10
    • 16244410153 scopus 로고    scopus 로고
    • Mu-calpain is functionally required for alpha-processing of Alzheimer's beta-amyloid precursor protein
    • M. Chen, and H.L. Fernandez Mu-calpain is functionally required for alpha-processing of Alzheimer's beta-amyloid precursor protein Biochem. Biophys. Res. Commun. 330 2005 714 721
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 714-721
    • Chen, M.1    Fernandez, H.L.2
  • 12
    • 33644853371 scopus 로고    scopus 로고
    • Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3
    • A. Fifre, I. Sponne, V. Koziel, B. Kriem, F.T. Yen Potin, B.E. Bihain, J.L. Olivier, T. Oster, and T. Pillot Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3 J. Biol. Chem. 281 2006 229 240
    • (2006) J. Biol. Chem. , vol.281 , pp. 229-240
    • Fifre, A.1    Sponne, I.2    Koziel, V.3    Kriem, B.4    Yen Potin, F.T.5    Bihain, B.E.6    Olivier, J.L.7    Oster, T.8    Pillot, T.9
  • 14
    • 0032529676 scopus 로고    scopus 로고
    • Cytochrome c induces caspase-dependent apoptosis in intact hematopoietic cells and overrides apoptosis suppression mediated by bcl-2, growth factor signaling, MAP-kinase-kinase, and malignant change
    • J.M. Garland, and C. Rudin Cytochrome c induces caspase-dependent apoptosis in intact hematopoietic cells and overrides apoptosis suppression mediated by bcl-2, growth factor signaling, MAP-kinase-kinase, and malignant change Blood 92 1998 1235 1246
    • (1998) Blood , vol.92 , pp. 1235-1246
    • Garland, J.M.1    Rudin, C.2
  • 17
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • R.U. Jänicke, M.L. Sprengart, M.R. Wati, and A.G. Porter Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis J. Biol. Chem. 273 1998 9357 9360
    • (1998) J. Biol. Chem. , vol.273 , pp. 9357-9360
    • Jänicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 18
    • 70049111544 scopus 로고    scopus 로고
    • Brain purine metabolism and xanthine dehydrogenase/oxidase conversion in hyperammonemia are under control of NMDA receptors and nitric oxide
    • Y. Kaminsky, and E. Kosenko Brain purine metabolism and xanthine dehydrogenase/oxidase conversion in hyperammonemia are under control of NMDA receptors and nitric oxide Brain Res. 1294 2009 193 201
    • (2009) Brain Res. , vol.1294 , pp. 193-201
    • Kaminsky, Y.1    Kosenko, E.2
  • 19
    • 78651112719 scopus 로고    scopus 로고
    • DNA fragmentation, poly(ADP-ribose) polymerase, NAD-synthetase, NAD-glycohydrolase, and p53 protein in nuclei from brain cells and Alzheimer's disease
    • Slovo Moscow
    • Y.G. Kaminsky, E.A. Kosenko, E.A. Mugantseva, I.Y. Podolski, C. Montoliu, and V. Felipo DNA fragmentation, poly(ADP-ribose) polymerase, NAD-synthetase, NAD-glycohydrolase, and p53 protein in nuclei from brain cells and Alzheimer's disease Basic Research for Medicine 2004 Slovo Moscow 15 17 (In Russian)
    • (2004) Basic Research for Medicine , pp. 15-17
    • Kaminsky, Y.G.1    Kosenko, E.A.2    Mugantseva, E.A.3    Podolski, I.Y.4    Montoliu, C.5    Felipo, V.6
  • 20
    • 34547793538 scopus 로고    scopus 로고
    • Apoptotic markers in the mitochondria, cytosol, and nuclei of brain cells during ammonia toxicity
    • Y.G. Kaminsky, E.A. Kosenko, N.I. Venediktova, V. Felipo, and C. Montoliu Apoptotic markers in the mitochondria, cytosol, and nuclei of brain cells during ammonia toxicity Neurochem. J. 1 2007 78 85
    • (2007) Neurochem. J. , vol.1 , pp. 78-85
    • Kaminsky, Y.G.1    Kosenko, E.A.2    Venediktova, N.I.3    Felipo, V.4    Montoliu, C.5
  • 22
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • R.M. Kluck, E. Bossy-Wetzel, D.R. Green, and D.D. Newmeyer The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis Science 275 1997 1132 1136
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 24
    • 2642586389 scopus 로고    scopus 로고
    • Acute ammonia intoxication induces an NMDA receptor-mediated increase in poly(ADP-ribose) polymerase level and NAD metabolism in nuclei of rat brain cells
    • E. Kosenko, C. Montoliu, G. Giordano, Y. Kaminsky, N. Venediktova, Y. Buryanov, and V. Felipo Acute ammonia intoxication induces an NMDA receptor-mediated increase in poly(ADP-ribose) polymerase level and NAD metabolism in nuclei of rat brain cells J. Neurochem. 89 2004 1101 1110
    • (2004) J. Neurochem. , vol.89 , pp. 1101-1110
    • Kosenko, E.1    Montoliu, C.2    Giordano, G.3    Kaminsky, Y.4    Venediktova, N.5    Buryanov, Y.6    Felipo, V.7
  • 25
    • 0031883959 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract
    • H.J. Lee, H. Sorimachi, S.Y. Jeong, S. Ishiura, and K. Suzuki Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract Biol. Chem. 379 1998 175 183
    • (1998) Biol. Chem. , vol.379 , pp. 175-183
    • Lee, H.J.1    Sorimachi, H.2    Jeong, S.Y.3    Ishiura, S.4    Suzuki, K.5
  • 26
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • P. Li, D. Nijhawan, I. Budihardjo, S.M. Srinivasula, M. Ahmad, E.S. Alnemri, and X. Wang Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade Cell 91 1997 479 489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 27
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • X. Liu, C.N. Kim, J. Yang, R. Jemmerson, and X. Wang Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c Cell 86 1996 147 157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 29
    • 33744514569 scopus 로고    scopus 로고
    • Roles of neuronal pathogenic proteins, glutamate receptors and mitochondria in the development of neurodegenerative diseases
    • A.V. Maltsev, E.A. Kosenko, N.I. Venediktova, and Y.G. Kaminsky Roles of neuronal pathogenic proteins, glutamate receptors and mitochondria in the development of neurodegenerative diseases Gerontologiya i Geriatriya 2 2003 78 83 (In Russian)
    • (2003) Gerontologiya i Geriatriya , vol.2 , pp. 78-83
    • Maltsev, A.V.1    Kosenko, E.A.2    Venediktova, N.I.3    Kaminsky, Y.G.4
  • 30
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • M. Manczak, T.S. Anekonda, E. Henson, B.S. Park, J. Quinn, and P.H. Red Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression Hum. Mol. Genet. 15 2006 1437 1449
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Red, P.H.6
  • 31
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • W.R. Markesbery Oxidative stress hypothesis in Alzheimer's disease Free Radic. Biol. Med. 23 1997 134 147
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 32
    • 0029836764 scopus 로고    scopus 로고
    • Correction in trans for Fabry disease: Expression, secretion and uptake of alpha-galactosidase A in patient-derived cells driven by a high-titer recombinant retroviral vector
    • J.A. Medin, M. Tudor, R. Simovitch, J.M. Quirk, S. Jacobson, G.J. Murray, and R.O. Brady Correction in trans for Fabry disease: expression, secretion and uptake of alpha-galactosidase A in patient-derived cells driven by a high-titer recombinant retroviral vector Proc. Natl. Acad. Sci. U. S. A. 93 1996 7917 7922
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7917-7922
    • Medin, J.A.1    Tudor, M.2    Simovitch, R.3    Quirk, J.M.4    Jacobson, S.5    Murray, G.J.6    Brady, R.O.7
  • 33
    • 0037192392 scopus 로고    scopus 로고
    • Induction of cytochrome c-mediated apoptosis by amyloid beta 25-35 requires functional mitochondria
    • S. Morais Cardoso, R.H. Swerdlow, and C.R. Oliveira Induction of cytochrome c-mediated apoptosis by amyloid beta 25-35 requires functional mitochondria Brain Res. 931 2002 117 125
    • (2002) Brain Res. , vol.931 , pp. 117-125
    • Morais Cardoso, S.1    Swerdlow, R.H.2    Oliveira, C.R.3
  • 35
    • 0019234255 scopus 로고
    • 2+-dependent arotease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin)
    • 2+-dependent arotease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin) Adv. Enzyme Regul. 19 1980 407 424
    • (1980) Adv. Enzyme Regul. , vol.19 , pp. 407-424
    • Murachi, T.1    Tanaka, K.2    Hatanaka, M.3    Murakami, T.4
  • 37
    • 0029085688 scopus 로고
    • Simple preparation of rat brain lysosomes and their proteolytic properties
    • T. Ohshita, and H. Kido Simple preparation of rat brain lysosomes and their proteolytic properties Anal. Biochem. 230 1995 41 47
    • (1995) Anal. Biochem. , vol.230 , pp. 41-47
    • Ohshita, T.1    Kido, H.2
  • 38
    • 0037073592 scopus 로고    scopus 로고
    • Memory impairment induced by chronic intracerebroventricular infusion of beta-amyloid (1-40) involves downregulation of protein kinase C
    • A. Olariu, K. Yamada, T. Mamiya, V. Hefco, and T. Nabeshima Memory impairment induced by chronic intracerebroventricular infusion of beta-amyloid (1-40) involves downregulation of protein kinase C Brain Res. 957 2002 278 286
    • (2002) Brain Res. , vol.957 , pp. 278-286
    • Olariu, A.1    Yamada, K.2    Mamiya, T.3    Hefco, V.4    Nabeshima, T.5
  • 39
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • G. Pan, K. O'Rourke, and V.M. Dixit Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex J. Biol. Chem. 273 1998 5841 5845
    • (1998) J. Biol. Chem. , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 41
    • 0034745636 scopus 로고    scopus 로고
    • Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro
    • J.K. Parks, T.S. Smith, P.A. Trimmer, J.P. Bennett, and W.D. Parker Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro J. Neurochem. 76 2001 1050 1056
    • (2001) J. Neurochem. , vol.76 , pp. 1050-1056
    • Parks, J.K.1    Smith, T.S.2    Trimmer, P.A.3    Bennett, J.P.4    Parker, W.D.5
  • 45
    • 33746126134 scopus 로고    scopus 로고
    • Implication of calpain in neuronal apoptosis. A possible regulation of Alzheimer's disease
    • F. Raynaud, and A. Marcilhac Implication of calpain in neuronal apoptosis. A possible regulation of Alzheimer's disease FEBS J. 273 2006 3437 3443
    • (2006) FEBS J. , vol.273 , pp. 3437-3443
    • Raynaud, F.1    Marcilhac, A.2
  • 46
    • 0001499607 scopus 로고
    • β-Amyloid and amyloid precursor protein: Chemistry, molecular biology, and neuropathology
    • N.K. Robakis β-Amyloid and amyloid precursor protein: chemistry, molecular biology, and neuropathology R. Terry, R. Kattmann, E. Bicke, Alzheimer's Disease 1994 Raven Press New York 317 326
    • (1994) Alzheimer's Disease , pp. 317-326
    • Robakis, N.K.1
  • 47
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • K. Saito, J.S. Elce, J.E. Hamos, and R.A. Nixon Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration Proc. Natl. Acad. Sci. U. S. A. 90 1993 2628 2632
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 48
    • 0036255318 scopus 로고    scopus 로고
    • Activity profile of calpains i and II in chronically infarcted rat myocardium-influence of the calpain inhibitor CAL 9961
    • S. Sandmann, F. Prenzel, L. Shaw, R. Schauer, and T. Unger Activity profile of calpains I and II in chronically infarcted rat myocardium-influence of the calpain inhibitor CAL 9961 Br. J. Pharmacol. 135 2002 1951 1958
    • (2002) Br. J. Pharmacol. , vol.135 , pp. 1951-1958
    • Sandmann, S.1    Prenzel, F.2    Shaw, L.3    Schauer, R.4    Unger, T.5
  • 50
    • 0025452640 scopus 로고
    • Proteolytic processing of beta-amyloid precursor by calpain i
    • R. Siman, J.P. Card, and L.G. Davis Proteolytic processing of beta-amyloid precursor by calpain I J. Neurosci. 10 1990 2400 2411
    • (1990) J. Neurosci. , vol.10 , pp. 2400-2411
    • Siman, R.1    Card, J.P.2    Davis, L.G.3
  • 51
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle
    • H. Sorimachi, S. Imajoh-Ohmi, Y. Emori, H. Kawasaki, S. Ohno, Y. Minami, and K. Suzuki Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle J. Biol. Chem. 264 1989 20106 20111
    • (1989) J. Biol. Chem. , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3    Kawasaki, H.4    Ohno, S.5    Minami, Y.6    Suzuki, K.7
  • 53
    • 33745228920 scopus 로고    scopus 로고
    • The various aggregation states of β-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression
    • E. Tamagno, P. Bardini, M. Guglielmotto, O. Danni, and M. Tabaton The various aggregation states of β-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression Free Radic. Biol. Med. 41 2006 202 212
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 202-212
    • Tamagno, E.1    Bardini, P.2    Guglielmotto, M.3    Danni, O.4    Tabaton, M.5
  • 54
    • 33745608709 scopus 로고    scopus 로고
    • The spirostenol (22R, 25R)-20alpha-spirost-5-en-3beta-yl hexanoate blocks mitochondrial uptake of Abeta in neuronal cells and prevents Abeta-induced impairment of mitochondrial function
    • L. Tillement, L. Lecanu, W. Yao, J. Greeson, and V. Papadopoulos The spirostenol (22R, 25R)-20alpha-spirost-5-en-3beta-yl hexanoate blocks mitochondrial uptake of Abeta in neuronal cells and prevents Abeta-induced impairment of mitochondrial function Steroids 71 2006 725 735
    • (2006) Steroids , vol.71 , pp. 725-735
    • Tillement, L.1    Lecanu, L.2    Yao, W.3    Greeson, J.4    Papadopoulos, V.5
  • 56
    • 7044262885 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide inhibits caspase-3 activity but does not protect cerebellar granule neurons against beta-amyloid (25-35)-induced apoptosis
    • D. Vaudry, C. Cottet-Rousselle, M. Basille, A. Falluel-Morel, A. Fournier, H. Vaudry, and B.J. Gonzalez Pituitary adenylate cyclase-activating polypeptide inhibits caspase-3 activity but does not protect cerebellar granule neurons against beta-amyloid (25-35)-induced apoptosis Regul. Pept. 123 2004 43 49
    • (2004) Regul. Pept. , vol.123 , pp. 43-49
    • Vaudry, D.1    Cottet-Rousselle, C.2    Basille, M.3    Falluel-Morel, A.4    Fournier, A.5    Vaudry, H.6    Gonzalez, B.J.7
  • 57
    • 0028180304 scopus 로고
    • 2+ channel blockers attenuate beta-amyloid peptide toxicity to cortical neurons in culture
    • 2+ channel blockers attenuate beta-amyloid peptide toxicity to cortical neurons in culture J. Neurochem. 62 1994 372 375
    • (1994) J. Neurochem. , vol.62 , pp. 372-375
    • Weiss, J.H.1    Pike, C.J.2    Cotman, C.W.3
  • 58
    • 0034981701 scopus 로고    scopus 로고
    • Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation
    • J. Xu, S. Chen, G. Ku, S.H. Ahmed, J. Xu, H. Chen, and C.Y. Hsu Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation J. Cereb. Blood Flow Metab. 21 2001 702 710
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 702-710
    • Xu, J.1    Chen, S.2    Ku, G.3    Ahmed, S.H.4    Xu, J.5    Chen, H.6    Hsu, C.Y.7
  • 59
    • 0021759029 scopus 로고
    • Purification and characterization of acid proteinase from human erythrocyte membranes
    • K. Yamamoto, and V.T. Marchesi Purification and characterization of acid proteinase from human erythrocyte membranes Biochim. Biophys. Acta 790 1984 208 218
    • (1984) Biochim. Biophys. Acta , vol.790 , pp. 208-218
    • Yamamoto, K.1    Marchesi, V.T.2
  • 60
    • 0032429784 scopus 로고    scopus 로고
    • Temporal relations among amyloid beta-peptide-induced free-radical oxidative stress, neuronal toxicity, and neuronal defensive responses
    • S.M. Yatin, M. Aksenova, M. Aksenov, W.R. Markesbery, T. Aulick, and D.A. Butterfield Temporal relations among amyloid beta-peptide-induced free-radical oxidative stress, neuronal toxicity, and neuronal defensive responses J. Mol. Neurosci. 11 1998 183 197
    • (1998) J. Mol. Neurosci. , vol.11 , pp. 183-197
    • Yatin, S.M.1    Aksenova, M.2    Aksenov, M.3    Markesbery, W.R.4    Aulick, T.5    Butterfield, D.A.6
  • 63
    • 1642464725 scopus 로고    scopus 로고
    • Genistein ameliorates beta-amyloid peptide (25-35)-induced hippocampal neuronal apoptosis
    • H. Zeng, Q. Chen, and B. Zhao Genistein ameliorates beta-amyloid peptide (25-35)-induced hippocampal neuronal apoptosis Free Radic. Biol. Med. 36 2004 180 188
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 180-188
    • Zeng, H.1    Chen, Q.2    Zhao, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.