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Copyright ©The Author(s) 2020.
World J Biol Chem. Sep 27, 2020; 11(2): 62-75
Published online Sep 27, 2020. doi: 10.4331/wjbc.v11.i2.62
Table 1 Mouse models used for the study of Alzheimer disease
StrainPromoter usedProteins expressedPathogenyRef.
3xTG–ADThy1 and mPS1Mutant of APP (hAPP695, Swedish mutation), PS1 (PSEN1, M146V) and tau (hTau-4R0N, P301L)Mice containing these mutations develop β-amyloid plaques and NFTs resembling the brain with AD[36,60,96,97]
CK-p25tetO (tet operator)These mice overexpress the truncated form of p35, p25p25 activates CDK5 (cyclin-dependent kinase 5), implicated in AD. CK-p25 mice develop neuronal loss, β-amyloid accumulation and loss of synaptic terminations in the hippocampus and cortex as well as memory deficits[57,98,99]
APPPS 1-21 /HDAC6–/– crossbredThy1Mutated APP (KM670/671NL) and the mutated presenilin 1 (L166P)Mice develop β-amyloid plaques leading to cerebral amyloidosis, dystrophic synaptic boutons, hyper-phosphorylated tau, inflammatory responses and the impairment of cognitive function[64,100,101]
TgCRND8Hamster PrPhAPP695 Swe/IndThe brain of mice contains plaques formed by depositions of β-amyloid, leading to inflammation and cognitive impairments. There is also neuronal loss, accumulation of NFTs, and neuritic changes similar to those observed in AD[93,102,103]
Tg19959Hamster PrPhAPP695 with two familial mutations (Swedish and Indiana mutations: K670N/M671L and V717F, respectively). (FVB X 129S6F1 background)Mice overexpress β-amyloid 1-42 peptide and Bace1 forming plaques[5,93,102,104]
Tg2576-APPswe crossbredHamster PrP and Mouse PrPThe Swedish mutation (hAPP695) and m/hAPP6953 (extra and intracellular regions of mouse β-amyloid, a human β-amyloid sequence and the Swedish mutations of β-amyloid, K594N/M595L)These mice develop β-amyloid plaques deposition and memory deficits[94,105,106]
APP/PSIThyMutated APP (KM670/671 NL) and mutated presenilin 1 (L166P)Mice show dystrophic synaptic, hyperphosphorylation of tau, gliosis, and neuronal loss in the dentate gyrus as well as impairment in reversal learning[95,101]