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Clinical Conference Lack of influence of the apolipoprotein E genotype on the outcome of selegiline treatment in Alzheimer's disease. 2003
Kálmán J, Juhász A, Rimanóczy A, Palotás A, Palotás M, Szabó Z, Boda K, Márki-Zay J, Janka Z. · Department of Psychiatry, Albert Szent-Györgyi Center for Medical and Pharmaceutical Sciences, Faculty of Medicine, University of Szeged, Semmelweis u.6, H-6725 Szeged, Hungary. · Dement Geriatr Cogn Disord. · Pubmed #12714797 No free full text.
Abstract: The objective of our study was to investigate whether an interaction exists between apolipoprotein E (APOE) genotype and the response of patients with Alzheimer's disease (AD) to selegiline treatment, and whether APOE genotype independently affects the rate of AD progression. A 48-week multicenter double-blind trial was undertaken on 43 patients with mild to moderate AD. Primary efficacy measures were the AD Assessment Scale (ADAS), an 11-item cognitive subscale of ADAS (ADAS-Cog/11) and the Mini Mental State Examination. Secondary outcome measures were Clinical Global Impression of severity and CGI of change scales. The therapeutic response to selegiline was not affected by APOE genotype. Our results revealed that the APOE4 allele carrier AD probands did not respond better to selegiline treatment than the APOE2-3 patients, i.e. APOE status did not influence the therapeutic outcome of selegiline treatment.
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Article Pentapeptide amides interfere with the aggregation of beta-amyloid peptide of Alzheimer's disease. 2002
Hetényi C, Szabó Z, Klement E, Datki Z, Körtvélyesi T, Zarándi M, Penke B. · Department of Medical Chemistry, University of Szeged, Dóm tér 8, Szeged, H-6720, Hungary. · Biochem Biophys Res Commun. · Pubmed #11944904 No free full text.
Abstract: Amyloid peptides (Abeta) play a central role in the pathogenesis of Alzheimer's disease (AD). The aggregation of Abeta molecules leads to fibril and plaque formation. Fibrillogenesis is at the same time a marker and an indirect cause of AD. Inhibition of the aggregation of Abeta could be a realistic therapy for the illness. Beta sheet breakers (BSBs) are one type of fibrillogenesis inhibitors. The first BSB peptides were designed by Tjernberg et al. (1996) and Soto et al. (1998). These pentapeptides have proved their efficiency in vitro and in vivo. In the present study, the effects of two pentapeptide amides are reported. These compounds were designed by using the C-terminal sequence of the amyloid peptide as a template. Biological assays were applied to demonstrate efficiency. Modes of action were studied by FT-IR spectroscopy and molecular modeling methods.
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