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Immunoprecipitation of peptide fragments common to all Tau protein isoforms using phospho-insensitive magnetic immunosorbents for diagnosis of Alzheimer´s disease

Rok: 2011

Druh publikace: ostatní - přednáška nebo poster

Strana od-do: nestránkováno

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Jazyk	Název	Abstrakt	Klíčová slova
eng	Immunoprecipitation of peptide fragments common to all Tau protein isoforms using phospho-insensitive magnetic immunosorbents for diagnosis of Alzheimer´s disease	Tau proteins are structural microtubule-associated proteins primarily localized in the axonal compartment of neurons. The aim of this study was to develop an effective miniaturized system for the determination of total soluble Tau in biological fluids. In the brain, Tau proteins constitute a family of six isoforms and there are seventy-nine putative Ser or Thr phosphorylation sites. Due to the complexity associated with Tau molecules we decided to focus on the detection of only a one fragment of the whole protein, which is common to all isoforms and can be detected regardless of the phosphorylation state. We used phosphorylation-insensitive antibodies that recognize all six Tau-isoforms, namely DC25 and HT7. The antibodies were covalently coupled on magnetic microparticles for immunoprecipitation of recombinant Tau proteins fragmented chemically with CNBr and/or proteolytically with Clostripain. Detection of specific fragments was performed using MALDI-TOF-MS and/or WB-analyses.	Tau protein; Alzheimer’s disease; magnetic immunosorbent; immunoprecipitation; peptide fragments

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