Simultaneous detection of tau phospho-epitopes with haptenylated antibodies.
Neurofibrillary tangles as a neuropathological hallmark of Alzheimer's disease are mainly composed of abnormally phosphorylated microtubule-associated protein tau. The present work was primarily focused on the immunohistochemical characterization of recently developed monoclonal antibodies directed against disease-associated epitopes. Anti-phospho-threonine 212/phospho-serine 214 (HPT-1), anti-phospho-threonine 231/phospho-serine 235 (HPT-101) and their biotinylated derivatives were shown to be sensitive markers for the immunohistochemical detection of neuropathological alterations during Alzheimer's disease. Triple carbocyanine immunofluorescence labelling was based on digoxigenylated, fluoresceinated and biotinylated primary antibodies. AT8-immunolabelling of phospho-serine 202 and phospho-threonine 205 combined with HPT-1 and HPT-101-staining revealed similar distribution patterns of the three double-phosphorylated tau epitopes in the neocortex of patients with Alzheimer's disease.
Härtig
Wolfgang
W
Paul Flechsig Institute for Brain Research, University of Leipzig, Germany. hartig@medizin.uni-leipzig.de
Lehmann
Jörg
J
Stieler
Jens
J
Singer
David
D
Grosche
Jens
J
Arendt
Thomas
T
Hoffmann
Ralf
R
D000544:Alzheimer Disease / Q000175:diagnosis / Q000473:pathology; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D000939:Epitopes / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D019579:Neocortex / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism*; D010766:Phosphorylation; D012694:Serine / Q000378:metabolism; D013912:Threonine / Q000378:metabolism; D016875:tau Proteins
D000911:Antibodies, Monoclonal; D000939:Epitopes; C054369:MAPT protein, human; D009419:Nerve Tissue Proteins; D016875:tau Proteins; D013912:Threonine; D012694:Serine