Alzheimer’s Disease Using a Mouse Model: Genotyping and Behavioral Studies

Alzheimer’s Disease Using a Mouse Model: Genotyping and Behavioral Studies

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Alzheimer’s disease (AD) is the most common form of age-related dementia. While first described over 100 years ago, little is known about how or when the disease process begins. The most recent reports estimate that 5.2 million Americans are living with AD (Fargo & Bleiler, 2014). The disease is characterized/diagnosed, in part, due to the cognitive decline of the patients and the accumulation of amyloid and neuritic plaques and neurofibrillary tangles. Unlike other cognitive disorders, AD affects different classes of neurons (Selkoe, 2001). The amyloid hypothesis suggests that the A amyloid plaques characteristic of AD are responsible for the onset of the disease (Hardy & Selkoe, 2002), although A levels do not correlate well with cognitive performance in the disease. These A plaques are composed of a protein originating from the cleavage of the larger amyloid precursor protein (APP). In order to better understand the onset and progression of AD, researchers have turned to the development of mouse models.
The creation of transgenic mice expressing a mutant from of human APP with two point mutations (APP695 K670N-M671L) showed a significant increase in plaque formation in older mice (10-12 months), but saw no increase in plaque formation in young mice (3 months) (Hsiao et al., 1996). Additionally, mice expressing a mutant human form of presenilin 1 (PS1 M146L), the -secretase complex involved in A processing, show no learning phenotype even with the accumulation of one isoform of the A protein (Duff et al., 1996; Duyckaerts, Potier, & Delatour, 2008). When both the human APP mutant and PS1 mutant proteins are included in the same transgenic mouse (APP/PS1), an earlier onset (3 months) of plaque formation and learning defect...


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...-regulation of the type 3 ryanodine receptor is neuroprotective in the TgCRND8 mouse model of Alzheimer's disease. Journal of Neurochemistry, 112(2), 356–365. doi:10.1111/j.1471-4159.2009.06487.x
Wehrens, X. H. T., Lehnart, S. E., Reiken, S., van der Nagel, R., Morales, R., Sun, J., et al. (2005). Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure. Proceedings of the National Academy of Sciences of the United States of America, 102(27), 9607–9612. doi:10.1073/pnas.0500353102
Wehrens, X. H. T., Lehnart, S. E., Reiken, S., Vest, J. A., Wronska, A., & Marks, A. R. (2006). Ryanodine receptor/calcium release channel PKA phosphorylation: a critical mediator of heart failure progression. Proceedings of the National Academy of Sciences of the United States of America, 103(3), 511–518. doi:10.1073/pnas.0510113103

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