Plasma amyloid-β, Aβ1-42, load is reduced by haemodialysis

被引:0
|
作者
Rubio, Isabel
Caramelo, Carlos
Gil, Ascencion
Lopez, Maria Dolores
de Yebenez, Justo Garcia
机构
[1] Univ Complutense Madrid, Fac Med, Banco Tejidos Invest Neurol, E-28040 Madrid, Spain
[2] Hosp Ramon & Cajal, Serv Bioquim, E-28034 Madrid, Spain
[3] Hosp Ramon & Cajal, Neurol Serv, E-28034 Madrid, Spain
关键词
amyloid; plasma; haemodialysis; dementia; therapy;
D O I
暂无
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Patients with chronic renal failure treated with haemodialysis have vascular risk factors that, in the general population, are associated with increased prevalence of Alzheimer's disease (AD). Patients in haemodialysis, however, present different kinds of dementia but they do not have an increased risk of AD. We have hypothesized that amyloid-beta (A,beta)(1-42) is washed out from plasma during the dialysis and that this procedure enhances A beta elimination and reduces the risk of AD. We have measured plasma A beta(1-42) levels in I I patients with renal failure, before and after haemodialysis. A single procedure reduced the plasma A beta levels in all subjects with it mean decrement of 30% of baseline. Since A beta deposition could be altered by certain metals like Cu and Zn, we have also measured the effects of dialysis on the levels of these ions in plasma. We found no changes in levels of Cu and Zn after dialysis. Haemodialysis, therefore, reduces very effectively plasma A beta without modifying Cu and Zn levels. The potential use of this strategy in patients with AD requires further investigation.
引用
收藏
页码:439 / 443
页数:5
相关论文
共 50 条
  • [31] A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration
    Marshall, Karen E.
    Vadukul, Devkee M.
    Dahal, Liza
    Theisen, Alina
    Fowler, Milena W.
    Al-Hilaly, Youssra
    Ford, Lenzie
    Kemenes, Gyorgy
    Day, Iain J.
    Staras, Kevin
    Serpell, Louise C.
    SCIENTIFIC REPORTS, 2016, 6
  • [32] Stability of early-stage amyloid-β(1-42) aggregation species
    Coalier, Kelley A.
    Paranjape, Geeta S.
    Karki, Sanjib
    Nichols, Michael R.
    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2013, 1834 (01): : 65 - 70
  • [33] Controlling Amyloid-β Peptide(1-42) Oligomerization and Toxicity by Fluorinated Nanoparticles
    Saraiva, Ana M.
    Cardoso, Isabel
    Carmo Pereira, M.
    Coelho, Manuel A. N.
    Joao Saraiva, Maria
    Moehwald, Helmuth
    Brezesinski, Gerald
    CHEMBIOCHEM, 2010, 11 (13) : 1905 - 1913
  • [34] Critical aggregation concentration for the formation of early Amyloid-β (1-42) oligomers
    Novo, Mercedes
    Freire, Sonia
    Al-Soufi, Wajih
    SCIENTIFIC REPORTS, 2018, 8
  • [35] Interferon-γ increases neuronal death in response to amyloid-β1-42
    Bate, Clive
    Kempster, Sarah
    Last, Victoria
    Williams, Alun
    JOURNAL OF NEUROINFLAMMATION, 2006, 3 (1)
  • [36] Prevention of Amyloid-β Fibril Formation Using Antibodies Against the C-terminal Region of Amyloid-β1-40 and Amyloid-β1-42
    Montanes, Maria
    Casabona, Diego
    Sarasa, Leticia
    Pesini, Pedro
    Sarasa, Manuel
    JOURNAL OF ALZHEIMERS DISEASE, 2013, 34 (01) : 133 - 137
  • [37] Interferon-γ increases neuronal death in response to amyloid-β1-42
    Clive Bate
    Sarah Kempster
    Victoria Last
    Alun Williams
    Journal of Neuroinflammation, 3
  • [38] Comparison of Alzheimer's amyloid-β(1-40) and amyloid-β(1-42) fibrils as determined by solution NMR spectroscopy
    Olofsson, A.
    Lindhagen-Persson, M.
    Sauer-Eriksson, A. E.
    Ohman, A.
    AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, 2006, 13 : 50 - 50
  • [39] A Sensitive and Cost-Effective Chemiluminescence ELISA for Measurement of Amyloid-β 1-42 Peptide in Human Plasma
    Mehta, Pankaj D.
    Patrick, Bruce A.
    Miller, David L.
    Coyle, Patricia K.
    Wisniewski, Thomas
    JOURNAL OF ALZHEIMERS DISEASE, 2020, 78 (03) : 1237 - 1244
  • [40] Electrochemical Immunosensor for the Sensitive Detection of Alzheimer's Biomarker Amyloid-β (1-42) Using the Heme-amyloid-β (1-42) Complex as the Signal Source
    Ding, Minling
    Shu, Qi
    Zhang, Nan
    Yan, Chaoren
    Niu, Huizhe
    Li, Xiaoqian
    Guan, Ping
    Hu, Xiaoling
    ELECTROANALYSIS, 2022, 34 (02) : 263 - 274