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P4‐200: Cholinergic impairment in Parkinson Plus Syndrome: A molecular imaging study
Author(s) -
Mazere Joachim,
Sibon Igor,
Messner Wassilios,
Mayo Willy,
Barret Olivier,
Guilloteau Denis,
Tison François,
Allard Michele
Publication year - 2009
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2009.04.767
Subject(s) - nucleus basalis , thalamus , cholinergic , neuroscience , medicine , striatum , spect imaging , cholinergic neuron , psychology , nuclear medicine , dopamine
enriched tau proteins from the control and transgenic mice were immunoprecipitated with a monoclonal antibody against tau. The immuno-precipitants were then digested with trypsin. The phosphorylated peptides in the control and transgenic mouse samples were enriched once again by the CHT-based method. The phosphopeptides were then analyzed by MALDI-TOF mass spectrometry and the peptide mass profiles of tau protein were compared between the age-matched wild type and transgenic animals to examine the changes in tau protein phosphorylation. Conclusions: Our study demonstrated that CHT-based fractionation is an easy-to-use, fast and convenient method for phosphoprotein/peptide enrichment with high binding capacity. It could potentially be used to enrich highly-phophorylated proteins and facilitate the biochemical study of hyperphosphorylated tau in Alzheimer’s disease.