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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 潘建源(Chien-Yuan Pan) | |
dc.contributor.author | Ai-Chuan Chou | en |
dc.contributor.author | 周愛鵑 | zh_TW |
dc.date.accessioned | 2021-06-08T02:06:15Z | - |
dc.date.copyright | 2016-02-24 | |
dc.date.issued | 2016 | |
dc.date.submitted | 2016-02-03 | |
dc.identifier.citation | References
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Phospholemman regulates cardiac Na+/Ca2+ exchanger by interacting with the exchanger's proximal linker domain. American journal of physiology Cell physiology 296, C911-921. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/19573 | - |
dc.description.abstract | 細胞內鈣離子濃度([Ca2 +] i)的變化是許多生理機制重要的訊息傳導途徑。鈉鈣交換蛋白(Na+/Ca2+ exchangers,NCX)根據胞內外鈉鈣離子的電化學梯度,可控制細胞膜內外鈣離子的進出以維持[Ca2 +]i動態平衡。鈣調素﹙Calmodulin,CaM﹚蛋白感知鈣離子濃度變化並藉與目標蛋白(如通道或是運輸蛋白)結合的方式調控鈣離子信號,但目前尚不清楚鈣調素與NCX1活性之間的相關性。在此篇研究,我們使用鈣調蛋白作為釣餌,與NCX1的兩種異構體的胞內片段(NCX1.1CL和NCX1.3CL)進行GST融合蛋白質免疫沉澱實驗﹙pull-down assay﹚。實驗結果顯示鈣調素在鈣離子存在時,可藉NCX1上的鈣調蛋白結合片段(calmodulin-binding segment,CaMS)與NCX結合。為了確定此結合使否調控NCX1活性,我們利用鈣離子顯影技術(calcium image)偵測[Ca2 +]i變化且同時在HEK 293T細胞內表現NCX1及鈣調素,或是同時表現不同的突變體來確定其中的調控機制。實驗結果顯示缺乏CaMS的NCX1.1及NCX1.3在細胞膜上的表現量及活性都顯著降低,此突變的NCX1.3若同時表現CaM1234則可回復此抑制效果。我們進一步依序點突變CaMS序列中4個重要胺基酸,顯示CaM對NCX1不同異構體有不同的交互機制。點突變第一、二個胺基酸位置會使NCX1.1活性大幅下降,而NCX1.3則是第二、三個位置抑制了NCX的活性。我們的研究結果發表了NCX1被CaM調控的直接證據,也提供了其結合的可能機制。 | zh_TW |
dc.description.abstract | The change in the intracellular Ca2+ concentration ([Ca2+]i) is an important signal for various physiological activities. The Na+/Ca2+ exchangers (NCX) at the plasma membrane transport Ca2+ into or out of the cell according to the electrochemical gradients of Na+ and Ca2+ to modulate the [Ca2+]i homeostasis. Calmodulin senses [Ca2+]i changes and binds to proteins, such as channels and transporters, to relay Ca2+ signaling. However, it is not clear how calmodulin modulates NCX activity. Using calmodulin as bait, we pulled down the intracellular loops of alternative splicing isoforms of NCX1: NCX1.1 and NCX1.3. This interaction requires both Ca2+ and a putative calmodulin-binding segment (CaMS). To determine whether calmodulin modulates NCX activities, we co-expressed NCX1 isoforms with CaM or CaM1234 (a Ca2+-binding deficient mutant) in 293T cells and measured the increase in [Ca2+]i caused by the influx of Ca2+ through NCX. Deleting the CaMS from NCX1.1 and NCX1.3 attenuated exchange activities and decreased localization to the plasma membrane. Removing the mutually exclusive exons from NCX1.3 reduced exchange activity, which could be rescued by CaM1234 co-expression. Point-mutations at any of the 4 conservative a.a. residues in the CaMS had differential effects in NCX1.1 and NCX1.3. Mutating the first two conservative a.a. in NCX1.1 decreased the exchange activity. In contrast, mutating the 2nd and 3rd conservative a.a. in NCX1.3 decreased the exchange activity. Taken together, our results demonstrate that calmodulin senses changes in [Ca2+]i and binds to the cytoplasmic loop of NCX to regulate exchange activity and Ca2+ homeostasis. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T02:06:15Z (GMT). No. of bitstreams: 1 ntu-105-F96b41030-1.pdf: 4298134 bytes, checksum: 6783e2b6a43138512ff1b6f44f10d612 (MD5) Previous issue date: 2016 | en |
dc.description.tableofcontents | Contents
口試委員審定書 i 中文摘要 v Abstract vii Contents ix Part I 鈣調素對鈉鈣交換蛋白之生理調控機制 Roles of Calmodulin in Regulating the Sodium/Calcium Exchanger 1 Introduction 3 The Na+-Ca2+ Exchanger Molecule 3 The Exchanger Superfamily 3 Isoforms, Expression, and Function of NCX1 5 NCX-related Diseases 8 Physiological Relevance: The Heart and Kidney 8 Neuroprotection 10 Ca2+ Regulation 12 Calcium Homeostasis 12 Ca2+ Regulation of NCX: Structural Basis for Ca2+ Regulation in NCX 12 Potential Mechanism 13 Protein-Protein Interaction 13 Calmodulin 14 Materials and Methods 17 Chemicals 17 Plasmid Preparation 17 Transfection of HEK 293T Cells 19 Calcium Imaging 19 Immunostaining 20 Protein Extraction 21 GST Pull-Down Assay 22 Data Analysis 22 Results 23 Putative CaM binding segment in the NCX1 cytoplasmic loop 23 CaM interacts with the NCX1 cytoplasmic loop 24 CaMS deletion affects membrane localization 25 CaMS deletion decreases exchange activity 27 Exons A and B are involved in CaM-mediated regulation 28 Mutating the conserved a.a. in the CaMS of NCX1.1 affects exchange activity 30 Mutating the middle 2 conserved a.a. in the CaMS of NCX1.3 reduces exchange activity 31 Intracellular Ca2+ signaling and NCX1 32 Discussion 35 Schemes 44 Scheme 1. Schematic illustration of CaCA superfamily 45 Scheme 2. Description of the constructs used in this study 47 Tables 48 Table 1. Sequence alignment of human and bovine 48 Table 2. Gene comparison between human and bovine 49 Figures 50 Fig. 1. Molecular biology of NCX1 51 Fig. 2. Immunostaining of NCX1.1 and NCX1.3 in non-permeabilized cells 52 Fig. 3. Immunostaining of NCX1 and NCX1CL 53 Fig. 4. CaM interacts with the NCX1 cytosolic loop 55 Fig. 5. The colocalization analysis of NCX1 and F-actin 57 Fig. 6. The CaMS affects the membrane localization of NCX1 splice variants 59 Fig. 7. Permeable staining of NCX1 and GFP-GPI coexpressed cell 61 Fig. 8. Deletion of the CaMS reduces exchange activity 63 Fig. 9. CaM attenuates the NCKX4 activities 65 Fig. 10. Deletion of exon A/B attenuates exchange activity 67 Fig. 11. Each of the conserved a.a. residues in the NCX1.1 CaMS has differential effects on exchange activity 69 Fig. 12. Mutations in the conserved a.a. residues of the NCX1.3 CaMS affect exchange activity 71 Fig. 13. Distribution of NCX1 mutants at the cell membrane 73 Fig. 14. EGFP-a1BCT could not rescue the CaM-mediated inhibition on NCX1.1L14D 75 Fig. 15. Depletion of internal Ca2+ stores affect CaM-mediated regulation of NCX1 in HEK 293T 77 Fig. 16. Hypothetical CaM-mediated regulation of NCX exchange activity 78 Acknowledgments 79 Abbreviations 80 Part II 利用上轉換奈米粒子以近紅外線控制光敏通道的活性 Near-Infrared Optogenetics: A Novel Design for Controlling the Channelrhodopsin-2 Activity with Cell Targeted Upconverting Nanoparticles 83 中文摘要 85 Abstract 87 Introduction 89 Optogenetics 89 Proteins of Optogenetics 90 Upconversion Nanoparticles (UCNPs) 91 Aims 95 Materials and Methods 97 Chemicals 97 Synthesis of Oleate Capped 97 Synthesis of Silica Coated UCNPs (Silica/UCNPs) 98 Synthesis of APTES Conjugated UCNPs (NH2/UCNPs) 99 Synthesis of NeutrAvidin Conjugated UCNP (NA/UCNP) 100 Constructs and Molecular Biology 100 Cell Culture and Transfection 101 Protein Extraction 102 Dot-Immunobinding Assay (Dot-Assay) 102 Pull-Down Assay 103 Immunostaining 103 NeutrAvidin Functionalized UCNP Targeting Experiment in Live Cell 104 Electrophysiological Measurements 104 Data Analysis 105 Results 107 Synthesis and quantification of UCNPs 107 Antibody-Antigen Reactions contribute to specificity of UCNPs 109 Fluorescence resonance energy transfer between UCNPs and LumioTM 110 VL-modification does not affect ChR2m localization 112 NAV/UCNPs recognized VL-ChR2m cells in live-cell experiments 112 ChR2-expressing cells exhibit excitatory activation upon NIR-light stimulation 113 Discussion 115 Conclusion 123 Scheme 124 Scheme 1. The Schematic illustrations of VL-ChR2m 125 Figures 126 Fig. 1. Schematic illustrations of the experimental design 127 Fig. 2. Physical properties of the synthesized UCNPs 128 Fig. 3. TEM image of silica coated UCNPs 129 Fig. 4. Ninhydrin assay for amine group modification 130 Fig. 5. Antibody modification of UCNPs 131 Fig. 6. The Zeta potential of modified UCNPs 132 Fig. 7. Titration experiment of dot-assay 133 Fig. 8. Dot-assay of the binding of antibody-modified UCNP to the target protein 135 Fig. 9. Confocal images of pull down assay samples 136 Fig. 10. Interaction between UCNP and fluorophores on target proteins 137 Fig. 11. Membrane localization of VL-ChR2m on cell membrane 139 Fig. 12. Specific binding of UCNPs to the VL-ChR2m 141 Fig. 13. Non-specific binding of UCNPs without PEG coating to the cell membrane 143 Fig. 14. NIR illumination induce an inward current from cells bound with UCNPs 145 Acknowledgments 147 Abbreviations 148 References 151 | |
dc.language.iso | en | |
dc.title | 鈣調素對鈉鈣交換蛋白之生理調控機制 | zh_TW |
dc.title | Roles of Calmodulin in Regulating the Sodium/Calcium Exchanger | en |
dc.type | Thesis | |
dc.date.schoolyear | 104-1 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 閔明源(Ming-Yuan Min),陳逸聰(Yit-Tsong Chen),朱有田(Yu-Ten Ju),李賢明(Hsien-Ming Lee),高閬仙(Lung-Sen Kao) | |
dc.subject.keyword | 1-5-8-14 motif,鈣離子恆定,調鈣素,反向模式,鈉鈣交換蛋白,交換蛋白抑制?, | zh_TW |
dc.subject.keyword | 1-5-8-14 motif,Ca2+ homeostasis,calmodulin,reverse mode,Na+/Ca2+ exchanger,XIP, | en |
dc.relation.page | 165 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2016-02-03 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 生命科學系 | zh_TW |
顯示於系所單位: | 生命科學系 |
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