메뉴 건너뛰기




Volumn 44, Issue 3, 2015, Pages 458-464

The peripheral blood of Aβ binding RBC as a biomarker for diagnosis of Alzheimer's disease

Author keywords

Alzheimer's disease; A fibrils; Older people; Red blood cells; Thioflavin T

Indexed keywords

AMYLOID BETA PROTEIN; THIOFLAVINE; BIOLOGICAL MARKER;

EID: 84929154954     PISSN: 00020729     EISSN: 14682834     Source Type: Journal    
DOI: 10.1093/ageing/afv009     Document Type: Article
Times cited : (29)

References (30)
  • 1
    • 84867956994 scopus 로고    scopus 로고
    • Alzheimer's disease, cerebrovascular disease, and the β-amyloid cascade
    • Honjo K, Black SE, Verhoeff NPLG. Alzheimer's disease, cerebrovascular disease, and the β-amyloid cascade. Can J Neurol Sci 2012; 39: 712-28.
    • (2012) Can J Neurol Sci , vol.39 , pp. 712-728
    • Honjo, K.1    Black, S.E.2    Verhoeff, N.P.L.G.3
  • 2
    • 1242331823 scopus 로고    scopus 로고
    • Is Alzheimer's disease a neurodegenerative or a vascular disorder? Data, dogma, and dialectics
    • de la Torre JC. Is Alzheimer's disease a neurodegenerative or a vascular disorder? Data, dogma, and dialectics. Lancet Neurol 2004; 3: 184-90.
    • (2004) Lancet Neurol , vol.3 , pp. 184-190
    • de la Torre, J.C.1
  • 3
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
    • Chimon S, Shaibat MA, Jones CR et al. Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid. Nat Struct Mol Biol 2007; 14: 1157-64.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3
  • 4
    • 75949127362 scopus 로고    scopus 로고
    • Inflammation, microglia and Alzheimer's disease
    • Cameron B, Landreth GE. Inflammation, microglia and Alzheimer's disease. Neurobiol Dis 2010; 37: 503.
    • (2010) Neurobiol Dis , vol.37 , pp. 503
    • Cameron, B.1    Landreth, G.E.2
  • 5
    • 70449411818 scopus 로고    scopus 로고
    • Oxidatively modified, mitochondriarelevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment
    • Sultana R, Butterfield DA. Oxidatively modified, mitochondriarelevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment. J Bioenerg Biomembr 2009; 41: 441-6.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 441-446
    • Sultana, R.1    Butterfield, D.A.2
  • 7
    • 20244388150 scopus 로고    scopus 로고
    • Red cell interactions with amyloid-β 1-40 fibrils in a murine model
    • Ravi LB, Poosala S, Ahn D et al. Red cell interactions with amyloid-β 1-40 fibrils in a murine model. Neurobiol Dis 2005; 19: 28-37.
    • (2005) Neurobiol Dis , vol.19 , pp. 28-37
    • Ravi, L.B.1    Poosala, S.2    Ahn, D.3
  • 8
    • 84934440941 scopus 로고    scopus 로고
    • Do red blood cell-β-amyloid interactions alter oxygen delivery in Alzheimer's disease?
    • Kang KA, Bruley DF, eds. USA: Springer
    • Mohanty JG, Eckley DM, Williamson JD et al. Do red blood cell-β-amyloid interactions alter oxygen delivery in Alzheimer's disease? In: Kang KA, Bruley DF, eds. Oxygen Transport to Tissue XXIX. USA: Springer, 2008; 29-35.
    • (2008) Oxygen Transport to Tissue XXIX , pp. 29-35
    • Mohanty, J.G.1    Eckley, D.M.2    Williamson, J.D.3
  • 9
    • 79954435392 scopus 로고    scopus 로고
    • Amyloid β-induced erythrocytic damage and its attenuation by carotenoids
    • Nakagawa K, Kiko T, Miyazawa T et al. Amyloid β-induced erythrocytic damage and its attenuation by carotenoids. FEBS Lett 2011; 585: 1249-54.
    • (2011) FEBS Lett , vol.585 , pp. 1249-1254
    • Nakagawa, K.1    Kiko, T.2    Miyazawa, T.3
  • 10
    • 84869208877 scopus 로고    scopus 로고
    • Amyloid β Levels in human red blood cells
    • Kiko T, Nakagawa K, Satoh A et al. Amyloid β Levels in human red blood cells. PloS One 2012; 7: e49620.
    • (2012) PloS One , vol.7
    • Kiko, T.1    Nakagawa, K.2    Satoh, A.3
  • 11
    • 77951228584 scopus 로고    scopus 로고
    • Alterations in the red blood cell membrane proteome in Alzheimer's subjects reflect disease-related changes and provide insight into altered cell morphology
    • Mohanty JG, Shukla HD, Williamson JD et al. Alterations in the red blood cell membrane proteome in Alzheimer's subjects reflect disease-related changes and provide insight into altered cell morphology. Proteome Sci 2010; 8: 11.
    • (2010) Proteome Sci , vol.8 , pp. 11
    • Mohanty, J.G.1    Shukla, H.D.2    Williamson, J.D.3
  • 12
    • 84878653298 scopus 로고    scopus 로고
    • Changes in phospholipid composition of erythrocyte membrane in Alzheimer's disease
    • Oma S, Mawatari S, Saito K et al. Changes in phospholipid composition of erythrocyte membrane in Alzheimer's disease. Dement Geriatr Cogn Dis Extra 2012; 2: 298-303.
    • (2012) Dement Geriatr Cogn Dis Extra , vol.2 , pp. 298-303
    • Oma, S.1    Mawatari, S.2    Saito, K.3
  • 13
    • 0026069358 scopus 로고
    • Erythrocyte membrane characteristics indicate abnormal cellular aging in patients with Alzheimer's disease
    • Bosman G, Bartholomeus IGP, De Man AJM et al. Erythrocyte membrane characteristics indicate abnormal cellular aging in patients with Alzheimer's disease. Neurobiol Aging 1991; 12: 13-8.
    • (1991) Neurobiol Aging , vol.12 , pp. 13-18
    • Bosman, G.1    Bartholomeus, I.G.P.2    De Man, A.J.M.3
  • 14
    • 33846135452 scopus 로고    scopus 로고
    • Monoclonal antibodies that target pathological assemblies of A β
    • Lambert MP, Velasco PT, Chang L et al. Monoclonal antibodies that target pathological assemblies of A β. J Neurochem 2007; 100: 23-35.
    • (2007) J Neurochem , vol.100 , pp. 23-35
    • Lambert, M.P.1    Velasco, P.T.2    Chang, L.3
  • 15
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed R, Head E, Sarsoza F et al. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2007; 2: 18.
    • (2007) Mol Neurodegener , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3
  • 16
    • 27644493692 scopus 로고    scopus 로고
    • Globular amyloid β-peptide 1-42 oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease
    • Barghorn S, Nimmrich V, Striebinger A et al. Globular amyloid β-peptide 1-42 oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease. J Neurochem 2005; 95: 834-47.
    • (2005) J Neurochem , vol.95 , pp. 834-847
    • Barghorn, S.1    Nimmrich, V.2    Striebinger, A.3
  • 17
    • 34548614101 scopus 로고    scopus 로고
    • Sensitive ELISA detection of amyloid-β protofibrils in biological samples
    • Englund H, Sehlin D, Johansson AS et al. Sensitive ELISA detection of amyloid-β protofibrils in biological samples. J Neurochem 2007; 103: 334-45.
    • (2007) J Neurochem , vol.103 , pp. 334-345
    • Englund, H.1    Sehlin, D.2    Johansson, A.S.3
  • 18
    • 78649754766 scopus 로고    scopus 로고
    • Amyloid-β oligomer specificity mediated by the IgM isotype-implications for a specific protective mechanism exerted by endogenous auto-antibodies
    • Lindhagen-Persson M, Brännström K, Vestling M et al. Amyloid-β oligomer specificity mediated by the IgM isotype-implications for a specific protective mechanism exerted by endogenous auto-antibodies. PLoS One 2010; 5: e13928.
    • (2010) PLoS One , vol.5
    • Lindhagen-Persson, M.1    Brännström, K.2    Vestling, M.3
  • 19
    • 84870697538 scopus 로고    scopus 로고
    • Amyloid-β oligomer detection by ELISA in cerebrospinal fluid and brain tissue
    • Bruggink KA, Jongbloed W, Biemans EALM et al. Amyloid-β oligomer detection by ELISA in cerebrospinal fluid and brain tissue. Anal Biochem 2013; 433: 112-20.
    • (2013) Anal Biochem , vol.433 , pp. 112-120
    • Bruggink, K.A.1    Jongbloed, W.2    Biemans, E.A.L.M.3
  • 20
    • 0033563079 scopus 로고    scopus 로고
    • Inhibition of fibril formation in β-amyloid peptide by a novel series of benzofurans
    • Howlett D, Perry A, Godfrey F et al. Inhibition of fibril formation in β-amyloid peptide by a novel series of benzofurans. Biochem J 1999; 340: 283-9.
    • (1999) Biochem J , vol.340 , pp. 283-289
    • Howlett, D.1    Perry, A.2    Godfrey, F.3
  • 21
    • 0034235515 scopus 로고    scopus 로고
    • Oligomerization of β-amyloid of the Alzheimer's and the Dutch-cerebral-haemorrhage types
    • Sian A, Frears E, El-Agnaf O et al. Oligomerization of β-amyloid of the Alzheimer's and the Dutch-cerebral-haemorrhage types. Biochem J 2000; 349: 299-308.
    • (2000) Biochem J , vol.349 , pp. 299-308
    • Sian, A.1    Frears, E.2    El-Agnaf, O.3
  • 22
    • 52949118083 scopus 로고    scopus 로고
    • Peripheral A β subspecies as risk biomarkers of Alzheimer's disease
    • Schupf N, Tang MX, Fukuyama H et al. Peripheral A β subspecies as risk biomarkers of Alzheimer's disease. Proc Natl Acad Sci USA 2008; 105: 14052-57.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14052-14057
    • Schupf, N.1    Tang, M.X.2    Fukuyama, H.3
  • 23
    • 52449103780 scopus 로고    scopus 로고
    • Amyloid oligomer conformation in a group of natively folded proteins
    • Yoshiike Y, Minai R, Matsuo Y et al. Amyloid oligomer conformation in a group of natively folded proteins. PLoS One 2008; 3: e3235.
    • (2008) PLoS One , vol.3
    • Yoshiike, Y.1    Minai, R.2    Matsuo, Y.3
  • 24
    • 76649138290 scopus 로고    scopus 로고
    • Binding mode of thioflavin T and other molecular probes in the context of amyloid fibrils-current status
    • Groenning M. Binding mode of thioflavin T and other molecular probes in the context of amyloid fibrils-current status. J Chem Biol 2010; 3: 1-18.
    • (2010) J Chem Biol , vol.3 , pp. 1-18
    • Groenning, M.1
  • 25
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    • Biancalana M, Koide S. Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochim Biophys Acta 2010; 1804: 1405-12.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 27
    • 0032559575 scopus 로고    scopus 로고
    • Alzheimer's amyloid β interaction with normal human plasma high density lipoprotein: association with apolipoprotein and lipids
    • Koudinov AR, Berezov TT, Kumar A et al. Alzheimer's amyloid β interaction with normal human plasma high density lipoprotein: association with apolipoprotein and lipids. Clin Chim Acta 1998; 270: 75-84.
    • (1998) Clin Chim Acta , vol.270 , pp. 75-84
    • Koudinov, A.R.1    Berezov, T.T.2    Kumar, A.3
  • 28
    • 0034708137 scopus 로고    scopus 로고
    • Amyloid-β peptides interact with plasma proteins and erythrocytes: implications for their quantitation in plasma
    • Kuo YM, Kokjohn TA, Kalback W et al. Amyloid-β peptides interact with plasma proteins and erythrocytes: implications for their quantitation in plasma. Biochem Biophys Res Commun 2000; 268: 750-6.
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 750-756
    • Kuo, Y.M.1    Kokjohn, T.A.2    Kalback, W.3
  • 29
    • 80054011898 scopus 로고    scopus 로고
    • Alzheimer's disease is characterized by more low-density erythrocytes with increased volume and enhanced β-amyloid x-40 content
    • Järemo P, Milovanovic M, Nilsson S et al. Alzheimer's disease is characterized by more low-density erythrocytes with increased volume and enhanced β-amyloid x-40 content. J Intern Med 2011; 270: 489-92.
    • (2011) J Intern Med , vol.270 , pp. 489-492
    • Järemo, P.1    Milovanovic, M.2    Nilsson, S.3
  • 30
    • 31944449691 scopus 로고    scopus 로고
    • Evidence that Perutz's double-betastranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes
    • Singer SJ, Dewji NN. Evidence that Perutz's double-betastranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes. Proc Natl Acad Sci USA 2006; 103: 1546-50.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1546-1550
    • Singer, S.J.1    Dewji, N.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.