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Surjyadipta Bhattacharjee, Jim M. Hill, Aileen I. Pogue, Walter J. Lukiw; Retinal Amyloid Peptides and complement factor H (CFH) in Transgenic Models of Alzheimer’s Disease (AD). Invest. Ophthalmol. Vis. Sci. 2012;53(14):3309.
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© ARVO (1962-2015); The Authors (2016-present)
Murine transgenic models of Alzheimer’s disease (Tg-AD) have been useful to analyze the contribution of beta-amyloid precursor protein (βAPP), Aβ42 peptide deposition, and the pro-inflammatory mechanisms that characterize Alzheimer-type neuropathology. In this report we have studied the levels of βAPP, Aβ40- and Aβ42-peptide, and the innate immune and inflammatory response regulator complement factor H (CFH) in the brain and retina in 4 different Tg-AD models including Tg2576, PSAPP, 3xTg-AD and 5xFAD.
Aβ42-peptide+IL-1β-induced stress; bioinformatics; DNA array; DNA sequencing; human brain postmortem tissue; human retinal tissue; human retinal and brain cells in primary culture; gel shift assay; micro-RNA array; Northern micro-dot blot analysis; RT-PCR; transfection assay; Western immunohistochemistry
Aged, symptomatic 5xFAD mice, showed the highest retinal abundance of Aβ42 peptides and deficits in CFH. The retina, superior colliculus and primary visual cortex obtained from late-stage Alzheimer’s disease patients revealed up-regulated amyloidogenic and inflammatory signaling along the entire anteroposterior axis of the retinal-primary visual cortex pathway.
Aging Tg-AD mice, and in particular Tg2576 and 5xFAD, display targeted Aβ42-peptide accumulation across the entire retinal-primary visual cortex signaling pathway. Advanced Tg-AD murine models may be a useful in studying the mechanisms of CFH biology and amyloid-mediated inflammatory degeneration in both the aging brain and retina.
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