Browsing by Author "Bauer, Ute"

The disturbed metabolism of beta-amyloid peptides generated from amyloid precursor protein is widely considered as a main factor during the pathogenesis of Alzheimer's disease. A neuropathological hallmark in the brains from cases with Alzheimer's disease are senile plaques mainly composed of hardly soluble beta-amyloid peptides comprising up to 43 amino acids. Age-dependent cortical beta-amyloidosis was also shown in several transgenic mice and old individuals from various mammalian species, e.g., nonhuman primates. beta-Amyloicli(1-42) is believed to be the main component in the core of senile plaques, whereas less hydrophobic beta-amyloid(1-40) predominantly occurs in the outer rim of plaques. Aminoterminally truncated pyroglutamyl-beta-amyloid(pE3-x), was recently found to be a beta-amyloid species of high relevance to the progression of the disease. While a few biochemical studies provided data on the co-occurrence of several beta-amyloid forms, their concomitant histochemical detection is still lacking. Here, we present a novel triple immunofluorescence labelling of amino- and differently carboxy-terminally truncated beta-amyloid peptides in cortical plaques from a case with Alzheimer's disease, senile macaques and baboons, and triple transgenic mice with age-dependent beta-amyloidosis and tau hyperphosphorylation. Additionally, beta-amyloidop(E3-x), and total P-amyloid were concomitantly detected with beta-amyloid peptides ending with amino acid 40 or 42, respectively. Simultaneous staining of several beta-amyloid species reveals for instance vascular amyloid containing beta-amyloid(pE3-x) in Alzheimer's disease and monkeys, and may contribute to the further elucidation of beta-amyloidosis in neurodegenerative disorders and animal models. (C) 2010 Elsevier B.V. All rights reserved.