메뉴 건너뛰기




Volumn 1800, Issue 3, 2010, Pages 290-296

Mitochondrial mechanisms in amyloid beta peptide-induced cerebrovascular degeneration

Author keywords

Aging; Amyloid beta peptide; Apoptosis; Ceramide; Cerebrovascular disease; Endothelial cells; Mitochondria; Stroke

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; APOPTOSIS INDUCING FACTOR; APOPTOSIS SIGNAL REGULATING KINASE 1; BIM PROTEIN; CERAMIDE; CYTOCHROME C; ENDONUCLEASE G; GLYCOGEN SYNTHASE KINASE 3BETA; MITOCHONDRIAL DNA; MITOGEN ACTIVATED PROTEIN KINASE KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; MITOGEN ACTIVATED PROTEIN KINASE KINASE 6; MITOGEN ACTIVATED PROTEIN KINASE KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN BAD; PROTEIN BAX; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR FKHRL1; X LINKED INHIBITOR OF APOPTOSIS;

EID: 76749138927     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.08.003     Document Type: Review
Times cited : (35)

References (135)
  • 1
    • 0031705997 scopus 로고    scopus 로고
    • Aging and cerebrovascular disease
    • Choi J.Y., Morris J.C., and Hsu C.Y. Aging and cerebrovascular disease. Neurol. Clin. 16 (1998) 687-711
    • (1998) Neurol. Clin. , vol.16 , pp. 687-711
    • Choi, J.Y.1    Morris, J.C.2    Hsu, C.Y.3
  • 3
    • 0022609354 scopus 로고
    • Histochemical study of the anulus fibrosus in normal canine caudal cervical intervertebral discs
    • Burke M.J., Banks W.J., Nelson A.W., and Seim H.B. Histochemical study of the anulus fibrosus in normal canine caudal cervical intervertebral discs. Res. Vet. Sci. 40 (1986) 18-23
    • (1986) Res. Vet. Sci. , vol.40 , pp. 18-23
    • Burke, M.J.1    Banks, W.J.2    Nelson, A.W.3    Seim, H.B.4
  • 4
    • 0025289830 scopus 로고
    • Effect of aging on endothelium-dependent vascular relaxation of isolated human basilar artery to thrombin and bradykinin
    • Hatake K., Kakishita E., Wakabayashi I., Sakiyama N., and Hishida S. Effect of aging on endothelium-dependent vascular relaxation of isolated human basilar artery to thrombin and bradykinin. Stroke 21 (1990) 1039-1043
    • (1990) Stroke , vol.21 , pp. 1039-1043
    • Hatake, K.1    Kakishita, E.2    Wakabayashi, I.3    Sakiyama, N.4    Hishida, S.5
  • 5
    • 0026800665 scopus 로고
    • Carnitine acetyltransferase activity in the human brain and its microvessels is decreased in Alzheimer's disease
    • Kalaria R.N., and Harik S.I. Carnitine acetyltransferase activity in the human brain and its microvessels is decreased in Alzheimer's disease. Ann. Neurol. 32 (1992) 583-586
    • (1992) Ann. Neurol. , vol.32 , pp. 583-586
    • Kalaria, R.N.1    Harik, S.I.2
  • 6
    • 0029119684 scopus 로고
    • Vascular pathology in the elderly
    • Hsu C.Y., and Hu Z.Y. Vascular pathology in the elderly. Eur. Neurol. 35 Suppl 1 (1995) 2-4
    • (1995) Eur. Neurol. , vol.35 , Issue.SUPPL. 1 , pp. 2-4
    • Hsu, C.Y.1    Hu, Z.Y.2
  • 7
    • 0030452414 scopus 로고    scopus 로고
    • Cerebral vessels in ageing and Alzheimer's disease
    • Kalaria R.N. Cerebral vessels in ageing and Alzheimer's disease. Pharmacol. Ther. 72 (1996) 193-214
    • (1996) Pharmacol. Ther. , vol.72 , pp. 193-214
    • Kalaria, R.N.1
  • 9
    • 0029896438 scopus 로고    scopus 로고
    • beta-Amyloid vasoactivity in Alzheimer's disease
    • Kalaria R.N., and Hedera P. beta-Amyloid vasoactivity in Alzheimer's disease. Lancet 347 (1996) 1492-1493
    • (1996) Lancet , vol.347 , pp. 1492-1493
    • Kalaria, R.N.1    Hedera, P.2
  • 10
    • 0030663141 scopus 로고    scopus 로고
    • Cerebrovascular degeneration is related to amyloid-beta protein deposition in Alzheimer's disease
    • Kalaria R.N. Cerebrovascular degeneration is related to amyloid-beta protein deposition in Alzheimer's disease. Ann. N. Y. Acad. Sci. 826 (1997) 263-271
    • (1997) Ann. N. Y. Acad. Sci. , vol.826 , pp. 263-271
    • Kalaria, R.N.1
  • 11
    • 0030833582 scopus 로고    scopus 로고
    • beta-Amyloid (A beta) deposition in the brains of aged orangutans
    • Gearing M., Tigges J., Mori H., and Mirra S.S. beta-Amyloid (A beta) deposition in the brains of aged orangutans. Neurobiol. Aging 18 (1997) 139-146
    • (1997) Neurobiol. Aging , vol.18 , pp. 139-146
    • Gearing, M.1    Tigges, J.2    Mori, H.3    Mirra, S.S.4
  • 12
    • 0030779705 scopus 로고    scopus 로고
    • Animal models of cerebral beta-amyloid angiopathy
    • Walker L.C. Animal models of cerebral beta-amyloid angiopathy. Brain Res. Brain Res. Rev. 25 (1997) 70-84
    • (1997) Brain Res. Brain Res. Rev. , vol.25 , pp. 70-84
    • Walker, L.C.1
  • 13
    • 0026558595 scopus 로고
    • Identification of a stable fragment of the Alzheimer amyloid precursor containing the beta-protein in brain microvessels
    • Tamaoka A., Kalaria R.N., Lieberburg I., and Selkoe D.J. Identification of a stable fragment of the Alzheimer amyloid precursor containing the beta-protein in brain microvessels. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 1345-1349
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 1345-1349
    • Tamaoka, A.1    Kalaria, R.N.2    Lieberburg, I.3    Selkoe, D.J.4
  • 14
    • 0028350718 scopus 로고
    • Pathological alterations of the cerebral microvasculature in Alzheimer's disease and related dementing disorders
    • Buee L., Hof P.R., Bouras C., Delacourte A., Perl D.P., Morrison J.H., and Fillit H.M. Pathological alterations of the cerebral microvasculature in Alzheimer's disease and related dementing disorders. Acta Neuropathol. 87 (1994) 469-480
    • (1994) Acta Neuropathol. , vol.87 , pp. 469-480
    • Buee, L.1    Hof, P.R.2    Bouras, C.3    Delacourte, A.4    Perl, D.P.5    Morrison, J.H.6    Fillit, H.M.7
  • 15
    • 0028872740 scopus 로고
    • Differential degeneration of the cerebral microvasculature in Alzheimer's disease
    • Kalaria R.N., and Hedera P. Differential degeneration of the cerebral microvasculature in Alzheimer's disease. NeuroReport 6 (1995) 477-480
    • (1995) NeuroReport , vol.6 , pp. 477-480
    • Kalaria, R.N.1    Hedera, P.2
  • 16
    • 13544268809 scopus 로고    scopus 로고
    • Neurovascular mechanisms of Alzheimer's neurodegeneration
    • Zlokovic B.V. Neurovascular mechanisms of Alzheimer's neurodegeneration. Trends Neurosci. 28 (2005) 202-208
    • (2005) Trends Neurosci. , vol.28 , pp. 202-208
    • Zlokovic, B.V.1
  • 19
    • 0031593597 scopus 로고    scopus 로고
    • The influence of coincidental vascular pathology on symptomatology and course of Alzheimer's disease
    • Pasquier F., Leys D., and Scheltens P. The influence of coincidental vascular pathology on symptomatology and course of Alzheimer's disease. J. Neural. Transm. Suppl. 54 (1998) 117-127
    • (1998) J. Neural. Transm. Suppl. , vol.54 , pp. 117-127
    • Pasquier, F.1    Leys, D.2    Scheltens, P.3
  • 20
    • 0025369198 scopus 로고
    • M. Vegter-Van der Vlis, R.A. Roos, Amyloid beta protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch)
    • Van Broeckhoven C., Haan J., Bakker E., Hardy J.A., Van Hul W., and Wehnert A. M. Vegter-Van der Vlis, R.A. Roos, Amyloid beta protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch). Science 248 (1990) 1120-1122
    • (1990) Science , vol.248 , pp. 1120-1122
    • Van Broeckhoven, C.1    Haan, J.2    Bakker, E.3    Hardy, J.A.4    Van Hul, W.5    Wehnert, A.6
  • 21
    • 0028335790 scopus 로고
    • Co-localization of beta/A4 and cystatin C in cortical blood vessels in Dutch, but not in Icelandic hereditary cerebral hemorrhage with amyloidosis
    • Haan J., Maat-Schieman M.L., van Duinen S.G., Jensson O., Thorsteinsson L., and Roos R.A. Co-localization of beta/A4 and cystatin C in cortical blood vessels in Dutch, but not in Icelandic hereditary cerebral hemorrhage with amyloidosis. Acta Neurol. Scand. 89 (1994) 367-371
    • (1994) Acta Neurol. Scand. , vol.89 , pp. 367-371
    • Haan, J.1    Maat-Schieman, M.L.2    van Duinen, S.G.3    Jensson, O.4    Thorsteinsson, L.5    Roos, R.A.6
  • 22
    • 0029920991 scopus 로고    scopus 로고
    • Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein
    • Davis J., and Van Nostrand W.E. Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 2996-3000
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 2996-3000
    • Davis, J.1    Van Nostrand, W.E.2
  • 23
    • 0029742659 scopus 로고    scopus 로고
    • Abundance of the longer A beta 42 in neocortical and cerebrovascular amyloid beta deposits in Swedish familial Alzheimer's disease and Down's syndrome
    • Kalaria R.N., Cohen D.L., Greenberg B.D., Savage M.J., Bogdanovic N.E., Winblad B., Lannfelt L., and Adem A. Abundance of the longer A beta 42 in neocortical and cerebrovascular amyloid beta deposits in Swedish familial Alzheimer's disease and Down's syndrome. NeuroReport 7 (1996) 1377-1381
    • (1996) NeuroReport , vol.7 , pp. 1377-1381
    • Kalaria, R.N.1    Cohen, D.L.2    Greenberg, B.D.3    Savage, M.J.4    Bogdanovic, N.E.5    Winblad, B.6    Lannfelt, L.7    Adem, A.8
  • 26
    • 0032496147 scopus 로고    scopus 로고
    • Instability of the amyloidogenic cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type
    • Wei L., Berman Y., Castano E.M., Cadene M., Beavis R.C., Devi L., and Levy E. Instability of the amyloidogenic cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type. J. Biol. Chem. 273 (1998) 11806-11814
    • (1998) J. Biol. Chem. , vol.273 , pp. 11806-11814
    • Wei, L.1    Berman, Y.2    Castano, E.M.3    Cadene, M.4    Beavis, R.C.5    Devi, L.6    Levy, E.7
  • 27
    • 13844298168 scopus 로고    scopus 로고
    • Pattern of cerebral hypoperfusion in Alzheimer disease and mild cognitive impairment measured with arterial spin-labeling MR imaging: initial experience
    • Johnson N.A., Jahng G.H., Weiner M.W., Miller B.L., Chui H.C., Jagust W.J., Gorno-Tempini M.L., and Schuff N. Pattern of cerebral hypoperfusion in Alzheimer disease and mild cognitive impairment measured with arterial spin-labeling MR imaging: initial experience. Radiology 234 (2005) 851-859
    • (2005) Radiology , vol.234 , pp. 851-859
    • Johnson, N.A.1    Jahng, G.H.2    Weiner, M.W.3    Miller, B.L.4    Chui, H.C.5    Jagust, W.J.6    Gorno-Tempini, M.L.7    Schuff, N.8
  • 29
    • 30844472909 scopus 로고    scopus 로고
    • IgG-assisted age-dependent clearance of Alzheimer's amyloid beta peptide by the blood-brain barrier neonatal Fc receptor
    • Deane R., Sagare A., Hamm K., Parisi M., LaRue B., Guo H., Wu Z., Holtzman D.M., and Zlokovic B.V. IgG-assisted age-dependent clearance of Alzheimer's amyloid beta peptide by the blood-brain barrier neonatal Fc receptor. J. Neurosci. 25 (2005) 11495-11503
    • (2005) J. Neurosci. , vol.25 , pp. 11495-11503
    • Deane, R.1    Sagare, A.2    Hamm, K.3    Parisi, M.4    LaRue, B.5    Guo, H.6    Wu, Z.7    Holtzman, D.M.8    Zlokovic, B.V.9
  • 30
    • 48949117577 scopus 로고    scopus 로고
    • The role of the cell surface LRP and soluble LRP in blood-brain barrier Abeta clearance in Alzheimer's disease
    • Deane R., Sagare A., and Zlokovic B.V. The role of the cell surface LRP and soluble LRP in blood-brain barrier Abeta clearance in Alzheimer's disease. Curr. Pharm. Des. 14 (2008) 1601-1605
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 1601-1605
    • Deane, R.1    Sagare, A.2    Zlokovic, B.V.3
  • 31
    • 0021849039 scopus 로고
    • Leukoencephalopathy in diffuse hemorrhagic cerebral amyloid angiopathy
    • Gray F., Dubas F., Roullet E., and Escourolle R. Leukoencephalopathy in diffuse hemorrhagic cerebral amyloid angiopathy. Ann. Neurol. 18 (1985) 54-59
    • (1985) Ann. Neurol. , vol.18 , pp. 54-59
    • Gray, F.1    Dubas, F.2    Roullet, E.3    Escourolle, R.4
  • 32
    • 0025996902 scopus 로고
    • The significance of cerebrovascular amyloid in the aetiology of superficial (lobar) cerebral haemorrhage and its incidence in the elderly population
    • Ishihara T., Takahashi M., Yokota T., Yamashita Y., Gondo T., Uchino F., and Iwamoto N. The significance of cerebrovascular amyloid in the aetiology of superficial (lobar) cerebral haemorrhage and its incidence in the elderly population. J. Pathol. 165 (1991) 229-234
    • (1991) J. Pathol. , vol.165 , pp. 229-234
    • Ishihara, T.1    Takahashi, M.2    Yokota, T.3    Yamashita, Y.4    Gondo, T.5    Uchino, F.6    Iwamoto, N.7
  • 33
    • 0029973286 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy in the brains of patients with Alzheimer's disease: the CERAD experience. Part XV
    • Ellis R.J., Olichney J.M., Thal L.J., Mirra S.S., Morris J.C., Beekly D., and Heyman A. Cerebral amyloid angiopathy in the brains of patients with Alzheimer's disease: the CERAD experience. Part XV. Neurology 46 (1996) 1592-1596
    • (1996) Neurology , vol.46 , pp. 1592-1596
    • Ellis, R.J.1    Olichney, J.M.2    Thal, L.J.3    Mirra, S.S.4    Morris, J.C.5    Beekly, D.6    Heyman, A.7
  • 35
    • 0023254674 scopus 로고
    • Cerebral amyloid angiopathy. A critical review
    • Vinters H.V. Cerebral amyloid angiopathy. A critical review. Stroke 18 (1987) 311-324
    • (1987) Stroke , vol.18 , pp. 311-324
    • Vinters, H.V.1
  • 37
    • 0027440372 scopus 로고
    • The clinical spectrum of cerebral amyloid angiopathy: presentations without lobar hemorrhage
    • Greenberg S.M., Vonsattel J.P., Stakes J.W., Gruber M., and Finklestein S.P. The clinical spectrum of cerebral amyloid angiopathy: presentations without lobar hemorrhage. Neurology 43 (1993) 2073-2079
    • (1993) Neurology , vol.43 , pp. 2073-2079
    • Greenberg, S.M.1    Vonsattel, J.P.2    Stakes, J.W.3    Gruber, M.4    Finklestein, S.P.5
  • 38
    • 0029038881 scopus 로고
    • Cerebral infarction in Alzheimer's disease is associated with severe amyloid angiopathy and hypertension
    • Olichney J.M., Hansen L.A., Hofstetter C.R., Grundman M., Katzman R., and Thal L.J. Cerebral infarction in Alzheimer's disease is associated with severe amyloid angiopathy and hypertension. Arch. Neurol. 52 (1995) 702-708
    • (1995) Arch. Neurol. , vol.52 , pp. 702-708
    • Olichney, J.M.1    Hansen, L.A.2    Hofstetter, C.R.3    Grundman, M.4    Katzman, R.5    Thal, L.J.6
  • 39
    • 0029655250 scopus 로고    scopus 로고
    • Ultrastructural features of the blood-brain barrier in biopsy tissue from Alzheimer's disease patients
    • Claudio L. Ultrastructural features of the blood-brain barrier in biopsy tissue from Alzheimer's disease patients. Acta Neuropathol. 91 (1996) 6-14
    • (1996) Acta Neuropathol. , vol.91 , pp. 6-14
    • Claudio, L.1
  • 41
    • 0027761330 scopus 로고
    • Distribution of beta/A4 protein and amyloid precursor protein in hereditary cerebral hemorrhage with amyloidosis-Dutch type and Alzheimer's disease
    • Rozemuller A.J., Roos R.A., Bots G.T., Kamphorst W., Eikelenboom P., and Van Nostrand W.E. Distribution of beta/A4 protein and amyloid precursor protein in hereditary cerebral hemorrhage with amyloidosis-Dutch type and Alzheimer's disease. Am. J. Pathol. 142 (1993) 1449-1457
    • (1993) Am. J. Pathol. , vol.142 , pp. 1449-1457
    • Rozemuller, A.J.1    Roos, R.A.2    Bots, G.T.3    Kamphorst, W.4    Eikelenboom, P.5    Van Nostrand, W.E.6
  • 42
    • 0029873575 scopus 로고    scopus 로고
    • Amyloid beta-protein induces the cerebrovascular cellular pathology of Alzheimer's disease and related disorders
    • Van Nostrand W.E., Davis-Salinas J., and Saporito-Irwin S.M. Amyloid beta-protein induces the cerebrovascular cellular pathology of Alzheimer's disease and related disorders. Ann. N. Y. Acad. Sci. 777 (1996) 297-302
    • (1996) Ann. N. Y. Acad. Sci. , vol.777 , pp. 297-302
    • Van Nostrand, W.E.1    Davis-Salinas, J.2    Saporito-Irwin, S.M.3
  • 43
    • 0031983456 scopus 로고    scopus 로고
    • Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells
    • Van Nostrand W.E., Melchor J.P., and Ruffini L. Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. J Neurochem 70 (1998) 216-223
    • (1998) J Neurochem , vol.70 , pp. 216-223
    • Van Nostrand, W.E.1    Melchor, J.P.2    Ruffini, L.3
  • 44
    • 0026631036 scopus 로고
    • The seminal role of beta-amyloid in the pathogenesis of Alzheimer disease
    • Joachim C.L., and Selkoe D.J. The seminal role of beta-amyloid in the pathogenesis of Alzheimer disease. Alzheimer Dis. Assoc. Disord. 6 (1992) 7-34
    • (1992) Alzheimer Dis. Assoc. Disord. , vol.6 , pp. 7-34
    • Joachim, C.L.1    Selkoe, D.J.2
  • 45
    • 0029927290 scopus 로고    scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D): II-A review of histopathological aspects
    • Maat-Schieman M.L., van Duinen S.G., Bornebroek M., Haan J., and Roos R.A. Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D): II-A review of histopathological aspects. Brain Pathol. 6 (1996) 115-120
    • (1996) Brain Pathol. , vol.6 , pp. 115-120
    • Maat-Schieman, M.L.1    van Duinen, S.G.2    Bornebroek, M.3    Haan, J.4    Roos, R.A.5
  • 46
    • 0029975660 scopus 로고    scopus 로고
    • Brain parenchymal and microvascular amyloid in Alzheimer's disease
    • Vinters H.V., Wang Z.Z., and Secor D.L. Brain parenchymal and microvascular amyloid in Alzheimer's disease. Brain Pathol. 6 (1996) 179-195
    • (1996) Brain Pathol. , vol.6 , pp. 179-195
    • Vinters, H.V.1    Wang, Z.Z.2    Secor, D.L.3
  • 49
    • 0030007964 scopus 로고    scopus 로고
    • Sequence of deposition of heterogeneous amyloid beta-peptides and APO E in Down syndrome: implications for initial events in amyloid plaque formation
    • Lemere C.A., Blusztajn J.K., Yamaguchi H., Wisniewski T., Saido T.C., and Selkoe D.J. Sequence of deposition of heterogeneous amyloid beta-peptides and APO E in Down syndrome: implications for initial events in amyloid plaque formation. Neurobiol. Dis. 3 (1996) 16-32
    • (1996) Neurobiol. Dis. , vol.3 , pp. 16-32
    • Lemere, C.A.1    Blusztajn, J.K.2    Yamaguchi, H.3    Wisniewski, T.4    Saido, T.C.5    Selkoe, D.J.6
  • 50
  • 52
    • 0030665870 scopus 로고    scopus 로고
    • Variable deposition of amyloid beta-protein
    • Akiyama H., Mori H., Sahara N., Kondo H., Ikeda K., Nishimura T., Oda T., and McGeer P.L. Variable deposition of amyloid beta-protein (A beta) with the carboxy-terminus that ends at residue valine40 (A beta 40) in the cerebral cortex of patients with Alzheimer's disease: a double-labeling immunohistochemical study with antibodies specific for A beta 40 and the A beta that ends at residues alanine42/threonine43 (A beta 42). Neurochem. Res. 22 (1997) 1499-1506
    • (1997) Neurochem. Res. , vol.22 , pp. 1499-1506
    • Akiyama, H.1    Mori, H.2    Sahara, N.3    Kondo, H.4    Ikeda, K.5    Nishimura, T.6    Oda, T.7    McGeer, P.L.8
  • 55
    • 0033943469 scopus 로고    scopus 로고
    • Clearance of amyloid beta-peptide from brain: transport or metabolism?
    • Zlokovic B.V., Yamada S., Holtzman D., Ghiso J., and Frangione B. Clearance of amyloid beta-peptide from brain: transport or metabolism?. Nat. Med. 6 (2000) 718-719
    • (2000) Nat. Med. , vol.6 , pp. 718-719
    • Zlokovic, B.V.1    Yamada, S.2    Holtzman, D.3    Ghiso, J.4    Frangione, B.5
  • 61
    • 0028179851 scopus 로고
    • Membrane-associated forms of the beta A4 amyloid protein precursor of Alzheimer's disease in human platelet and brain: surface expression on the activated human platelet
    • Li Q.X., Berndt M.C., Bush A.I., Rumble B., Mackenzie I., Friedhuber A., Beyreuther K., and Masters C.L. Membrane-associated forms of the beta A4 amyloid protein precursor of Alzheimer's disease in human platelet and brain: surface expression on the activated human platelet. Blood 84 (1994) 133-142
    • (1994) Blood , vol.84 , pp. 133-142
    • Li, Q.X.1    Berndt, M.C.2    Bush, A.I.3    Rumble, B.4    Mackenzie, I.5    Friedhuber, A.6    Beyreuther, K.7    Masters, C.L.8
  • 63
    • 0031576348 scopus 로고    scopus 로고
    • Stimulated release of the beta-amyloid protein of Alzheimer's disease by normal human platelets
    • Smith C.C. Stimulated release of the beta-amyloid protein of Alzheimer's disease by normal human platelets. Neurosci. Lett. 235 (1997) 157-159
    • (1997) Neurosci. Lett. , vol.235 , pp. 157-159
    • Smith, C.C.1
  • 64
    • 15244340676 scopus 로고    scopus 로고
    • Human apolipoprotein E4 alters the amyloid-beta 40:42 ratio and promotes the formation of cerebral amyloid angiopathy in an amyloid precursor protein transgenic model
    • Fryer J.D., Simmons K., Parsadanian M., Bales K.R., Paul S.M., Sullivan P.M., and Holtzman D.M. Human apolipoprotein E4 alters the amyloid-beta 40:42 ratio and promotes the formation of cerebral amyloid angiopathy in an amyloid precursor protein transgenic model. J. Neurosci. 25 (2005) 2803-2810
    • (2005) J. Neurosci. , vol.25 , pp. 2803-2810
    • Fryer, J.D.1    Simmons, K.2    Parsadanian, M.3    Bales, K.R.4    Paul, S.M.5    Sullivan, P.M.6    Holtzman, D.M.7
  • 65
    • 0024385242 scopus 로고
    • Amyloid and Alzheimer's disease-cause or effect?
    • discussion 477-478
    • Yankner B.A. Amyloid and Alzheimer's disease-cause or effect?. Neurobiol. Aging 10 (1989) 470-471 discussion 477-478
    • (1989) Neurobiol. Aging , vol.10 , pp. 470-471
    • Yankner, B.A.1
  • 66
    • 0029670094 scopus 로고    scopus 로고
    • beta-Amyloid-mediated vasoactivity and vascular endothelial damage
    • Thomas T., Thomas G., McLendon C., Sutton T., and Mullan M. beta-Amyloid-mediated vasoactivity and vascular endothelial damage. Nature 380 (1996) 168-171
    • (1996) Nature , vol.380 , pp. 168-171
    • Thomas, T.1    Thomas, G.2    McLendon, C.3    Sutton, T.4    Mullan, M.5
  • 67
    • 0031461944 scopus 로고    scopus 로고
    • Fragments of amyloid beta induce apoptosis in vascular endothelial cells
    • Hase M., Araki S., and Hayashi H. Fragments of amyloid beta induce apoptosis in vascular endothelial cells. Endothelium 5 (1997) 221-229
    • (1997) Endothelium , vol.5 , pp. 221-229
    • Hase, M.1    Araki, S.2    Hayashi, H.3
  • 69
    • 15644376284 scopus 로고    scopus 로고
    • Amyloid beta-peptide possesses a transforming growth factor-beta activity
    • Huang S.S., Huang F.W., Xu J., Chen S., Hsu C.Y., and Huang J.S. Amyloid beta-peptide possesses a transforming growth factor-beta activity. J. Biol. Chem. 273 (1998) 27640-27644
    • (1998) J. Biol. Chem. , vol.273 , pp. 27640-27644
    • Huang, S.S.1    Huang, F.W.2    Xu, J.3    Chen, S.4    Hsu, C.Y.5    Huang, J.S.6
  • 70
    • 0032534611 scopus 로고    scopus 로고
    • Endothelial cell dysfunction in response to intracellular overexpression of amyloid precursor protein
    • Jahroudi N., Kitney J., Greenberger J.S., and Bowser R. Endothelial cell dysfunction in response to intracellular overexpression of amyloid precursor protein. J. Neurosci. Res. 54 (1998) 828-839
    • (1998) J. Neurosci. Res. , vol.54 , pp. 828-839
    • Jahroudi, N.1    Kitney, J.2    Greenberger, J.S.3    Bowser, R.4
  • 71
    • 0032512867 scopus 로고    scopus 로고
    • Toxic effects of beta-amyloid(25-35) on immortalised rat brain endothelial cell: protection by carnosine, homocarnosine and beta-alanine
    • Preston J.E., Hipkiss A.R., Himsworth D.T., Romero I.A., and Abbott J.N. Toxic effects of beta-amyloid(25-35) on immortalised rat brain endothelial cell: protection by carnosine, homocarnosine and beta-alanine. Neurosci. Lett. 242 (1998) 105-108
    • (1998) Neurosci. Lett. , vol.242 , pp. 105-108
    • Preston, J.E.1    Hipkiss, A.R.2    Himsworth, D.T.3    Romero, I.A.4    Abbott, J.N.5
  • 72
    • 0033528254 scopus 로고    scopus 로고
    • Intravascular infusions of soluble beta-amyloid compromise the blood-brain barrier, activate CNS glial cells and induce peripheral hemorrhage
    • Su G.C., Arendash G.W., Kalaria R.N., Bjugstad K.B., and Mullan M. Intravascular infusions of soluble beta-amyloid compromise the blood-brain barrier, activate CNS glial cells and induce peripheral hemorrhage. Brain Res. 818 (1999) 105-117
    • (1999) Brain Res. , vol.818 , pp. 105-117
    • Su, G.C.1    Arendash, G.W.2    Kalaria, R.N.3    Bjugstad, K.B.4    Mullan, M.5
  • 73
    • 0034981701 scopus 로고    scopus 로고
    • Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation
    • Xu J., Chen S., Ku G., Ahmed S.H., Chen H., and Hsu C.Y. 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    Chen, H.5    Hsu, C.Y.6
  • 74
    • 0037112194 scopus 로고    scopus 로고
    • Amyloid-beta induces Smac release via AP-1/Bim activation in cerebral endothelial cells
    • Yin K.J., Lee J.M., Chen S.D., Xu J., and Hsu C.Y. Amyloid-beta induces Smac release via AP-1/Bim activation in cerebral endothelial cells. J. Neurosci. 22 (2002) 9764-9770
    • (2002) J. Neurosci. , vol.22 , pp. 9764-9770
    • Yin, K.J.1    Lee, J.M.2    Chen, S.D.3    Xu, J.4    Hsu, C.Y.5
  • 75
    • 33645633087 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulates bim expression via the Akt/FKHRL1 signaling pathway in amyloid-beta peptide-induced cerebrovascular endothelial cell death
    • Yin K.J., Hsu C.Y., Hu X.Y., Chen H., Chen S.W., Xu J., and Lee J.M. Protein phosphatase 2A regulates bim expression via the Akt/FKHRL1 signaling pathway in amyloid-beta peptide-induced cerebrovascular endothelial cell death. J. Neurosci. 26 (2006) 2290-2299
    • (2006) J. Neurosci. , vol.26 , pp. 2290-2299
    • Yin, K.J.1    Hsu, C.Y.2    Hu, X.Y.3    Chen, H.4    Chen, S.W.5    Xu, J.6    Lee, J.M.7
  • 76
    • 34250665401 scopus 로고    scopus 로고
    • Apoptosis signal-regulating kinase 1 in amyloid beta peptide-induced cerebral endothelial cell apoptosis
    • Hsu M.J., Hsu C.Y., Chen B.C., Chen M.C., Ou G., and Lin C.H. Apoptosis signal-regulating kinase 1 in amyloid beta peptide-induced cerebral endothelial cell apoptosis. J. Neurosci. 27 (2007) 5719-5729
    • (2007) J. Neurosci. , vol.27 , pp. 5719-5729
    • Hsu, M.J.1    Hsu, C.Y.2    Chen, B.C.3    Chen, M.C.4    Ou, G.5    Lin, C.H.6
  • 77
    • 0028982272 scopus 로고
    • Amyloid beta-protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells
    • Davis-Salinas J., and Van Nostrand W.E. Amyloid beta-protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells. J. Biol. Chem. 270 (1995) 20887-20890
    • (1995) J. Biol. Chem. , vol.270 , pp. 20887-20890
    • Davis-Salinas, J.1    Van Nostrand, W.E.2
  • 79
    • 0347122965 scopus 로고    scopus 로고
    • Amyloid-beta peptide induces oligodendrocyte death by activating the neutral sphingomyelinase-ceramide pathway
    • Lee J.T., Xu J., Lee J.M., Ku G., Han X., Yang D.I., Chen S., and Hsu C.Y. Amyloid-beta peptide induces oligodendrocyte death by activating the neutral sphingomyelinase-ceramide pathway. J Cell Biol 164 (2004) 123-131
    • (2004) J Cell Biol , vol.164 , pp. 123-131
    • Lee, J.T.1    Xu, J.2    Lee, J.M.3    Ku, G.4    Han, X.5    Yang, D.I.6    Chen, S.7    Hsu, C.Y.8
  • 80
    • 4444370898 scopus 로고    scopus 로고
    • Neutral sphingomyelinase activation in endothelial and glial cell death induced by amyloid beta-peptide
    • Yang D.I., Yeh C.H., Chen S., Xu J., and Hsu C.Y. Neutral sphingomyelinase activation in endothelial and glial cell death induced by amyloid beta-peptide. Neurobiol. Dis. 17 (2004) 99-107
    • (2004) Neurobiol. Dis. , vol.17 , pp. 99-107
    • Yang, D.I.1    Yeh, C.H.2    Chen, S.3    Xu, J.4    Hsu, C.Y.5
  • 81
    • 18744427237 scopus 로고
    • Selective transport across the blood-brain barrier
    • Banks W.A., Kastin A.J., and Michals E.A. Selective transport across the blood-brain barrier. Ann. Intern. Med. 105 (1986) 472
    • (1986) Ann. Intern. Med. , vol.105 , pp. 472
    • Banks, W.A.1    Kastin, A.J.2    Michals, E.A.3
  • 82
    • 0031004788 scopus 로고    scopus 로고
    • Amyloid beta-peptide induces cell monolayer albumin permeability, impairs glucose transport, and induces apoptosis in vascular endothelial cells
    • Blanc E.M., Toborek M., Mark R.J., Hennig B., and Mattson M.P. Amyloid beta-peptide induces cell monolayer albumin permeability, impairs glucose transport, and induces apoptosis in vascular endothelial cells. J. Neurochem. 68 (1997) 1870-1881
    • (1997) J. Neurochem. , vol.68 , pp. 1870-1881
    • Blanc, E.M.1    Toborek, M.2    Mark, R.J.3    Hennig, B.4    Mattson, M.P.5
  • 83
    • 0030848729 scopus 로고    scopus 로고
    • Increased susceptibility to ischemic brain damage in transgenic mice overexpressing the amyloid precursor protein
    • Zhang F., Eckman C., Younkin S., Hsiao K.K., and Iadecola C. Increased susceptibility to ischemic brain damage in transgenic mice overexpressing the amyloid precursor protein. J. Neurosci. 17 (1997) 7655-7661
    • (1997) J. Neurosci. , vol.17 , pp. 7655-7661
    • Zhang, F.1    Eckman, C.2    Younkin, S.3    Hsiao, K.K.4    Iadecola, C.5
  • 87
    • 22444441299 scopus 로고    scopus 로고
    • Mechanism of amyloid peptide induced CCR5 expression in monocytes and its inhibition by siRNA for Egr-1
    • Giri R.K., Rajagopal V., Shahi S., Zlokovic B.V., and Kalra V.K. Mechanism of amyloid peptide induced CCR5 expression in monocytes and its inhibition by siRNA for Egr-1. Am. J. Physiol. Cell Physiol. 289 (2005) C264-C276
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Giri, R.K.1    Rajagopal, V.2    Shahi, S.3    Zlokovic, B.V.4    Kalra, V.K.5
  • 89
    • 0141744905 scopus 로고    scopus 로고
    • Age-dependent impairment of somatosensory response in the amyloid precursor protein 23 transgenic mouse model of Alzheimer's disease
    • Mueggler T., Baumann D., Rausch M., Staufenbiel M., and Rudin M. Age-dependent impairment of somatosensory response in the amyloid precursor protein 23 transgenic mouse model of Alzheimer's disease. J. Neurosci. 23 (2003) 8231-8236
    • (2003) J. Neurosci. , vol.23 , pp. 8231-8236
    • Mueggler, T.1    Baumann, D.2    Rausch, M.3    Staufenbiel, M.4    Rudin, M.5
  • 90
    • 0037038820 scopus 로고    scopus 로고
    • Vascular disorder in Alzheimer's disease: role in pathogenesis of dementia and therapeutic targets
    • Zlokovic B.V. Vascular disorder in Alzheimer's disease: role in pathogenesis of dementia and therapeutic targets. Adv. Drug Deliv. Rev. 54 (2002) 1553-1559
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 1553-1559
    • Zlokovic, B.V.1
  • 91
    • 0036627214 scopus 로고    scopus 로고
    • Circulating amyloid-beta peptide crosses the blood-brain barrier in aged monkeys and contributes to Alzheimer's disease lesions
    • Mackic J.B., Bading J., Ghiso J., Walker L., Wisniewski T., Frangione B., and Zlokovic B.V. Circulating amyloid-beta peptide crosses the blood-brain barrier in aged monkeys and contributes to Alzheimer's disease lesions. Vasc. Pharmacol. 38 (2002) 303-313
    • (2002) Vasc. Pharmacol. , vol.38 , pp. 303-313
    • Mackic, J.B.1    Bading, J.2    Ghiso, J.3    Walker, L.4    Wisniewski, T.5    Frangione, B.6    Zlokovic, B.V.7
  • 92
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., and Reed J.C. Mitochondria and apoptosis. Science 281 (1998) 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 93
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G., Dallaporta B., and Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu. Rev. Physiol. 60 (1998) 619-642
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 94
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z., and Lipton S.A. S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324 (2009) 102-105
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 95
  • 96
    • 0033510014 scopus 로고    scopus 로고
    • Mitochondria in neurodegeneration: acute ischemia and chronic neurodegenerative diseases
    • Fiskum G., Murphy A.N., and Beal M.F. Mitochondria in neurodegeneration: acute ischemia and chronic neurodegenerative diseases. J. Cereb. Blood Flow. Metab. 19 (1999) 351-369
    • (1999) J. Cereb. Blood Flow. Metab. , vol.19 , pp. 351-369
    • Fiskum, G.1    Murphy, A.N.2    Beal, M.F.3
  • 97
    • 0032504710 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • Beal M.F. Mitochondrial dysfunction in neurodegenerative diseases. Biochim. Biophys. Acta 1366 (1998) 211-223
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 211-223
    • Beal, M.F.1
  • 98
    • 0032504622 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative disorders
    • Schapira A.H. Mitochondrial dysfunction in neurodegenerative disorders. Biochim. Biophys. Acta 1366 (1998) 225-233
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 225-233
    • Schapira, A.H.1
  • 99
    • 0033386202 scopus 로고    scopus 로고
    • Mitochondria in neurodegeneration: bioenergetic function in cell life and death
    • Murphy A.N., Fiskum G., and Beal M.F. Mitochondria in neurodegeneration: bioenergetic function in cell life and death. J. Cereb. Blood Flow. Metab. 19 (1999) 231-245
    • (1999) J. Cereb. Blood Flow. Metab. , vol.19 , pp. 231-245
    • Murphy, A.N.1    Fiskum, G.2    Beal, M.F.3
  • 100
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace D.C. Mitochondrial diseases in man and mouse. Science 283 (1999) 1482-1488
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 101
    • 0031080027 scopus 로고    scopus 로고
    • beta-amyloid-induced endothelial necrosis and inhibition of nitric oxide production
    • Sutton E.T., Hellermann G.R., and Thomas T. beta-amyloid-induced endothelial necrosis and inhibition of nitric oxide production. Exp. Cell Res. 230 (1997) 368-376
    • (1997) Exp. Cell Res. , vol.230 , pp. 368-376
    • Sutton, E.T.1    Hellermann, G.R.2    Thomas, T.3
  • 102
    • 0032032969 scopus 로고    scopus 로고
    • Characteristics of the in vitro vasoactivity of beta-amyloid peptides
    • Crawford F., Suo Z., Fang C., and Mullan M. Characteristics of the in vitro vasoactivity of beta-amyloid peptides. Exp. Neurol. 150 (1998) 159-168
    • (1998) Exp. Neurol. , vol.150 , pp. 159-168
    • Crawford, F.1    Suo, Z.2    Fang, C.3    Mullan, M.4
  • 103
    • 0029743756 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegeneration
    • Schapira A.H. Oxidative stress and mitochondrial dysfunction in neurodegeneration. Curr. Opin. Neurol. 9 (1996) 260-264
    • (1996) Curr. Opin. Neurol. , vol.9 , pp. 260-264
    • Schapira, A.H.1
  • 104
    • 0031962324 scopus 로고    scopus 로고
    • Bcl-2 protects isolated plasma and mitochondrial membranes against lipid peroxidation induced by hydrogen peroxide and amyloid beta-peptide
    • Bruce-Keller A.J., Begley J.G., Fu W., Butterfield D.A., Bredesen D.E., Hutchins J.B., Hensley K., and Mattson M.P. Bcl-2 protects isolated plasma and mitochondrial membranes against lipid peroxidation induced by hydrogen peroxide and amyloid beta-peptide. J. Neurochem. 70 (1998) 31-39
    • (1998) J. Neurochem. , vol.70 , pp. 31-39
    • Bruce-Keller, A.J.1    Begley, J.G.2    Fu, W.3    Butterfield, D.A.4    Bredesen, D.E.5    Hutchins, J.B.6    Hensley, K.7    Mattson, M.P.8
  • 105
    • 27544479978 scopus 로고    scopus 로고
    • Abeta25-35 alters Akt activity, resulting in Bad translocation and mitochondrial dysfunction in cerebrovascular endothelial cells
    • Yin K.J., Lee J.M., Chen H., Xu J., and Hsu C.Y. Abeta25-35 alters Akt activity, resulting in Bad translocation and mitochondrial dysfunction in cerebrovascular endothelial cells. J. Cereb. Blood Flow. Metab. 25 (2005) 1445-1455
    • (2005) J. Cereb. Blood Flow. Metab. , vol.25 , pp. 1445-1455
    • Yin, K.J.1    Lee, J.M.2    Chen, H.3    Xu, J.4    Hsu, C.Y.5
  • 107
    • 34848895758 scopus 로고    scopus 로고
    • Apoptosis induced by capsaicin in prostate PC-3 cells involves ceramide accumulation, neutral sphingomyelinase, and JNK activation
    • Sanchez A.M., Malagarie-Cazenave S., Olea N., Vara D., Chiloeches A., and Diaz-Laviada I. Apoptosis induced by capsaicin in prostate PC-3 cells involves ceramide accumulation, neutral sphingomyelinase, and JNK activation. Apoptosis 12 (2007) 2013-2024
    • (2007) Apoptosis , vol.12 , pp. 2013-2024
    • Sanchez, A.M.1    Malagarie-Cazenave, S.2    Olea, N.3    Vara, D.4    Chiloeches, A.5    Diaz-Laviada, I.6
  • 109
    • 0032568836 scopus 로고    scopus 로고
    • Involvement of de novo ceramide biosynthesis in tumor necrosis factor-alpha/cycloheximide-induced cerebral endothelial cell death
    • Xu J., Yeh C.H., Chen S., He L., Sensi S.L., Canzoniero L.M., Choi D.W., and Hsu C.Y. Involvement of de novo ceramide biosynthesis in tumor necrosis factor-alpha/cycloheximide-induced cerebral endothelial cell death. J. Biol. Chem. 273 (1998) 16521-16526
    • (1998) J. Biol. Chem. , vol.273 , pp. 16521-16526
    • Xu, J.1    Yeh, C.H.2    Chen, S.3    He, L.4    Sensi, S.L.5    Canzoniero, L.M.6    Choi, D.W.7    Hsu, C.Y.8
  • 110
    • 34447633192 scopus 로고    scopus 로고
    • Mitochondrial superoxide production and nuclear factor erythroid 2-related factor 2 activation in p75 neurotrophin receptor-induced motor neuron apoptosis
    • Pehar M., Vargas M.R., Robinson K.M., Cassina P., Diaz-Amarilla P.J., Hagen T.M., Radi R., Barbeito L., and Beckman J.S. Mitochondrial superoxide production and nuclear factor erythroid 2-related factor 2 activation in p75 neurotrophin receptor-induced motor neuron apoptosis. J. Neurosci. 27 (2007) 7777-7785
    • (2007) J. Neurosci. , vol.27 , pp. 7777-7785
    • Pehar, M.1    Vargas, M.R.2    Robinson, K.M.3    Cassina, P.4    Diaz-Amarilla, P.J.5    Hagen, T.M.6    Radi, R.7    Barbeito, L.8    Beckman, J.S.9
  • 111
    • 57649210164 scopus 로고    scopus 로고
    • Identification of Mg2+-dependent neutral sphingomyelinase 1 as a mediator of heat stress-induced ceramide generation and apoptosis
    • Yabu T., Imamura S., Yamashita M., and Okazaki T. Identification of Mg2+-dependent neutral sphingomyelinase 1 as a mediator of heat stress-induced ceramide generation and apoptosis. J. Biol. Chem. 283 (2008) 29971-29982
    • (2008) J. Biol. Chem. , vol.283 , pp. 29971-29982
    • Yabu, T.1    Imamura, S.2    Yamashita, M.3    Okazaki, T.4
  • 113
    • 0024596564 scopus 로고
    • Purified rat brain microvessels exhibit both acid and neutral sphingomyelinase activities
    • Carre J.B., Morand O., Homayoun P., Roux F., Bourre J.M., and Baumann N. Purified rat brain microvessels exhibit both acid and neutral sphingomyelinase activities. J. Neurochem. 52 (1989) 1294-1299
    • (1989) J. Neurochem. , vol.52 , pp. 1294-1299
    • Carre, J.B.1    Morand, O.2    Homayoun, P.3    Roux, F.4    Bourre, J.M.5    Baumann, N.6
  • 114
    • 0033859771 scopus 로고    scopus 로고
    • Receptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface
    • Jiang G., den Hertog J., and Hunter T. Receptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface. Mol. Cell. Biol. 20 (2000) 5917-5929
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5917-5929
    • Jiang, G.1    den Hertog, J.2    Hunter, T.3
  • 115
    • 24744454380 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulates apoptosis in intestinal epithelial cells
    • Ray R.M., Bhattacharya S., and Johnson L.R. Protein phosphatase 2A regulates apoptosis in intestinal epithelial cells. J. Biol. Chem. 280 (2005) 31091-31100
    • (2005) J. Biol. Chem. , vol.280 , pp. 31091-31100
    • Ray, R.M.1    Bhattacharya, S.2    Johnson, L.R.3
  • 116
    • 0037007096 scopus 로고    scopus 로고
    • Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits
    • Silverstein A.M., Barrow C.A., Davis A.J., and Mumby M.C. Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 4221-4226
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4221-4226
    • Silverstein, A.M.1    Barrow, C.A.2    Davis, A.J.3    Mumby, M.C.4
  • 117
    • 59649092928 scopus 로고    scopus 로고
    • Bad targets the permeability transition pore independent of Bax or Bak to switch between Ca2+-dependent cell survival and death
    • Roy S.S., Madesh M., Davies E., Antonsson B., Danial N., and Hajnoczky G. Bad targets the permeability transition pore independent of Bax or Bak to switch between Ca2+-dependent cell survival and death. Mol. Cell 33 (2009) 377-388
    • (2009) Mol. Cell , vol.33 , pp. 377-388
    • Roy, S.S.1    Madesh, M.2    Davies, E.3    Antonsson, B.4    Danial, N.5    Hajnoczky, G.6
  • 118
    • 36148969680 scopus 로고    scopus 로고
    • A protein kinase Cepsilon-anti-apoptotic kinase signaling complex protects human vascular endothelial cells against apoptosis through induction of Bcl-2
    • Steinberg R., Harari O.A., Lidington E.A., Boyle J.J., Nohadani M., Samarel A.M., Ohba M., Haskard D.O., and Mason J.C. A protein kinase Cepsilon-anti-apoptotic kinase signaling complex protects human vascular endothelial cells against apoptosis through induction of Bcl-2. J. Biol. Chem. 282 (2007) 32288-32297
    • (2007) J. Biol. Chem. , vol.282 , pp. 32288-32297
    • Steinberg, R.1    Harari, O.A.2    Lidington, E.A.3    Boyle, J.J.4    Nohadani, M.5    Samarel, A.M.6    Ohba, M.7    Haskard, D.O.8    Mason, J.C.9
  • 119
    • 42249107850 scopus 로고    scopus 로고
    • PARP-1 inhibition prevents oxidative and nitrosative stress-induced endothelial cell death via transactivation of the VEGF receptor 2
    • Mathews M.T., and Berk B.C. PARP-1 inhibition prevents oxidative and nitrosative stress-induced endothelial cell death via transactivation of the VEGF receptor 2. Arterioscler. Thromb. Vasc. Biol. 28 (2008) 711-717
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 711-717
    • Mathews, M.T.1    Berk, B.C.2
  • 121
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., and Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 (1995) 785-789
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 122
    • 0035369623 scopus 로고    scopus 로고
    • Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway
    • Brunet A., Datta S.R., and Greenberg M.E. Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway. Curr. Opin. Neurobiol. 11 (2001) 297-305
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 297-305
    • Brunet, A.1    Datta, S.R.2    Greenberg, M.E.3
  • 123
    • 33847014888 scopus 로고    scopus 로고
    • Phosphoinositide-3-kinase/akt survival signal pathways are implicated in neuronal survival after stroke
    • Zhao H., Sapolsky R.M., and Steinberg G.K. Phosphoinositide-3-kinase/akt survival signal pathways are implicated in neuronal survival after stroke. Mol. Neurobiol. 34 (2006) 249-270
    • (2006) Mol. Neurobiol. , vol.34 , pp. 249-270
    • Zhao, H.1    Sapolsky, R.M.2    Steinberg, G.K.3
  • 125
    • 43549112759 scopus 로고    scopus 로고
    • Bcl-2-family proteins and hematologic malignancies: history and future prospects
    • Reed J.C. Bcl-2-family proteins and hematologic malignancies: history and future prospects. Blood 111 (2008) 3322-3330
    • (2008) Blood , vol.111 , pp. 3322-3330
    • Reed, J.C.1
  • 127
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • Willis S.N., and Adams J.M. Life in the balance: how BH3-only proteins induce apoptosis. Curr. Opin. Cell Biol. 17 (2005) 617-625
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 128
    • 33645858245 scopus 로고    scopus 로고
    • Amyloid beta peptide increases DP5 expression via activation of neutral sphingomyelinase and JNK in oligodendrocytes
    • Chen S., Lee J.M., Zeng C., Chen H., Hsu C.Y., and Xu J. Amyloid beta peptide increases DP5 expression via activation of neutral sphingomyelinase and JNK in oligodendrocytes. J. Neurochem. 97 (2006) 631-640
    • (2006) J. Neurochem. , vol.97 , pp. 631-640
    • Chen, S.1    Lee, J.M.2    Zeng, C.3    Chen, H.4    Hsu, C.Y.5    Xu, J.6
  • 129
    • 33846603289 scopus 로고    scopus 로고
    • Pathophysiological roles of ASK1-MAP kinase signaling pathways
    • Nagai H., Noguchi T., Takeda K., and Ichijo H. Pathophysiological roles of ASK1-MAP kinase signaling pathways. J. Biochem. Mol. Biol. 40 (2007) 1-6
    • (2007) J. Biochem. Mol. Biol. , vol.40 , pp. 1-6
    • Nagai, H.1    Noguchi, T.2    Takeda, K.3    Ichijo, H.4
  • 131
    • 66949169952 scopus 로고    scopus 로고
    • Amyloid beta interaction with receptor for advanced glycation end products up-regulates brain endothelial CCR5 expression and promotes T cells crossing the blood-brain barrier
    • Li M., Shang D.S., Zhao W.D., Tian L., Li B., Fang W.G., Zhu L., Man S.M., and Chen Y.H. Amyloid beta interaction with receptor for advanced glycation end products up-regulates brain endothelial CCR5 expression and promotes T cells crossing the blood-brain barrier. J. Immunol. 182 (2009) 5778-5788
    • (2009) J. Immunol. , vol.182 , pp. 5778-5788
    • Li, M.1    Shang, D.S.2    Zhao, W.D.3    Tian, L.4    Li, B.5    Fang, W.G.6    Zhu, L.7    Man, S.M.8    Chen, Y.H.9
  • 132
    • 0034006944 scopus 로고    scopus 로고
    • beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology
    • Wang H.Y., Lee D.H., D'Andrea M.R., Peterson P.A., Shank R.P., and Reitz A.B. beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J. Biol. Chem. 275 (2000) 5626-5632
    • (2000) J. Biol. Chem. , vol.275 , pp. 5626-5632
    • Wang, H.Y.1    Lee, D.H.2    D'Andrea, M.R.3    Peterson, P.A.4    Shank, R.P.5    Reitz, A.B.6
  • 134
    • 0037040889 scopus 로고    scopus 로고
    • Amyloid beta binds trimers as well as monomers of the 75-kDa neurotrophin receptor and activates receptor signaling
    • Yaar M., Zhai S., Fine R.E., Eisenhauer P.B., Arble B.L., Stewart K.B., and Gilchrest B.A. Amyloid beta binds trimers as well as monomers of the 75-kDa neurotrophin receptor and activates receptor signaling. J. Biol. Chem. 277 (2002) 7720-7725
    • (2002) J. Biol. Chem. , vol.277 , pp. 7720-7725
    • Yaar, M.1    Zhai, S.2    Fine, R.E.3    Eisenhauer, P.B.4    Arble, B.L.5    Stewart, K.B.6    Gilchrest, B.A.7
  • 135
    • 0031784830 scopus 로고    scopus 로고
    • Non-Alzheimer degenerative dementias
    • Pasquier F., and Delacourte A. Non-Alzheimer degenerative dementias. Curr. Opin. Neurol. 11 (1998) 417-427
    • (1998) Curr. Opin. Neurol. , vol.11 , pp. 417-427
    • Pasquier, F.1    Delacourte, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.