Basic and clinical studies on ApoE gene typing by line probe assay
(LiPA) as a biological marker for Alzheimer's disease and related
disorders: Multicenter study in Japan

Nishimura, T; Takeda, Mayu; Shinosaki, Kazuhiro; Nishikawa, Tomokazu; Nakamura, Yoko; Yoshida, Yasuji; Sasaki, Hiroshi; Arai, Hidee; Hirai, S; Shouji, Michi; Isse, Kunihiro; Tanaka, Kuniaki; Hamamoto, Makoto; Yamamoto, Hideki; Matsubayashi, T; Nakashima, Kenichiro; Urakami, Katsuya; Adachi, Yoshiki; Nakamura, Shin; Toji, Hiromasa; Yoshida, Hiroto

doi:10.1358/mf.1998.20.9.487527

Cited by 8 publications

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Genotyping of Apolipoprotein E: Comparative Evaluation of Different Protocols

et al. 2003

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Disease-associated gene polymorphisms provide both scientific insight into pathophysiological mechanisms and clinical information regarding risk and progression. Of special interest is the epsilon4 allele of the apolipoprotein E gene, which has emerged as a substantial risk factor for late-onset forms of Alzheimer disease and also influences the risk of cardiovascular disease. Genotyping of apolipoprotein E can be performed by several methods; presented here are a quality and cost-benefit analysis of four different protocols on a cohort of 42 clinical samples is included in the unit. Each method resulted in genotyping with a high sensitivity and specificity. The newer microtiter-plate-based high-throughput techniques, fluorescence polarization and SNaPshot analysis, were as reliable as the traditional techniques of restriction fragment length polymorphism analysis and reverse hybridization. The reverse hybridization method tends to be more cost- and time-effective when the number of analyses is limited, although economy of scale favors fluorescence polarization or SNaPshot analysis in larger studies. The latter approaches also provide the flexibility to investigate other polymorphic disease markers.

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Genotyping of Apolipoprotein E: Comparative Evaluation of Different Protocols

et al. 2003

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Electrophoretic separation of amyloid β peptides in plasma

et al. 2004

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In this prospective study, for the first time we have separated and quantified amyloid beta (Abeta) peptides in the plasma of patients with Alzheimer's disease (AD, n = 8) and age- and environment-matched healthy controls (n = 9) with urea-based Abeta-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)/immunoblot. In addition to the Abeta peptides 1-37/38/39/40/42, which we recently identified as regular constituents of human cerebrospinal fluid (CSF), we have observed a novel electrophoretic band migrating slightly cathodically to Abeta1-42. Since a standard peptide with the amino acid sequence Abeta2-40 migrates in the same position, we hypothesize that this plasma-specific band may correspond to Abeta2-40. The concentration of Abeta peptides in the plasma has been approximately 100-fold lower compared to the CSF. Interestingly, the concentration of the two shortest peptides and the longest one of these considered here (i.e., Abeta1-37/38/42) have increased significantly when the samples have been frozen at -80 degrees C before immunoprecipitation, while the 'middle-length' peptides (i.e., Abeta1-39/40) have not been affected by this procedure. We have not observed significant differences of the Abeta peptides concentrations between AD and control subjects. Our method can be used to investigate the significance of plasma Abeta peptides in neurodegenerative disorders, and to monitor the efficiency of drugs with beta/gamma-secretase inhibitory potency.

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