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Volumn 1832, Issue 12, 2013, Pages 2191-2203

Activation of the endoplasmic reticulum stress response by the amyloid-beta 1-40 peptide in brain endothelial cells

Author keywords

Alzheimer's disease; Amyloid beta peptide; Apoptosis; Calcium homeostasis; Endoplasmic reticulum stress; Endothelial cells

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; APOPTOSIS INDUCING FACTOR; CALCIUM; CASPASE 12; CASPASE 3; CASPASE 9; CYTOCHROME C;

EID: 84883780939     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2013.08.007     Document Type: Article
Times cited : (111)

References (86)
  • 1
    • 80052266213 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics
    • Karran E., Mercken M., De Strooper B. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat. Rev. Drug Discov. 2011, 10:698-712.
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 698-712
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 2
    • 81555200043 scopus 로고    scopus 로고
    • Neurovascular pathways to neurodegeneration in Alzheimer's disease and other disorders
    • Zlokovic B.V. Neurovascular pathways to neurodegeneration in Alzheimer's disease and other disorders. Nat. Rev. 2011, 12:723-738.
    • (2011) Nat. Rev. , vol.12 , pp. 723-738
    • Zlokovic, B.V.1
  • 3
    • 77954560175 scopus 로고    scopus 로고
    • Vascular risk factors: imaging and neuropathologic correlates
    • Knopman D., Roberts R. Vascular risk factors: imaging and neuropathologic correlates. J. Alzheimers Dis. 2010, 20:699-709.
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 699-709
    • Knopman, D.1    Roberts, R.2
  • 5
    • 2342614850 scopus 로고    scopus 로고
    • Neurovascular regulation in the normal brain and in Alzheimer's disease
    • Iadecola C. Neurovascular regulation in the normal brain and in Alzheimer's disease. Nat. Rev. 2004, 5:347-360.
    • (2004) Nat. Rev. , vol.5 , pp. 347-360
    • Iadecola, C.1
  • 7
    • 78649526212 scopus 로고    scopus 로고
    • Capillary CAA and perivascular Abeta-deposition: two distinct features of Alzheimer's disease pathology
    • Attems J., Yamaguchi H., Saido T.C., Thal D.R. Capillary CAA and perivascular Abeta-deposition: two distinct features of Alzheimer's disease pathology. J. Neurol. Sci. 2010, 299:155-162.
    • (2010) J. Neurol. Sci. , vol.299 , pp. 155-162
    • Attems, J.1    Yamaguchi, H.2    Saido, T.C.3    Thal, D.R.4
  • 8
    • 25144486849 scopus 로고    scopus 로고
    • Cerebral microvascular amyloid beta protein deposition induces vascular degeneration and neuroinflammation in transgenic mice expressing human vasculotropic mutant amyloid beta precursor protein
    • Miao J., Xu F., Davis J., Otte-Holler I., Verbeek M.M., Van Nostrand W.E. Cerebral microvascular amyloid beta protein deposition induces vascular degeneration and neuroinflammation in transgenic mice expressing human vasculotropic mutant amyloid beta precursor protein. Am. J. Pathol. 2005, 167:505-515.
    • (2005) Am. J. Pathol. , vol.167 , pp. 505-515
    • Miao, J.1    Xu, F.2    Davis, J.3    Otte-Holler, I.4    Verbeek, M.M.5    Van Nostrand, W.E.6
  • 9
    • 76749138927 scopus 로고    scopus 로고
    • Mitochondrial mechanisms in amyloid beta peptide-induced cerebrovascular degeneration
    • Hsu M.J., Sheu J.R., Lin C.H., Shen M.Y., Hsu C.Y. Mitochondrial mechanisms in amyloid beta peptide-induced cerebrovascular degeneration. Biochim. Biophys. Acta 2010, 1800:290-296.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 290-296
    • Hsu, M.J.1    Sheu, J.R.2    Lin, C.H.3    Shen, M.Y.4    Hsu, C.Y.5
  • 12
    • 73949094104 scopus 로고    scopus 로고
    • Long-term incubation with beta-amyloid peptides impairs endothelium-dependent vasodilatation in isolated rat basilar artery
    • Chisari M., Merlo S., Sortino M., Salomone S. Long-term incubation with beta-amyloid peptides impairs endothelium-dependent vasodilatation in isolated rat basilar artery. Pharmacol. Res. 2010, 61:157-161.
    • (2010) Pharmacol. Res. , vol.61 , pp. 157-161
    • Chisari, M.1    Merlo, S.2    Sortino, M.3    Salomone, S.4
  • 13
    • 1242338809 scopus 로고    scopus 로고
    • Co-accumulation of vascular endothelial growth factor with beta-amyloid in the brain of patients with Alzheimer's disease
    • Yang S., Bae D., Kang H., Gwag B., Gho Y., Chae C. Co-accumulation of vascular endothelial growth factor with beta-amyloid in the brain of patients with Alzheimer's disease. Neurobiol. Aging 2004, 25:283-290.
    • (2004) Neurobiol. Aging , vol.25 , pp. 283-290
    • Yang, S.1    Bae, D.2    Kang, H.3    Gwag, B.4    Gho, Y.5    Chae, C.6
  • 15
    • 45549103421 scopus 로고    scopus 로고
    • AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response
    • Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F., Min W. AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response. J. Biol. Chem. 2008, 283:11905-11912.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11905-11912
    • Luo, D.1    He, Y.2    Zhang, H.3    Yu, L.4    Chen, H.5    Xu, Z.6    Tang, S.7    Urano, F.8    Min, W.9
  • 17
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin J.H., Walter P., Yen T.S. Endoplasmic reticulum stress in disease pathogenesis. Annu. Rev. Pathol. 2008, 3:399-425.
    • (2008) Annu. Rev. Pathol. , vol.3 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Yen, T.S.3
  • 18
    • 79954426601 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells
    • Kimata Y., Kohno K. Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells. Curr. Opin. Cell Biol. 2011, 23:135-142.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 135-142
    • Kimata, Y.1    Kohno, K.2
  • 21
    • 72449160579 scopus 로고    scopus 로고
    • The unfolded protein response and its relevance to connective tissue diseases
    • Boot-Handford R.P., Briggs M.D. The unfolded protein response and its relevance to connective tissue diseases. Cell Tissue Res. 2010, 339:197-211.
    • (2010) Cell Tissue Res. , vol.339 , pp. 197-211
    • Boot-Handford, R.P.1    Briggs, M.D.2
  • 23
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada T., Yoshida H., Akazawa R., Negishi M., Mori K. Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem. J. 2002, 366:585-594.
    • (2002) Biochem. J. , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 24
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S., Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 2004, 11:381-389.
    • (2004) Cell Death Differ. , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 26
    • 31444449462 scopus 로고    scopus 로고
    • Role of the unfolded protein response in cell death
    • Kim R., Emi M., Tanabe K., Murakami S. Role of the unfolded protein response in cell death. Apoptosis 2006, 11:5-13.
    • (2006) Apoptosis , vol.11 , pp. 5-13
    • Kim, R.1    Emi, M.2    Tanabe, K.3    Murakami, S.4
  • 27
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • Giorgi C., De Stefani D., Bononi A., Rizzuto R., Pinton P. Structural and functional link between the mitochondrial network and the endoplasmic reticulum. Int. J. Biochem. Cell Biol. 2009, 41:1817-1827.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 28
    • 43649083316 scopus 로고    scopus 로고
    • The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway
    • Ferreiro E., Oliveira C.R., Pereira C.M.F. The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway. Neurobiol. Dis. 2008, 30:331-342.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 331-342
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.M.F.3
  • 31
    • 60349129257 scopus 로고    scopus 로고
    • Constant illumination induces Alzheimer-like damages with endoplasmic reticulum involvement and the protection of melatonin
    • Ling Z., Tian Q., Wang L., Fu Z., Wang X., Wang Q., Wang J. Constant illumination induces Alzheimer-like damages with endoplasmic reticulum involvement and the protection of melatonin. J. Alzheimers Dis. 2009, 16:287-300.
    • (2009) J. Alzheimers Dis. , vol.16 , pp. 287-300
    • Ling, Z.1    Tian, Q.2    Wang, L.3    Fu, Z.4    Wang, X.5    Wang, Q.6    Wang, J.7
  • 32
    • 38349169247 scopus 로고    scopus 로고
    • Presenilin-1 mutation activates the signaling pathway of caspase-4 in endoplasmic reticulum stress-induced apoptosis
    • Yukioka F., Matsuzaki S., Kawamoto K., Koyama Y., Hitomi J., Katayama T., Tohyama M. Presenilin-1 mutation activates the signaling pathway of caspase-4 in endoplasmic reticulum stress-induced apoptosis. Neurochem. Int. 2008, 52:683-687.
    • (2008) Neurochem. Int. , vol.52 , pp. 683-687
    • Yukioka, F.1    Matsuzaki, S.2    Kawamoto, K.3    Koyama, Y.4    Hitomi, J.5    Katayama, T.6    Tohyama, M.7
  • 33
    • 80052646443 scopus 로고    scopus 로고
    • Presenilins function in ER calcium leak and Alzheimer's disease pathogenesis
    • Supnet C., Bezprozvanny I. Presenilins function in ER calcium leak and Alzheimer's disease pathogenesis. Cell Calcium 2011, 50:303-309.
    • (2011) Cell Calcium , vol.50 , pp. 303-309
    • Supnet, C.1    Bezprozvanny, I.2
  • 34
    • 33947271016 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides
    • Hoshino T., Nakaya T., Araki W., Suzuki K., Suzuki T., Mizushima T. Endoplasmic reticulum chaperones inhibit the production of amyloid-beta peptides. Biochem. J. 2007, 402:581-589.
    • (2007) Biochem. J. , vol.402 , pp. 581-589
    • Hoshino, T.1    Nakaya, T.2    Araki, W.3    Suzuki, K.4    Suzuki, T.5    Mizushima, T.6
  • 35
    • 0032475957 scopus 로고    scopus 로고
    • The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion
    • Yang Y., Turner R.S., Gaut J.R. The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. J. Biol. Chem. 1998, 273:25552-25555.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25552-25555
    • Yang, Y.1    Turner, R.S.2    Gaut, J.R.3
  • 37
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • Ferreiro E., Resende R., Costa R., Oliveira C.R., Pereira C.M.F. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol. Dis. 2006, 23:669-678.
    • (2006) Neurobiol. Dis. , vol.23 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.M.F.5
  • 38
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of Aβ1-42 peptide: involvement of endoplasmic reticulum calcium release in oligomers-induced cell death
    • Resende R., Ferreiro E., Pereira C., Oliveira C.R. Neurotoxic effect of oligomeric and fibrillar species of Aβ1-42 peptide: involvement of endoplasmic reticulum calcium release in oligomers-induced cell death. Neuroscience 2008, 155:725-737.
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Oliveira, C.R.4
  • 39
    • 2542625173 scopus 로고    scopus 로고
    • Alzheimer's disease-a sum greater than its parts?
    • Adlard P.A., Cummings B.J. Alzheimer's disease-a sum greater than its parts?. Neurobiol. Aging 2004, 25:725-733.
    • (2004) Neurobiol. Aging , vol.25 , pp. 725-733
    • Adlard, P.A.1    Cummings, B.J.2
  • 40
    • 0642280834 scopus 로고    scopus 로고
    • Development and characterization of immortalized cerebral endothelial cell lines
    • Couraud P.O., Greenwood J., Roux F., Adamson P. Development and characterization of immortalized cerebral endothelial cell lines. Methods Mol. Med. 2003, 89:349-364.
    • (2003) Methods Mol. Med. , vol.89 , pp. 349-364
    • Couraud, P.O.1    Greenwood, J.2    Roux, F.3    Adamson, P.4
  • 41
    • 0033022771 scopus 로고    scopus 로고
    • Involvement of oxidative stress on the impairment of energy metabolism induced by A beta peptides on PC12 cells: protection by antioxidants
    • Pereira C., Santos M.S., Oliveira C. Involvement of oxidative stress on the impairment of energy metabolism induced by A beta peptides on PC12 cells: protection by antioxidants. Neurobiol. Dis. 1999, 6:209-219.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 209-219
    • Pereira, C.1    Santos, M.S.2    Oliveira, C.3
  • 42
    • 0030757990 scopus 로고    scopus 로고
    • Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress
    • Pereira C.M., Oliveira C.R. Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress. Free Radic. Biol. Med. 1997, 23:637-647.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 637-647
    • Pereira, C.M.1    Oliveira, C.R.2
  • 44
    • 33745782720 scopus 로고    scopus 로고
    • Comparative study of microglia activation induced by amyloid-beta and prion peptides: role in neurodegeneration
    • Garção P., Oliveira C.R., Agostinho P. Comparative study of microglia activation induced by amyloid-beta and prion peptides: role in neurodegeneration. J. Neurosci. Res. 2006, 84:182-193.
    • (2006) J. Neurosci. Res. , vol.84 , pp. 182-193
    • Garção, P.1    Oliveira, C.R.2    Agostinho, P.3
  • 45
    • 74449092406 scopus 로고    scopus 로고
    • Effects of antioxidants on glucose-induced oxidative stress and endoplasmic reticulum stress in endothelial cells
    • Sheikh-Ali M., Sultan S., Alamir A.R., Haas M.J., Mooradian A.D. Effects of antioxidants on glucose-induced oxidative stress and endoplasmic reticulum stress in endothelial cells. Diabetes Res. Clin. Pract. 2010, 87:161-166.
    • (2010) Diabetes Res. Clin. Pract. , vol.87 , pp. 161-166
    • Sheikh-Ali, M.1    Sultan, S.2    Alamir, A.R.3    Haas, M.J.4    Mooradian, A.D.5
  • 46
    • 79961158316 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces retinal endothelial permeability of extracellular-superoxide dismutase
    • Adachi T., Yasuda H., Nakamura S., Kamiya T., Hara H., Hara H., Ikeda T. Endoplasmic reticulum stress induces retinal endothelial permeability of extracellular-superoxide dismutase. Free Radic. Res. 2011, 45:1083-1092.
    • (2011) Free Radic. Res. , vol.45 , pp. 1083-1092
    • Adachi, T.1    Yasuda, H.2    Nakamura, S.3    Kamiya, T.4    Hara, H.5    Hara, H.6    Ikeda, T.7
  • 47
    • 79960840653 scopus 로고    scopus 로고
    • Up-regulation of K(ir)2.1 by ER stress facilitates cell death of brain capillary endothelial cells
    • Kito H., Yamazaki D., Ohya S., Yamamura H., Asai K., Imaizumi Y. Up-regulation of K(ir)2.1 by ER stress facilitates cell death of brain capillary endothelial cells. Biochem. Biophys. Res. Commun. 2011, 411:293-298.
    • (2011) Biochem. Biophys. Res. Commun. , vol.411 , pp. 293-298
    • Kito, H.1    Yamazaki, D.2    Ohya, S.3    Yamamura, H.4    Asai, K.5    Imaizumi, Y.6
  • 50
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil G.S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010, 140:900-917.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 51
    • 84863484781 scopus 로고    scopus 로고
    • TRAIL death receptors DR4 and DR5 mediate cerebral microvascular endothelial cell apoptosis induced by oligomeric Alzheimer's Abeta
    • Fossati S., Ghiso J., Rostagno A. TRAIL death receptors DR4 and DR5 mediate cerebral microvascular endothelial cell apoptosis induced by oligomeric Alzheimer's Abeta. Cell Death Dis. 2012, 3:e321.
    • (2012) Cell Death Dis. , vol.3
    • Fossati, S.1    Ghiso, J.2    Rostagno, A.3
  • 52
    • 7644225312 scopus 로고    scopus 로고
    • RAGE (yin) versus LRP (yang) balance regulates Alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier
    • Deane R., Wu Z., Zlokovic B.V. RAGE (yin) versus LRP (yang) balance regulates Alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier. Stroke; J. Cereb. Circ. 2004, 35:2628-2631.
    • (2004) Stroke; J. Cereb. Circ. , vol.35 , pp. 2628-2631
    • Deane, R.1    Wu, Z.2    Zlokovic, B.V.3
  • 53
    • 33646166316 scopus 로고    scopus 로고
    • The role of the endoplasmic reticulum in the accumulation of beta-amyloid peptide in Alzheimer's disease
    • Ghribi O. The role of the endoplasmic reticulum in the accumulation of beta-amyloid peptide in Alzheimer's disease. Curr. Mol. Med. 2006, 6:119-133.
    • (2006) Curr. Mol. Med. , vol.6 , pp. 119-133
    • Ghribi, O.1
  • 55
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F.M. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. 2002, 3:862-872.
    • (2002) Nat. Rev. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 57
    • 0034657414 scopus 로고    scopus 로고
    • Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice
    • Leissring M.A., Akbari Y., Fanger C.M., Cahalan M.D., Mattson M.P., LaFerla F.M. Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice. J. Cell Biol. 2000, 149:793-798.
    • (2000) J. Cell Biol. , vol.149 , pp. 793-798
    • Leissring, M.A.1    Akbari, Y.2    Fanger, C.M.3    Cahalan, M.D.4    Mattson, M.P.5    LaFerla, F.M.6
  • 58
    • 77954515355 scopus 로고    scopus 로고
    • Presenilin-1 holoprotein is an interacting partner of sarco endoplasmic reticulum calcium-ATPase and confers resistance to endoplasmic reticulum stress
    • Jin H., Sanjo N., Uchihara T., Watabe K., St George-Hyslop P., Fraser P.E., Mizusawa H. Presenilin-1 holoprotein is an interacting partner of sarco endoplasmic reticulum calcium-ATPase and confers resistance to endoplasmic reticulum stress. J. Alzheimers Dis. 2010, 20:261-273.
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 261-273
    • Jin, H.1    Sanjo, N.2    Uchihara, T.3    Watabe, K.4    St George-Hyslop, P.5    Fraser, P.E.6    Mizusawa, H.7
  • 60
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 2002, 32:269-278.
    • (2002) Cell Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Robert Parker, J.M.2    Opas, M.3
  • 61
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schröder M. Endoplasmic reticulum stress responses. Cell. Mol. Life Sci. 2008, 65:862-894.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 862-894
    • Schröder, M.1
  • 62
    • 77549084517 scopus 로고    scopus 로고
    • The dysregulation of intracellular calcium in Alzheimer disease
    • Supnet C., Bezprozvanny I. The dysregulation of intracellular calcium in Alzheimer disease. Cell Calcium 2010, 47:183-189.
    • (2010) Cell Calcium , vol.47 , pp. 183-189
    • Supnet, C.1    Bezprozvanny, I.2
  • 63
    • 70350304571 scopus 로고    scopus 로고
    • Calcium dysregulation in Alzheimer's disease: from mechanisms to therapeutic opportunities
    • Yu J.T., Chang R.C., Tan L. Calcium dysregulation in Alzheimer's disease: from mechanisms to therapeutic opportunities. Prog. Neurobiol. 2009, 89:240-255.
    • (2009) Prog. Neurobiol. , vol.89 , pp. 240-255
    • Yu, J.T.1    Chang, R.C.2    Tan, L.3
  • 65
    • 84875867608 scopus 로고    scopus 로고
    • Cerebral atrophy in mild cognitive impairment and Alzheimer disease: rates and acceleration
    • Leung K.K., Bartlett J.W., Barnes J., Manning E.N., Ourselin S., Fox N.C. Cerebral atrophy in mild cognitive impairment and Alzheimer disease: rates and acceleration. Neurology 2013, 80:648-654.
    • (2013) Neurology , vol.80 , pp. 648-654
    • Leung, K.K.1    Bartlett, J.W.2    Barnes, J.3    Manning, E.N.4    Ourselin, S.5    Fox, N.C.6
  • 66
    • 84860580628 scopus 로고    scopus 로고
    • Caspase-3 activation as a bifurcation point between plasticity and cell death
    • Snigdha S., Smith E.D., Prieto G.A., Cotman C.W. Caspase-3 activation as a bifurcation point between plasticity and cell death. Neurosci. Bull. 2012, 28:14-24.
    • (2012) Neurosci. Bull. , vol.28 , pp. 14-24
    • Snigdha, S.1    Smith, E.D.2    Prieto, G.A.3    Cotman, C.W.4
  • 68
    • 0031017399 scopus 로고    scopus 로고
    • Rapid degeneration of cultured human brain pericytes by amyloid beta protein
    • Verbeek M.M., de Waal R.M., Schipper J.J., Van Nostrand W.E. Rapid degeneration of cultured human brain pericytes by amyloid beta protein. J. Neurochem. 1997, 68:1135-1141.
    • (1997) J. Neurochem. , vol.68 , pp. 1135-1141
    • Verbeek, M.M.1    de Waal, R.M.2    Schipper, J.J.3    Van Nostrand, W.E.4
  • 69
    • 0039228392 scopus 로고    scopus 로고
    • Pathogenic amyloid beta-protein induces apoptosis in cultured human cerebrovascular smooth muscle cells
    • Davis J., Cribbs D.H., Cotman C.W., Van Nostrand W.E. Pathogenic amyloid beta-protein induces apoptosis in cultured human cerebrovascular smooth muscle cells. Amyloid 1999, 6:157-164.
    • (1999) Amyloid , vol.6 , pp. 157-164
    • Davis, J.1    Cribbs, D.H.2    Cotman, C.W.3    Van Nostrand, W.E.4
  • 71
    • 18344384228 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium pool depletion-induced apoptosis is coupled with activation of the death receptor 5 pathway
    • He Q., Lee D.I., Rong R., Yu M., Luo X., Klein M., El-Deiry W.S., Huang Y., Hussain A., Sheikh M.S. Endoplasmic reticulum calcium pool depletion-induced apoptosis is coupled with activation of the death receptor 5 pathway. Oncogene 2002, 21:2623-2633.
    • (2002) Oncogene , vol.21 , pp. 2623-2633
    • He, Q.1    Lee, D.I.2    Rong, R.3    Yu, M.4    Luo, X.5    Klein, M.6    El-Deiry, W.S.7    Huang, Y.8    Hussain, A.9    Sheikh, M.S.10
  • 72
    • 84859882828 scopus 로고    scopus 로고
    • Neuronal calcium signaling and Alzheimer's disease
    • Woods N.K., Padmanabhan J. Neuronal calcium signaling and Alzheimer's disease. Adv. Exp. Med. Biol. 2012, 740:1193-1217.
    • (2012) Adv. Exp. Med. Biol. , vol.740 , pp. 1193-1217
    • Woods, N.K.1    Padmanabhan, J.2
  • 73
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra J.D., Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 2007, 18:716-731.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 75
    • 66149102423 scopus 로고    scopus 로고
    • Mechanisms of endothelial dysfunction, injury, and death
    • Pober J.S., Min W., Bradley J.R. Mechanisms of endothelial dysfunction, injury, and death. Annu. Rev. Pathol. 2009, 4:71-95.
    • (2009) Annu. Rev. Pathol. , vol.4 , pp. 71-95
    • Pober, J.S.1    Min, W.2    Bradley, J.R.3
  • 76
    • 84858169363 scopus 로고    scopus 로고
    • PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration
    • Chaitanya G.V., Steven A.J., Babu P.P. PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration. Cell Commun. Signal 2010, 8:31.
    • (2010) Cell Commun. Signal , vol.8 , pp. 31
    • Chaitanya, G.V.1    Steven, A.J.2    Babu, P.P.3
  • 77
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000, 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 78
    • 34147141497 scopus 로고    scopus 로고
    • Switch between apoptosis and autophagy: radiation-induced endoplasmic reticulum stress?
    • (Georgetown, Tex)
    • Moretti L., Cha Y.I., Niermann K.J., Lu B. Switch between apoptosis and autophagy: radiation-induced endoplasmic reticulum stress?. Cell Cycle 2007, 6:793-798. (Georgetown, Tex).
    • (2007) Cell Cycle , vol.6 , pp. 793-798
    • Moretti, L.1    Cha, Y.I.2    Niermann, K.J.3    Lu, B.4
  • 80
    • 77958608037 scopus 로고    scopus 로고
    • Hydrogen peroxide regulates glucose-regulated protein 78 expression via a cyclooxygenase-2 dependent mechanism
    • Chen Y.Y., Zheng M.Z., Lv P.P., Hu L., Wang L.L., Shen Y.L. Hydrogen peroxide regulates glucose-regulated protein 78 expression via a cyclooxygenase-2 dependent mechanism. J. Biochem. Mol. Toxicol. 2010, 24:279-285.
    • (2010) J. Biochem. Mol. Toxicol. , vol.24 , pp. 279-285
    • Chen, Y.Y.1    Zheng, M.Z.2    Lv, P.P.3    Hu, L.4    Wang, L.L.5    Shen, Y.L.6
  • 82
    • 14844328621 scopus 로고    scopus 로고
    • Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria
    • Polster B.M., Basanez G., Etxebarria A., Hardwick J.M., Nicholls D.G. Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria. J. Biol. Chem. 2005, 280:6447-6454.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6447-6454
    • Polster, B.M.1    Basanez, G.2    Etxebarria, A.3    Hardwick, J.M.4    Nicholls, D.G.5
  • 84
    • 80051668693 scopus 로고    scopus 로고
    • Apoptosis: why and how does it occur in biology?
    • Ulukaya E., Acilan C., Yilmaz Y. Apoptosis: why and how does it occur in biology?. Cell Biochem. Funct. 2011, 29:468-480.
    • (2011) Cell Biochem. Funct. , vol.29 , pp. 468-480
    • Ulukaya, E.1    Acilan, C.2    Yilmaz, Y.3
  • 85
    • 77957316569 scopus 로고    scopus 로고
    • Restoring endoplasmic reticulum function by chemical chaperones: an emerging therapeutic approach for metabolic diseases
    • Engin F., Hotamisligil G.S. Restoring endoplasmic reticulum function by chemical chaperones: an emerging therapeutic approach for metabolic diseases. Diabetes Obes. Metab. 2010, 12(Suppl. 2):108-115.
    • (2010) Diabetes Obes. Metab. , vol.12 , Issue.SUPPL. 2 , pp. 108-115
    • Engin, F.1    Hotamisligil, G.S.2
  • 86
    • 84859799949 scopus 로고    scopus 로고
    • Stress management at the ER: regulators of ER stress-induced apoptosis
    • Gorman A.M., Healy S.J., Jager R., Samali A. Stress management at the ER: regulators of ER stress-induced apoptosis. Pharmacol. Ther. 2012, 134:306-316.
    • (2012) Pharmacol. Ther. , vol.134 , pp. 306-316
    • Gorman, A.M.1    Healy, S.J.2    Jager, R.3    Samali, A.4


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