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Volumn 25, Issue 1, 2004, Pages 93-103

Insulin inhibits amyloid β-induced cell death in cultured human brain pericytes

Author keywords

Alzheimer's disease; Amyloid ; Fibril formation; Human brain pericytes; Insulin

Indexed keywords

AMYLOID BETA PROTEIN; INSULIN; PROTEIN INHIBITOR;

EID: 0346220380     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-4580(03)00039-3     Document Type: Article
Times cited : (64)

References (39)
  • 1
    • 0035980149 scopus 로고    scopus 로고
    • Insulin rescues retinal neurons from apoptosis by a phosphatidylinositol 3-kinase/Akt-mediated mechanism that reduces the activation of caspase-3
    • Barber A.J., Nakamura M., Wolpert E.B., Reiter C.E., Seigel G.M., Antonetti D.A.et al. Insulin rescues retinal neurons from apoptosis by a phosphatidylinositol 3-kinase/Akt-mediated mechanism that reduces the activation of caspase-3. J. Biol. Chem. 276(35):2001;32814-32821.
    • (2001) J. Biol. Chem. , vol.276 , Issue.35 , pp. 32814-32821
    • Barber, A.J.1    Nakamura, M.2    Wolpert, E.B.3    Reiter, C.E.4    Seigel, G.M.5    Antonetti, D.A.6
  • 2
    • 0033605607 scopus 로고    scopus 로고
    • Insulin-degrading enzyme in the Alzheimer's disease brain: Prominent localization in neurons and senile plaques
    • Bernstein H.G., Ansorge S., Riederer P., Reiser M., Frolich L., Bogerts B. Insulin-degrading enzyme in the Alzheimer's disease brain: prominent localization in neurons and senile plaques. Neurosci. Lett. 263(2/3):1999;161- 164.
    • (1999) Neurosci. Lett. , vol.263 , Issue.2-3 , pp. 161-164
    • Bernstein, H.G.1    Ansorge, S.2    Riederer, P.3    Reiser, M.4    Frolich, L.5    Bogerts, B.6
  • 4
    • 0026745610 scopus 로고
    • Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production
    • Citron M., Oltersdorf T., Haass C., McConlogue L., Hung A.Y., Seubert P.et al. Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production. Nature. 360(6405):1992;672-674.
    • (1992) Nature , vol.360 , Issue.6405 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3    McConlogue, L.4    Hung, A.Y.5    Seubert, P.6
  • 5
    • 0031907459 scopus 로고    scopus 로고
    • Cerebrospinal fluid and plasma insulin levels in Alzheimer's disease: Relationship to severity of dementia and apolipoprotein e genotype
    • Craft S., Peskind E., Schwartz M.W., Schellenberg G.D., Raskind M., Porte D. Jr.et al. Cerebrospinal fluid and plasma insulin levels in Alzheimer's disease: relationship to severity of dementia and apolipoprotein E genotype. Neurology. 50(1):1998;164-168.
    • (1998) Neurology , vol.50 , Issue.1 , pp. 164-168
    • Craft, S.1    Peskind, E.2    Schwartz, M.W.3    Schellenberg, G.D.4    Raskind, M.5    Porte Jr., D.6
  • 6
    • 0028982272 scopus 로고
    • Amyloid beta-protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells
    • Davis-Salinas J., Van Nostrand W.E. Amyloid beta-protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells. J. Biol. Chem. 270(36):1995;20887-20890.
    • (1995) J. Biol. Chem. , vol.270 , Issue.36 , pp. 20887-20890
    • Davis-Salinas, J.1    Van Nostrand, W.E.2
  • 7
    • 0029920991 scopus 로고    scopus 로고
    • Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein
    • Davis J., Van Nostrand W.E. Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein. Proc. Natl. Acad. Sci. U.S.A. 93(7):1996;2996-3000.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , Issue.7 , pp. 2996-3000
    • Davis, J.1    Van Nostrand, W.E.2
  • 8
    • 0030902595 scopus 로고    scopus 로고
    • Insulin-like growth factor I protects and rescues hippocampal neurons against beta-amyloid and human amylin-induced toxicity
    • Dore S., Kar S., Quirion R. Insulin-like growth factor I protects and rescues hippocampal neurons against beta-amyloid and human amylin-induced toxicity. Proc. Natl. Acad. Sci. U.S.A. 94(9):1997;4772-4777.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , Issue.9 , pp. 4772-4777
    • Dore, S.1    Kar, S.2    Quirion, R.3
  • 10
    • 0033378682 scopus 로고    scopus 로고
    • A disturbance in the neuronal insulin receptor signal transduction in sporadic Alzheimer's disease
    • Frolich L., Blum-Degen D., Riederer P., Hoyer S. A disturbance in the neuronal insulin receptor signal transduction in sporadic Alzheimer's disease. Ann. N.Y. Acad. Sci. 893:1999;290-293.
    • (1999) Ann. N.Y. Acad. Sci. , vol.893 , pp. 290-293
    • Frolich, L.1    Blum-Degen, D.2    Riederer, P.3    Hoyer, S.4
  • 11
    • 0036591657 scopus 로고    scopus 로고
    • Does insulin dysfunction play a role in Alzheimer's disease?
    • Gasparini L., Netzer W.J., Greengard P., Xu H. Does insulin dysfunction play a role in Alzheimer's disease? Trends Pharmacol. Sci. 23(6):2002;288-293.
    • (2002) Trends Pharmacol. Sci. , vol.23 , Issue.6 , pp. 288-293
    • Gasparini, L.1    Netzer, W.J.2    Greengard, P.3    Xu, H.4
  • 12
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G.G., Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120(3):1984;885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 13
    • 0030612192 scopus 로고    scopus 로고
    • Models of Alzheimer's disease: Cellular and molecular aspects
    • Hoyer S. Models of Alzheimer's disease: cellular and molecular aspects. J. Neural Transm. Suppl. 49:1997;11-21.
    • (1997) J. Neural Transm. Suppl. , vol.49 , pp. 11-21
    • Hoyer, S.1
  • 14
    • 0032496368 scopus 로고    scopus 로고
    • Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme
    • Kurochkin I.V. Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme. FEBS Lett. 427(2):1998;153-156.
    • (1998) FEBS Lett. , vol.427 , Issue.2 , pp. 153-156
    • Kurochkin, I.V.1
  • 15
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2(3):1993;404-410.
    • (1993) Protein Sci. , vol.2 , Issue.3 , pp. 404-410
    • Levine, H.1
  • 16
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H. III Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309:1999;274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • Levine III, H.1
  • 17
    • 0028271766 scopus 로고
    • High glucose downregulates glucose transport activity in retinal capillary pericytes but not endothelial cells
    • Mandarino L.J., Finlayson J., Hassell J.R. High glucose downregulates glucose transport activity in retinal capillary pericytes but not endothelial cells. Invest. Ophthalmol. Vis. Sci. 35(3):1994;964-972.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , Issue.3 , pp. 964-972
    • Mandarino, L.J.1    Finlayson, J.2    Hassell, J.R.3
  • 18
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid beta-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark R.J., Pang Z., Geddes J.W., Uchida K., Mattson M.P. Amyloid beta-peptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J. Neurosci. 17(3):1997;1046-1054.
    • (1997) J. Neurosci. , vol.17 , Issue.3 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 19
    • 0026570528 scopus 로고
    • Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12(2):1992;376-389.
    • (1992) J. Neurosci. , vol.12 , Issue.2 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 20
    • 0034737720 scopus 로고    scopus 로고
    • Fibrillar amyloid beta-protein mediates the pathologic accumulation of its secreted precursor in human cerebrovascular smooth muscle cells
    • Melchor J.P., Van Nostrand W.E. Fibrillar amyloid beta-protein mediates the pathologic accumulation of its secreted precursor in human cerebrovascular smooth muscle cells. J. Biol. Chem. 275(13):2000;9782-9791.
    • (2000) J. Biol. Chem. , vol.275 , Issue.13 , pp. 9782-9791
    • Melchor, J.P.1    Van Nostrand, W.E.2
  • 21
    • 0025908356 scopus 로고
    • The consortium to establish a registry for Alzheimer's disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra S.S., Heyman A., McKeel D., Sumi S.M., Crain B.J., Brownlee L.M.et al. The consortium to establish a registry for Alzheimer's disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology. 41:1991;479-486.
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6
  • 22
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline
    • Naslund J., Haroutunian V., Mohs R., Davis K.L., Davies P., Greengard P.et al. Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. J. Am. Med. Assoc. 283(12):2000;1571-1577.
    • (2000) J. Am. Med. Assoc. , vol.283 , Issue.12 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6
  • 23
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton E.J., Tito P., Sunde M., Bouchard M., Dobson C.M., Robinson C.V. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 79(2):2000;1053-1065.
    • (2000) Biophys. J. , vol.79 , Issue.2 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 24
    • 0030894036 scopus 로고    scopus 로고
    • The inhibitory effects of beta-amyloid on glutamate and glucose uptakes by cultured astrocytes
    • Parpura-Gill A., Beitz D., Uemura E. The inhibitory effects of beta-amyloid on glutamate and glucose uptakes by cultured astrocytes. Brain Res. 754(1/2):1997;65-71.
    • (1997) Brain Res. , vol.754 , Issue.1-2 , pp. 65-71
    • Parpura-Gill, A.1    Beitz, D.2    Uemura, E.3
  • 25
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., Cotman C.W. Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13(4):1993;1676-1687.
    • (1993) J. Neurosci. , vol.13 , Issue.4 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 26
    • 0000398342 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation
    • Qiu W.Q., Walsh D.M., Ye Z., Vekrellis K., Zhang J., Podlisny M.B.et al. Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J. Biol. Chem. 273(49):1998;32730-32738.
    • (1998) J. Biol. Chem. , vol.273 , Issue.49 , pp. 32730-32738
    • Qiu, W.Q.1    Walsh, D.M.2    Ye, Z.3    Vekrellis, K.4    Zhang, J.5    Podlisny, M.B.6
  • 28
    • 0027427734 scopus 로고
    • Toxic effect of a beta-amyloid peptide (beta 22-35) on the hippocampal neuron and its prevention
    • Takadera T., Sakura N., Mohri T., Hashimoto T. Toxic effect of a beta-amyloid peptide (beta 22-35) on the hippocampal neuron and its prevention. Neurosci. Lett. 161(1):1993;41-44.
    • (1993) Neurosci. Lett. , vol.161 , Issue.1 , pp. 41-44
    • Takadera, T.1    Sakura, N.2    Mohri, T.3    Hashimoto, T.4
  • 30
    • 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., Ruffini L. Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. J. Neurochem. 70(1):1998;216-223.
    • (1998) J. Neurochem. , vol.70 , Issue.1 , pp. 216-223
    • Van Nostrand, W.E.1    Melchor, J.P.2    Ruffini, L.3
  • 31
    • 0034161516 scopus 로고    scopus 로고
    • Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme
    • Vekrellis K., Ye Z., Qiu W.Q., Walsh D., Hartley D., Chesneau V.et al. Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme. J. Neurosci. 20(5):2000;1657-1665.
    • (2000) J. Neurosci. , vol.20 , Issue.5 , pp. 1657-1665
    • Vekrellis, K.1    Ye, Z.2    Qiu, W.Q.3    Walsh, D.4    Hartley, D.5    Chesneau, V.6
  • 32
    • 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. 68(3):1997;1135-1141.
    • (1997) J. Neurochem. , vol.68 , Issue.3 , pp. 1135-1141
    • Verbeek, M.M.1    De Waal, R.M.2    Schipper, J.J.3    Van Nostrand, W.E.4
  • 33
    • 0031011209 scopus 로고    scopus 로고
    • Differences between the pathogenesis of senile plaques and congophilic angiopathy in Alzheimer disease
    • Verbeek M.M., Eikelenboom P., De Waal R.M. Differences between the pathogenesis of senile plaques and congophilic angiopathy in Alzheimer disease. J. Neuropathol. Exp. Neurol. 56(7):1997;751-761.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , Issue.7 , pp. 751-761
    • Verbeek, M.M.1    Eikelenboom, P.2    De Waal, R.M.3
  • 34
    • 0028179175 scopus 로고
    • Induction of alpha-smooth muscle actin expression in cultured human brain pericytes by transforming growth factor-beta 1
    • Verbeek M.M., Otte Holler I., Wesseling P., Ruiter D.J., De Waal R.M. Induction of alpha-smooth muscle actin expression in cultured human brain pericytes by transforming growth factor-beta 1. Am. J. Pathol. 144(2):1994;372-382.
    • (1994) Am. J. Pathol. , vol.144 , Issue.2 , pp. 372-382
    • Verbeek, M.M.1    Otte Holler, I.2    Wesseling, P.3    Ruiter, D.J.4    De Waal, R.M.5
  • 35
    • 0002755993 scopus 로고    scopus 로고
    • Degeneration of human cerebrovascular smooth muscle cells and pericytes caused by amyloid β protein
    • Verbeek MM, De Waal RMW, Vinters HV, editors. Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Verbeek MM, Van Nostrand WE, De Waal RMW. Degeneration of human cerebrovascular smooth muscle cells and pericytes caused by amyloid β protein. In: Verbeek MM, De Waal RMW, Vinters HV, editors. Cerebral amyloid angiopathy in Alzheimer's disease and related disorders. Dordrecht, The Netherlands: Kluwer Academic Publishers; 2000. p. 265-79.
    • (2000) Cerebral Amyloid Angiopathy in Alzheimer's Disease and Related Disorders , pp. 265-279
    • Verbeek, M.M.1    Van Nostrand, W.E.2    De Waal, R.M.W.3
  • 36
    • 0029016245 scopus 로고
    • T lymphocyte adhesion to human brain pericytes is mediated via very late antigen-4/vascular cell adhesion molecule-1 interactions
    • Verbeek M.M., Westphal J.R., Ruiter D.J., De Waal R.M. T lymphocyte adhesion to human brain pericytes is mediated via very late antigen-4/vascular cell adhesion molecule-1 interactions. J. Immunol. 154(11):1995;5876-5884.
    • (1995) J. Immunol. , vol.154 , Issue.11 , pp. 5876-5884
    • Verbeek, M.M.1    Westphal, J.R.2    Ruiter, D.J.3    De Waal, R.M.4
  • 37
    • 0026685656 scopus 로고
    • Ultrastructural studies of the cells forming amyloid in the cortical vessel wall in Alzheimer's disease
    • Wisniewski H.M., Wegiel J., Wang K.C., Lach B. Ultrastructural studies of the cells forming amyloid in the cortical vessel wall in Alzheimer's disease. Acta Neuropathol. 84:1992;117-127.
    • (1992) Acta Neuropathol. , vol.84 , pp. 117-127
    • Wisniewski, H.M.1    Wegiel, J.2    Wang, K.C.3    Lach, B.4
  • 38
  • 39
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science. 250(4978):1990;279-282.
    • (1990) Science , vol.250 , Issue.4978 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3


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