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  • Title: Concomitant detection of beta-amyloid peptides with N-terminal truncation and different C-terminal endings in cortical plaques from cases with Alzheimer's disease, senile monkeys and triple transgenic mice.
    Author: Härtig W, Goldhammer S, Bauer U, Wegner F, Wirths O, Bayer TA, Grosche J.
    Journal: J Chem Neuroanat; 2010 Sep; 40(1):82-92. PubMed ID: 20347032.
    Abstract:
    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., non-human primates. Beta-amyloid(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. Amino-terminally 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-amyloid(pE3-x) and total beta-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.
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