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Amyloid beta1-40 quantification in CSF: comparison between chromatographic and immunochemical methods.

Artikel i vetenskaplig tidskrift
Författare A H Simonsen
S F Hansson
Ulla Rüetschi
J McGuire
V N Podust
H A Davies
P Mehta
G Waldemar
Henrik Zetterberg
N Andreasen
Anders Wallin
Kaj Blennow
Publicerad i Dementia and geriatric cognitive disorders
Volym 23
Nummer/häfte 4
Sidor 246-50
ISSN 1420-8008
Publiceringsår 2007
Publicerad vid Institutionen för neurovetenskap och fysiologi, sektionen för psykiatri och neurokemi
Sidor 246-50
Språk en
Länkar dx.doi.org/10.1159/000100020
Ämnesord Aged, Aged, 80 and over, Alzheimer Disease, cerebrospinal fluid, Amyloid beta-Protein, analysis, cerebrospinal fluid, Biological Markers, analysis, cerebrospinal fluid, Cerebrospinal Fluid, chemistry, Enzyme-Linked Immunosorbent Assay, methods, Female, Humans, Immunochemistry, methods, Male, Peptide Fragments, analysis, cerebrospinal fluid, Reference Values, Reproducibility of Results, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, methods
Ämneskategorier Neurokemi

Sammanfattning

BACKGROUND/AIMS: Amyloid beta (Abeta) is the principal component of senile plaques, one of the hallmarks of Alzheimer's disease (AD). Evidence is accumulating that soluble aggregates (oligomers) of Abeta are important in the pathogenesis of AD. METHODS: We compared three different methods for quantification of the 40 amino acid form of Abeta (Abeta40) in CSF, two based on antibodies [ELISA and surface-enhanced laser desorption/ionization-time of flight (SELDI-TOF) with antibody-coated arrays] and one based on direct binding of proteins to a protein array [SELDI-TOF and immobilized metal affinity [copper] (IMAC30)]. RESULTS: CSF Abeta40 concentration was only found to be significantly elevated in AD (127% of control levels; p=0.0095) using SELDI-TOF with IMAC30 arrays. CONCLUSIONS: These data suggest that the measured Abeta level in CSF may differ depending on whether antibody-based methods are used or not, possibly caused by epitope masking due to Abeta oligomerization or to binding of Abeta to carrier proteins.

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