(Siest et al., 1995). ApoE3 influences the clearance of amyloid-B peptides, therefore preventing amyloid-B peptide deposits (Mahley and Rall, 2000). Nevertheless, the ApoE4 is one of the dysfunctional isoforms of the protein and can evidently increase one’s susceptibility to late-onset of Alzheimer’s disease. One of the first evidences of identifying ApoE4 as a probable risk factor in Alzheimer’s Disease came from Shimano et al., who found a “twofold greater relative frequency of the E4 allele in AD pateints” (Siest et al., 1995). Later, Namba et al. (1991, p.163) conducted immunohistochemical experiments in patients with Alzheimers disease using antibodies to ApoE. Through ApoE immunoreactivity, the localization of ApoE4 protein in amyloid plaques and neurofibrillary tangles in patients with Alzheimer’s Disease was observed. (Namba et al.,
(Siest et al., 1995). ApoE3 influences the clearance of amyloid-B peptides, therefore preventing amyloid-B peptide deposits (Mahley and Rall, 2000). Nevertheless, the ApoE4 is one of the dysfunctional isoforms of the protein and can evidently increase one’s susceptibility to late-onset of Alzheimer’s disease. One of the first evidences of identifying ApoE4 as a probable risk factor in Alzheimer’s Disease came from Shimano et al., who found a “twofold greater relative frequency of the E4 allele in AD pateints” (Siest et al., 1995). Later, Namba et al. (1991, p.163) conducted immunohistochemical experiments in patients with Alzheimers disease using antibodies to ApoE. Through ApoE immunoreactivity, the localization of ApoE4 protein in amyloid plaques and neurofibrillary tangles in patients with Alzheimer’s Disease was observed. (Namba et al.,