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Volumn 51, Issue 2, 2016, Pages 471-487

Iron regulates apolipoprotein e expression and secretion in neurons and astrocytes

Author keywords

Apolipoprotein E; iron; lipoprotein receptor related protein; low density lipoprotein receptor

Indexed keywords

APOLIPOPROTEIN E; IRON; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; AMYLOID BETA PROTEIN; COPPER; FERRITIN; LOW DENSITY LIPOPROTEIN RECEPTOR; LRP1 PROTEIN, MOUSE; MESSENGER RNA; REACTIVE OXYGEN METABOLITE; TUMOR SUPPRESSOR PROTEIN; ZINC;

EID: 84961792801     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-150797     Document Type: Article
Times cited : (39)

References (74)
  • 2
    • 0036970185 scopus 로고    scopus 로고
    • Brain iron metabolism and neurodegenerative disorders
    • Sipe JC, Lee P, Beutler E. (2002). Brain iron metabolism and neurodegenerative disorders. Dev Neurosci 24, 188-196.
    • (2002) Dev Neurosci , vol.24 , pp. 188-196
    • Sipe, J.C.1    Lee, P.2    Beutler, E.3
  • 3
    • 84903870684 scopus 로고    scopus 로고
    • Iron accumulation confers neurotoxicity to a vulnerable population of nigral neurons: Implications for Parkinson's disease
    • Ayton S, Lei P, Adlard PA, Volitakis I, Cherny RA, Bush AI, Finkelstein DI. (2014). Iron accumulation confers neurotoxicity to a vulnerable population of nigral neurons: Implications for Parkinson's disease. Mol Neurodegener 9, 27.
    • (2014) Mol Neurodegener , vol.9 , pp. 27
    • Ayton, S.1    Lei, P.2    Adlard, P.A.3    Volitakis, I.4    Cherny, R.A.5    Bush, A.I.6    Finkelstein, D.I.7
  • 4
    • 84855461629 scopus 로고    scopus 로고
    • MRI estimates of brain iron concentration in normal aging using quantitative susceptibility mapping
    • Bilgic B, Pfefferbaum A, Rohlfing T, Sullivan EV, Adalsteinsson E. (2012). MRI estimates of brain iron concentration in normal aging using quantitative susceptibility mapping. Neuroimage 59, 2625-2635.
    • (2012) Neuroimage , vol.59 , pp. 2625-2635
    • Bilgic, B.1    Pfefferbaum, A.2    Rohlfing, T.3    Sullivan, E.V.4    Adalsteinsson, E.5
  • 6
    • 84950311757 scopus 로고    scopus 로고
    • The relationship between iron dyshomeostasis and amyloidogenesis in Alzheimer's disease: Two sides of the same coin
    • Peters DG, Connor JR, Meadowcroft MD. (2015). The relationship between iron dyshomeostasis and amyloidogenesis in Alzheimer's disease: Two sides of the same coin. Neurobiol Dis 81, 49-65.
    • (2015) Neurobiol Dis , vol.81 , pp. 49-65
    • Peters, D.G.1    Connor, J.R.2    Meadowcroft, M.D.3
  • 8
    • 84872562074 scopus 로고    scopus 로고
    • The metal theory of Alzheimer's disease
    • Bush AI. (2013). The metal theory of Alzheimer's disease. J Alzheimers Dis 33(Suppl 1), S277-S281.
    • (2013) J Alzheimers Dis , vol.33 , pp. S277-S281
    • Bush, A.I.1
  • 9
    • 84875697145 scopus 로고    scopus 로고
    • Metal dyshomeostasis and oxidative stress in Alzheimer's disease
    • Greenough MA, Camakaris J, Bush AI. (2013). Metal dyshomeostasis and oxidative stress in Alzheimer's disease. Neurochem Int 62, 540-555.
    • (2013) Neurochem Int , vol.62 , pp. 540-555
    • Ma, G.1    Camakaris, J.2    Bush, A.I.3
  • 10
    • 77957730965 scopus 로고    scopus 로고
    • Genome-wide association studies in Alzheimer's disease
    • Bertram L, Tanzi RE. (2009). Genome-wide association studies in Alzheimer's disease. Hum Mol Genet 18, R137-R145.
    • (2009) Hum Mol Genet , vol.18 , pp. R137-R145
    • Bertram, L.1    Tanzi, R.E.2
  • 11
    • 2542441462 scopus 로고    scopus 로고
    • Apolipoprotein gene and its interaction with the environmentally driven risk factors: Molecular, genetic and epidemiological studies of Alzheimer's disease
    • Lahiri DK, Sambamurti K, Bennett DA. (2004). Apolipoprotein gene and its interaction with the environmentally driven risk factors: Molecular, genetic and epidemiological studies of Alzheimer's disease. Neurobiol Aging 25, 651-660.
    • (2004) Neurobiol Aging , vol.25 , pp. 651-660
    • Lahiri, D.K.1    Sambamurti, K.2    Bennett, D.A.3
  • 12
    • 67349270965 scopus 로고    scopus 로고
    • Apolipoprotein e and its receptors in Alzheimer's disease: Pathways, pathogenesis and therapy
    • Bu G. (2009). Apolipoprotein E and its receptors in Alzheimer's disease: Pathways, pathogenesis and therapy. Nat Rev Neurosci 10, 333-344.
    • (2009) Nat Rev Neurosci , vol.10 , pp. 333-344
    • Bu, G.1
  • 15
    • 0037710127 scopus 로고    scopus 로고
    • Cholesterol homeostasis and function in neurons of the central nervous system
    • Pfrieger FW. (2003). Cholesterol homeostasis and function in neurons of the central nervous system. Cell Mol Life Sci 60, 1158-1171.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1158-1171
    • Pfrieger, F.W.1
  • 16
    • 84893208400 scopus 로고    scopus 로고
    • Both targeted mass spectrometry and flow sorting analysis methods detected the decreased serum apolipoprotein e level in Alzheimer's disease patients
    • Han SH, Kim JS, Lee Y, Choi H, Kim JW, Na DL, Yang EG, Yu MH, Hwang D, Lee C, Mook-Jung I. (2014). Both targeted mass spectrometry and flow sorting analysis methods detected the decreased serum apolipoprotein E level in Alzheimer's disease patients. Mol Cell Proteomics 13, 407-419.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 407-419
    • Han, S.H.1    Kim, J.S.2    Lee, Y.3    Choi, H.4    Kim, J.W.5    Na, D.L.6    Yang, E.G.7    Yu, M.H.8    Hwang, D.9    Lee, C.10    Mook-Jung, I.11
  • 18
    • 77955921493 scopus 로고    scopus 로고
    • Brain lipid metabolism, apolipoprotein e and the pathophysiology of Alzheimer's disease
    • Bales KR. (2010). Brain lipid metabolism, apolipoprotein E and the pathophysiology of Alzheimer's disease. Neuropharmacology 59, 295-302.
    • (2010) Neuropharmacology , vol.59 , pp. 295-302
    • Bales, K.R.1
  • 19
    • 0025971426 scopus 로고
    • Apolipoprotein e immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease
    • Namba Y, Tomonaga M, Kawasaki H, Otomo E, Ikeda K. (1991). Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res 541, 163-166.
    • (1991) Brain Res , vol.541 , pp. 163-166
    • Namba, Y.1    Tomonaga, M.2    Kawasaki, H.3    Otomo, E.4    Ikeda, K.5
  • 21
    • 84863504256 scopus 로고    scopus 로고
    • Apolipoprotein e and apolipoprotein e receptors: Normal biology and roles in Alzheimer disease
    • Holtzman DM, Herz J, Bu G. (2012). Apolipoprotein E and apolipoprotein E receptors: Normal biology and roles in Alzheimer disease. Cold Spring Harb Perspect Med 2, a006312.
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. a006312
    • Holtzman, D.M.1    Herz, J.2    Bu, G.3
  • 23
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz J, Strickland DK. (2001). LRP: A multifunctional scavenger and signaling receptor. J Clin Invest 108, 779-784.
    • (2001) J Clin Invest , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 24
    • 0025369190 scopus 로고
    • Proteolytic processing of the 600kd low density lipoprotein receptor-related protein LRP) occurs in a trans-Golgi compartment
    • Herz J, Kowal RC, Goldstein JL, Brown MS. (1990). Proteolytic processing of the 600kd low density lipoprotein receptor-related protein. (LRP). occurs in a trans-Golgi compartment. EMBO J 9, 1769-1776.
    • (1990) EMBO J , vol.9 , pp. 1769-1776
    • Herz, J.1    Kowal, R.C.2    Goldstein, J.L.3    Brown, M.S.4
  • 27
    • 84855767006 scopus 로고    scopus 로고
    • Association of ApoE and LRP mRNA levels with dementia and AD neuropathology
    • Akram A, Schmeidler J, Katsel P, Hof PR, Haroutunian V. (2012). Association of ApoE and LRP mRNA levels with dementia and AD neuropathology. Neurobiol Aging 33, 628 e621-628 e614.
    • (2012) Neurobiol Aging , vol.33 , pp. 628e621-628e614
    • Akram, A.1    Schmeidler, J.2    Katsel, P.3    Hof, P.R.4    Haroutunian, V.5
  • 30
    • 39149122831 scopus 로고    scopus 로고
    • Apoptosis of cultured astrocytes induced by the copper and neocuproine complex through oxidative stress andJNKactivation
    • Chen SH, Lin JK, Liu SH, Liang YC, Lin-Shiau SY. (2008). Apoptosis of cultured astrocytes induced by the copper and neocuproine complex through oxidative stress andJNKactivation. Toxicol Sci 102, 138-149.
    • (2008) Toxicol Sci , vol.102 , pp. 138-149
    • Chen, S.H.1    Lin, J.K.2    Liu, S.H.3    Liang, Y.C.4    Lin-Shiau, S.Y.5
  • 31
    • 0035873398 scopus 로고    scopus 로고
    • Pyruvate released by astrocytes protects neurons from copper-catalyzed cysteine neurotoxicity
    • Wang XF, Cynader MS. (2001). Pyruvate released by astrocytes protects neurons from copper-catalyzed cysteine neurotoxicity. J Neurosci 21, 3322-3331.
    • (2001) J Neurosci , vol.21 , pp. 3322-3331
    • Wang, X.F.1    Cynader, M.S.2
  • 32
    • 0035093878 scopus 로고    scopus 로고
    • Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary neuronal cultures: Possible risk factors in the Alzheimer's-type neurodegenerative pathways
    • White AR, Huang X, Jobling MF, Barrow CJ, Beyreuther K, Masters CL, Bush AI, Cappai R. (2001). Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary neuronal cultures: Possible risk factors in the Alzheimer's-type neurodegenerative pathways. J Neurochem 76, 1509-1520.
    • (2001) J Neurochem , vol.76 , pp. 1509-1520
    • White, A.R.1    Huang, X.2    Jobling, M.F.3    Barrow, C.J.4    Beyreuther, K.5    Masters, C.L.6    Bush, A.I.7    Cappai, R.8
  • 33
    • 33645809950 scopus 로고    scopus 로고
    • Zinc deficiency increases the susceptibility of human neuroblastoma cells to lead-induced activator protein-1 activation
    • Aimo L, Oteiza PI. (2006). Zinc deficiency increases the susceptibility of human neuroblastoma cells to lead-induced activator protein-1 activation. Toxicol Sci 91, 184-191.
    • (2006) Toxicol Sci , vol.91 , pp. 184-191
    • Aimo, L.1    Oteiza, P.I.2
  • 35
    • 84946873089 scopus 로고    scopus 로고
    • Iron misregulation and neurodegenerative disease in mouse models that lack iron regulatory proteins
    • Ghosh MC, Zhang L, Rouault TA. (2015). Iron misregulation and neurodegenerative disease in mouse models that lack iron regulatory proteins. Neurobiol Dis 81, 66-75.
    • (2015) Neurobiol Dis , vol.81 , pp. 66-75
    • Ghosh, M.C.1    Zhang, L.2    Rouault, T.A.3
  • 37
  • 38
    • 0029765553 scopus 로고    scopus 로고
    • Apolipoprotein e allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and beta-Amyloid peptides
    • Miyata M, Smith JD. (1996). Apolipoprotein E allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and beta-Amyloid peptides. Nat Genet 14, 55-61.
    • (1996) Nat Genet , vol.14 , pp. 55-61
    • Miyata, M.1    Smith, J.D.2
  • 39
    • 84899908763 scopus 로고    scopus 로고
    • Apolipoprotein E, amyloid-beta, and neuroinflammation in Alzheimer's disease
    • Dorey E, Chang N, Liu QY, Yang Z, Zhang W. (2014). Apolipoprotein E, amyloid-beta, and neuroinflammation in Alzheimer's disease. Neurosci Bull 30, 317-330.
    • (2014) Neurosci Bull , vol.30 , pp. 317-330
    • Dorey, E.1    Chang, N.2    Liu, Q.Y.3    Yang, Z.4    Zhang, W.5
  • 40
  • 41
    • 84937538891 scopus 로고    scopus 로고
    • Quantitative susceptibility mapping by inversion of a perturbation field model: Correlation with brain iron in normal aging
    • Poynton C, Jenkinson M, Adalsteinsson E, Sullivan E, Pfefferbaum A, Wells W. (2015). Quantitative susceptibility mapping by inversion of a perturbation field model: Correlation with brain iron in normal aging. IEEE Trans Med Imaging 34, 339-353.
    • (2015) IEEE Trans Med Imaging , vol.34 , pp. 339-353
    • Poynton, C.1    Jenkinson, M.2    Adalsteinsson, E.3    Sullivan, E.4    Pfefferbaum, A.5    Wells, W.6
  • 42
    • 84890862804 scopus 로고    scopus 로고
    • Iron levels in the human brain: A post-mortem study of anatomical region differences and age-related changes
    • Ramos P, Santos A, Pinto NR, Mendes R, Magalhaes T, Almeida A. (2014). Iron levels in the human brain: A post-mortem study of anatomical region differences and age-related changes. J Trace Elem Med Biol 28, 13-17.
    • (2014) J Trace Elem Med Biol , vol.28 , pp. 13-17
    • Ramos, P.1    Santos, A.2    Pinto, N.R.3    Mendes, R.4    Magalhaes, T.5    Almeida, A.6
  • 43
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush AI. (2003). The metallobiology of Alzheimer's disease. Trends Neurosci 26, 207-214.
    • (2003) Trends Neurosci , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 44
    • 0032401837 scopus 로고    scopus 로고
    • Iron quantification in cerebrospinal fluid
    • LeVine SM, Wulser MJ, Lynch SG. (1998). Iron quantification in cerebrospinal fluid. Anal Biochem 265, 74-78.
    • (1998) Anal Biochem , vol.265 , pp. 74-78
    • LeVine, S.M.1    Wulser, M.J.2    Lynch, S.G.3
  • 46
    • 69049113059 scopus 로고    scopus 로고
    • Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: Binding affinities, redox properties, and relevance to iron-induced oxidative stress in Alzheimer's disease
    • Jiang D, Li X, Williams R, Patel S, Men L, Wang Y, Zhou F. (2009). Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: Binding affinities, redox properties, and relevance to iron-induced oxidative stress in Alzheimer's disease. Biochemistry 48, 7939-7947.
    • (2009) Biochemistry , vol.48 , pp. 7939-7947
    • Jiang, D.1    Li, X.2    Williams, R.3    Patel, S.4    Men, L.5    Wang, Y.6    Zhou, F.7
  • 47
    • 84930225631 scopus 로고    scopus 로고
    • Ferritin levels in the cerebrospinal fluid predict Alzheimer's disease outcomes and are regulated by APOE
    • Ayton S, Faux NG, Bush AI. (2015). Ferritin levels in the cerebrospinal fluid predict Alzheimer's disease outcomes and are regulated by APOE. Nat Commun 6, 6760.
    • (2015) Nat Commun , vol.6 , pp. 6760
    • Ayton, S.1    Faux, N.G.2    Bush, A.I.3
  • 48
    • 84903715152 scopus 로고    scopus 로고
    • Apolipoprotein e and lipid homeostasis in the etiology and treatment of sporadic Alzheimer's disease
    • Poirier J, Miron J, Picard C, Gormley P, Theroux L, Breitner J, Dea D. (2014). Apolipoprotein E and lipid homeostasis in the etiology and treatment of sporadic Alzheimer's disease. Neurobiol Aging 35(Suppl 2), S3-S10.
    • (2014) Neurobiol Aging , vol.35 , pp. S3-S10
    • Poirier, J.1    Miron, J.2    Picard, C.3    Gormley, P.4    Theroux, L.5    Breitner, J.6    Dea, D.7
  • 53
    • 34748897213 scopus 로고    scopus 로고
    • Amyloid precursor protein regulates brain apolipoprotein e and cholesterol metabolism through lipoprotein receptor LRP1.
    • Liu Q, Zerbinatti CV, Zhang J, Hoe HS, Wang B, Cole SL, Herz J, Muglia L, Bu G. (2007). Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1. Neuron 56, 66-78.
    • (2007) Neuron , vol.56 , pp. 66-78
    • Liu, Q.1    Zerbinatti, C.V.2    Zhang, J.3    Hoe, H.S.4    Wang, B.5    Cole, S.L.6    Herz, J.7    Muglia, L.8    Bu, G.9
  • 54
    • 0031911126 scopus 로고    scopus 로고
    • Increased apolipoprotein e mRNA in the hippocampus in Alzheimer disease and in rats after entorhinal cortex lesioning
    • Zarow C, Victoroff J. (1998). Increased apolipoprotein E mRNA in the hippocampus in Alzheimer disease and in rats after entorhinal cortex lesioning. Exp Neurol 149, 79-86.
    • (1998) Exp Neurol , vol.149 , pp. 79-86
    • Zarow, C.1    Victoroff, J.2
  • 55
    • 84909578703 scopus 로고    scopus 로고
    • Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer's diseases
    • PtA
    • Huang Y, Mahley RW. (2014). Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer's diseases. Neurobiol Dis 72 Pt A 3-12.
    • (2014) Neurobiol Dis , vol.72 , pp. 3-12
    • Huang, Y.1    Mahley, R.W.2
  • 56
    • 0035902514 scopus 로고    scopus 로고
    • Apolipoprotein e fragments present in Alzheimer's disease brains induce neurofibrillary tanglelike intracellular inclusions in neurons
    • Huang Y, Liu XQ, Wyss-Coray T, Brecht WJ, Sanan DA, Mahley RW. (2001). Apolipoprotein E fragments present in Alzheimer's disease brains induce neurofibrillary tanglelike intracellular inclusions in neurons. Proc Natl Acad Sci U S A 98, 8838-8843.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8838-8843
    • Huang, Y.1    Liu, X.Q.2    Wyss-Coray, T.3    Brecht, W.J.4    Sanan, D.A.5    Mahley, R.W.6
  • 58
    • 0027374047 scopus 로고
    • Apolipoprotein e in sporadic Alzheimer's disease: Allelic variation and receptor interactions
    • Rebeck GW, Reiter JS, Strickland DK, Hyman BT. (1993). Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions. Neuron 11, 575-580.
    • (1993) Neuron , vol.11 , pp. 575-580
    • Rebeck, G.W.1    Reiter, J.S.2    Strickland, D.K.3    Hyman, B.T.4
  • 59
    • 33744991531 scopus 로고    scopus 로고
    • Implication of apoE isoforms in cholesterol metabolism by primary rat hippocampal neurons and astrocytes
    • Rapp A, Gmeiner B, Huttinger M. (2006). Implication of apoE isoforms in cholesterol metabolism by primary rat hippocampal neurons and astrocytes. Biochimie 88, 473-483.
    • (2006) Biochimie , vol.88 , pp. 473-483
    • Rapp, A.1    Gmeiner, B.2    Huttinger, M.3
  • 61
    • 84866464632 scopus 로고    scopus 로고
    • LRP-1 and LRP-2 receptors function in the membrane neuron Trafficking mechanisms and proteolytic processing in Alzheimer's disease
    • Spuch C, Ortolano S, Navarro C. (2012). LRP-1 and LRP-2 receptors function in the membrane neuron. Trafficking mechanisms and proteolytic processing in Alzheimer's disease. Front Physiol 3, 269.
    • (2012) Front Physiol , vol.3 , pp. 269
    • Spuch, C.1    Ortolano, S.2    Navarro, C.3
  • 62
    • 33846021307 scopus 로고    scopus 로고
    • Apolipoprotein e and low density lipoprotein receptor-related protein facilitate intraneuronal Abeta42 accumulation in amyloid model mice
    • Zerbinatti CV, Wahrle SE, Kim H, Cam JA, Bales K, Paul SM, Holtzman DM, Bu G. (2006). Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Abeta42 accumulation in amyloid model mice. J Biol Chem 281, 36180-36186.
    • (2006) J Biol Chem , vol.281 , pp. 36180-36186
    • Zerbinatti, C.V.1    Wahrle, S.E.2    Kim, H.3    Cam, J.A.4    Bales, K.5    Paul, S.M.6    Holtzman, D.M.7    Bu, G.8
  • 63
    • 71449125786 scopus 로고    scopus 로고
    • Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular A beta clearance
    • Kim J, Castellano JM, Jiang H, Basak JM, Parsadanian M, Pham V, Mason SM, Paul SM, Holtzman DM. (2009). Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular A beta clearance. Neuron 64, 632-644.
    • (2009) Neuron , vol.64 , pp. 632-644
    • Kim, J.1    Castellano, J.M.2    Jiang, H.3    Basak, J.M.4    Parsadanian, M.5    Pham, V.6    Mason, S.M.7    Paul, S.M.8    Holtzman, D.M.9
  • 64
    • 84859980871 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Abeta uptake and degradation by astrocytes
    • Basak JM, Verghese PB, Yoon H, Kim J, Holtzman DM. (2012). Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Abeta uptake and degradation by astrocytes. J Biol Chem 287, 13959-13971.
    • (2012) J Biol Chem , vol.287 , pp. 13959-13971
    • Basak, J.M.1    Verghese, P.B.2    Yoon, H.3    Kim, J.4    Holtzman, D.M.5
  • 65
    • 0034595799 scopus 로고    scopus 로고
    • The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein
    • Li Y, Marzolo MP, Van Kerkhof P, Strous GJ, Bu G. (2000). The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein. J Biol Chem 275, 17187-17194.
    • (2000) J Biol Chem , vol.275 , pp. 17187-17194
    • Li, Y.1    Marzolo, M.P.2    Van Kerkhof, P.3    Strous, G.J.4    Bu, G.5
  • 68
    • 84910071896 scopus 로고    scopus 로고
    • Iron increases APP translation and amyloid-beta production in the retina
    • Guo LY, Alekseev O, Li Y, Song Y, Dunaief JL. (2014). Iron increases APP translation and amyloid-beta production in the retina. Exp Eye Res 129, 31-37.
    • (2014) Exp Eye Res , vol.129 , pp. 31-37
    • Guo, L.Y.1    Alekseev, O.2    Li, Y.3    Song, Y.4    Dunaief, J.L.5
  • 69
    • 84880355746 scopus 로고    scopus 로고
    • Altered APP carboxyl-terminal processing under ferrous iron treatment in PC12 cells
    • Kim CH, Yoo YM. (2013). Altered APP carboxyl-terminal processing under ferrous iron treatment in PC12 cells. Korean J Physiol Pharmacol 17, 189-195.
    • (2013) Korean J Physiol Pharmacol , vol.17 , pp. 189-195
    • Kawas, C.H.1    Yoo, Y.M.2
  • 70
    • 57449119060 scopus 로고    scopus 로고
    • Physiological and pathological aspects of Abeta in iron homeostasis via 5'UTR in the APP mRNA and the therapeutic use of iron-chelators
    • Suppl
    • Avramovich-Tirosh Y, Amit T, Bar-Am O, Weinreb O, Youdim MB. (2008). Physiological and pathological aspects of Abeta in iron homeostasis via 5'UTR in the APP mRNA and the therapeutic use of iron-chelators. BMC Neurosci 9. (Suppl). 2, S2.
    • (2008) BMC Neurosci , vol.9 , Issue.2 , pp. S2
    • Avramovich-Tirosh, Y.1    Amit, T.2    Bar-Am, O.3    Weinreb, O.4    Youdim, M.B.5
  • 71
    • 34248577510 scopus 로고    scopus 로고
    • Metal specificity of an iron-responsive element in Alzheimer's APP mRNA 5'untranslated region, tolerance of SH-SY5Y and H4 neural cells to desferrioxamine, clioquinol, VK-28, and a piperazine chelator
    • Bandyopadhyay S, Huang X, Cho H, Greig NH, Youdim MB, Rogers JT. (2006). Metal specificity of an iron-responsive element in Alzheimer's APP mRNA 5'untranslated region, tolerance of SH-SY5Y and H4 neural cells to desferrioxamine, clioquinol, VK-28, and a piperazine chelator. J Neural Transm Suppl 237-247.
    • (2006) J Neural Transm Suppl , pp. 237-247
    • Bandyopadhyay, S.1    Huang, X.2    Cho, H.3    Greig, N.H.4    Youdim, M.B.5    Rogers, J.T.6
  • 73
    • 0032577578 scopus 로고    scopus 로고
    • Physical interaction of ApoE with amyloid precursor protein independent of the amyloid Abeta region in vitro
    • Hass S, Fresser F, Kochl S, Beyreuther K, Utermann G, Baier G. (1998). Physical interaction of ApoE with amyloid precursor protein independent of the amyloid Abeta region in vitro. J Biol Chem 273, 13892-13897.
    • (1998) J Biol Chem , vol.273 , pp. 13892-13897
    • Hass, S.1    Fresser, F.2    Kochl, S.3    Beyreuther, K.4    Utermann, G.5    Baier, G.6
  • 74
    • 77953286012 scopus 로고    scopus 로고
    • Abeta-independent roles of apolipoprotein E4 in the pathogenesis of Alzheimer's disease
    • Huang Y. (2010). Abeta-independent roles of apolipoprotein E4 in the pathogenesis of Alzheimer's disease. Trends Mol Med 16, 287-294.
    • (2010) Trends Mol Med , vol.16 , pp. 287-294
    • Huang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.