| 论文摘要 | 第1-6页 |
| REMERCIEMENTS | 第6-9页 |
| General introduction | 第9-15页 |
| Introduction | 第10-14页 |
| Ⅰ.The cholinesterases:acetylcholinesterase and butyrylcholinesterase | 第10-12页 |
| Ⅱ.Cholinesterase-associated structural proteins:ColQ and PRiMA | 第12-13页 |
| Ⅲ.The CutA protein | 第13-14页 |
| Objectives of this thesis | 第14-15页 |
| Chapter Ⅰ:The roles of the catalytic domain and of the C-terminal t peptide in oligomerization of cholinesterases | 第15-51页 |
| Introduction | 第16-23页 |
| Article Ⅰ:Respective roles of catalytic domain and C-terminal t peptides in the oligomerization of acetylcholinesterase and butyrylcholinesterase | 第23-48页 |
| Discussion | 第48-51页 |
| Chapter Ⅱ:A search of binding partners of the C-terminal peptide of PRiMA Ⅰ by two-hybrid strategies | 第51-60页 |
| Introduction | 第52-53页 |
| Two-hybrid system in Saccharomyces cerevisiae | 第53-54页 |
| Two-hybrid system in Escherichia coli | 第54-56页 |
| Procedure of library screening and analysis | 第56-57页 |
| Co-expression of PRiMA Ⅰ and candidate partners in transfected COS cells | 第57-59页 |
| Discussion | 第59-60页 |
| Chapter Ⅲ:Insertion of PRiMA-anchored AChE in membrane rafts:role of the cytoplasmic domains of PRiMA Ⅰ and PRiMA Ⅱ | 第60-88页 |
| Introduction | 第61-62页 |
| Article Ⅱ:Targeting of acetylcholinesterase(AChE) to membrane rafts:a function of proline rich membrane anchor(PRiMA) in neurons | 第62-87页 |
| Conclusion | 第87-88页 |
| Chapter Ⅳ:A study of the CutA protein and its possible interaction with AChE | 第88-142页 |
| Introduction | 第89-90页 |
| Conservation and crystallographic structure of CutA protein | 第90-92页 |
| Isoforms of CutA | 第92页 |
| The subcellular location of the CutA protein is problematic | 第92-96页 |
| Article Ⅲ:The protein CutA undergoes an unusual transfer into the secretory pathway,and affects the folding,oligomerization and secretion of acetylcholinesterase | 第96-136页 |
| Discussion | 第136-142页 |
| The mouse CutA variants | 第136页 |
| The long and short CutA proteins | 第136-137页 |
| Subcellular localization of the long and short CutA proteins:an unusual secretory process | 第137页 |
| N-glycosylation of CutA mutants? | 第137-138页 |
| Post-translational modification of CutA in the ER? | 第138页 |
| The effect of CutA on AChE production | 第138-140页 |
| The full length CutA variant might play a role in the ER environment and in protein folding | 第140页 |
| Is CutA involved in the formation of the PRiMA complex? | 第140页 |
| CutA facilitates the formation of AChE_T tetramers | 第140-142页 |
| Chapter Ⅴ:A review article:Old and new questions about cholinesterases | 第142-159页 |
| Perspectives for future studies | 第159-163页 |
| Bibliography | 第163-172页 |
| Summary | 第172-175页 |
| Résumé | 第175-178页 |
