α-Synuclein/Amyloid Interactions.

作者: Poul Henning Jensen

DOI: 10.1385/1-59259-142-6:61

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摘要: Human α-synuclein was originally identified as the precursor of a peptide named non-Aβ component Alzheimer's disease (NAC) that tightly associated to purified amyloid (1). Senile plaques consist predominantly 39-42 amino acid residue Aβ arranged in β-pleated sheets. is generated by hydrolysis from transmembrane protein APP. The mechanism which intracellular presynaptic or its NAC fragment becomes integrated extracellular senile still unclear. However, vitro studies have shown and potential participate actively biology since can (1) interact with (2), (2) form fibrils (3), (3) stimulate aggregation (4). also situ (5). techniques described this chapter allow study interactions brain sections peptides solution. Information on following points are found Jensen et al. (5) references therein: Expression purification recombinant human α-synuclein; methodology for performing sodium dodecyl sulfate (SDS) gel electrophoresis fluorography; standard histologic fixing, sectioning, handling tissue.

参考文章(3)
K Uéda, H Fukushima, E Masliah, Y Xia, A Iwai, M Yoshimoto, D A Otero, J Kondo, Y Ihara, T Saitoh, Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease Proceedings of the National Academy of Sciences of the United States of America. ,vol. 90, pp. 11282- 11286 ,(1993) , 10.1073/PNAS.90.23.11282
M. Yoshimoto, A. Iwai, D. Kang, D. A. Otero, Y. Xia, T. Saitoh, NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer disease amyloid, binds A beta and stimulates A beta aggregation Proceedings of the National Academy of Sciences of the United States of America. ,vol. 92, pp. 9141- 9145 ,(1995) , 10.1073/PNAS.92.20.9141