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The effect of neurosin on amyloid precursor protein processing.

Leung Man-hin. / Thesis submitted in: August 2004. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2005. / Includes bibliographical references (leaves 119-133). / Abstracts in English and Chinese. / Abstract --- p.ii / Acknowledgement --- p.iv / Abbreviations --- p.v / Figure List --- p.vii / Chapter Chapter 1: --- General introduction / Chapter 1.1 --- Introduction --- p.1 / Chapter 1.2 --- Pathogenesis of Alzheimer's disease / Chapter 1.2.1 --- Amyloid cascade hypothesis --- p.2 / Chapter 1.2.2 --- Tauopathy --- p.5 / Chapter 1.3 --- The amyloid precursor proteins / Chapter 1.3.1 --- Structure of amyloid precursor proteins and related peptides --- p.5 / Chapter 1.3.2 --- Amyloid precursor protein mutations --- p.6 / Chapter 1.3.3 --- Amyloid precursor protein processing --- p.10 / Chapter 1.3.4 --- Physiological roles of APP --- p.12 / Chapter 1.3.5 --- The pathophysiological role of Ap --- p.17 / Chapter 1.3.6 --- The pathophysiological role of APP-CTF --- p.20 / Chapter 1.4 --- The role of proteases in amyloid precursor protein processing / Chapter 1.4.1 --- α-secretase and p-secretase --- p.22 / Chapter 1.4.2 --- γ-secretase complex --- p.30 / Chapter 1.4.3 --- Caspases --- p.36 / Chapter 1.4.4 --- Kallikrein-like proteases --- p.37 / Chapter 1.5 --- Objective of the present study --- p.40 / Chapter Chapter 2: --- Materials and methods / Chapter 2.1 --- Experimental procedure / Chapter 2.1.1 --- Plasmid construction --- p.42 / Chapter 2.1.2 --- "DNA purification, ligation and restriction enzyme digestion" --- p.44 / Chapter 2.1.3 --- Competent cell preparation --- p.47 / Chapter 2.1.4 --- Transformation --- p.47 / Chapter 2.1.5 --- Plasmid miniprep --- p.48 / Chapter 2.1.6 --- Prokaryotic expression of neurosin --- p.49 / Chapter 2.1.7 --- SDS-PAGE --- p.51 / Chapter 2.1.8 --- Protein sample preparation --- p.51 / Chapter 2.1.9 --- Western Blot --- p.52 / Chapter 2.1.10 --- Immobilized metal affinity chromatography --- p.54 / Chapter 2.1.11 --- Enzyme assay --- p.55 / Chapter 2.1.12 --- Cell culture and transfection --- p.56 / Chapter 2.1.13 --- Live cell imaging --- p.57 / Chapter 2.2 --- Materials --- p.59 / Chapter Chapter 3 : --- Results / Chapter 3.1 --- Recombinant expression and characterization of neurosin / Chapter 3.1.1 --- Construction of neurosin prokaryotic expression vectors --- p.62 / Chapter 3.1.2 --- Prokaryotic expression of neurosin --- p.64 / Chapter 3.1.3 --- Neurosin was expressed as inclusion bodies --- p.68 / Chapter 3.1.4 --- Co-expression of molecular chaperones with neurosin --- p.70 / Chapter 3.1.5 --- Purification of recombinant neurosin by IMAC --- p.76 / Chapter 3.1.6 --- Enzyme assay --- p.81 / Chapter 3.2 --- Effect of neurosin on APP processing in neuronal cells / Chapter 3.2.1 --- Generation of APP constructs --- p.84 / Chapter 3.2.2 --- Expression of APP in mammalian cultures --- p.89 / Chapter 3.2.3 --- Cellular localization of APP and its processing products --- p.96 / Chapter 3.2.4 --- The role of over-expression of neurosin on APP processing in B103 cells --- p.101 / Chapter Chapter 4: --- Discussion / Chapter 4.1 --- Discussion of neurosin expression --- p.103 / Chapter 4.2 --- Discussion of APP cell model --- p.109 / Chapter 4.3 --- Conclusion --- p.119 / References --- p.121 / Appendix / Chapter A. --- Tables on primers used --- p.138 / Chapter B. --- Plasmid maps --- p.139 / Chapter C. --- Raw data on the DNA sequencing --- p.141

Identiferoai:union.ndltd.org:cuhk.edu.hk/oai:cuhk-dr:cuhk_325342
Date January 2005
ContributorsLeung, Man-hin., Chinese University of Hong Kong Graduate School. Division of Biochemistry.
Source SetsThe Chinese University of Hong Kong
LanguageEnglish, Chinese
Detected LanguageEnglish
TypeText, bibliography
Formatprint, x, 141 leaves : ill. (some col.) ; 30 cm.
RightsUse of this resource is governed by the terms and conditions of the Creative Commons “Attribution-NonCommercial-NoDerivatives 4.0 International” License (http://creativecommons.org/licenses/by-nc-nd/4.0/)

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