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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/20353完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 潘建源 | |
| dc.contributor.author | Chih-Hung Chi | en |
| dc.contributor.author | 紀志弘 | zh_TW |
| dc.date.accessioned | 2021-06-08T02:46:02Z | - |
| dc.date.copyright | 2018-01-04 | |
| dc.date.issued | 2017 | |
| dc.date.submitted | 2017-10-17 | |
| dc.identifier.citation | Abele, K., and Yang, J. (2012). Regulation of voltage-gated calcium channels by proteolysis. Sheng Li Xue Bao 64, 504-514.
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/20353 | - |
| dc.description.abstract | 細胞內鈣離子的提升能活化細胞內各種生理作用，其主要來源是透過細胞外鈣離子通過細胞膜上的電壓依賴型鈣離子通道進入細胞內。此鈣離子依賴型不活化已知與調鈣素偵測鈣離子濃度有關。調鈣素如何調節電壓依賴型鈣離子通道CaV2.2仍保有未知，因此我們在胚胎腎臟皮質細胞中表現CaV2.2與調鈣素或其突變型並記錄其電流來探討此鈣離子依賴不活化現象。結果顯示CaV2.2在鈣離子溶液中能快速的不活化，但是並不存在於鋇離子為溶液時。當與缺乏鈣離子結合能力的調鈣素突變型共同表現時，此鈣離子依賴型不活化效果隨之減小。利用谷胱甘肽轉移酶標記之調鈣素或突變型為餌，我們發現在不論鈣離子有無的情況下，調鈣素能和胞內的電壓依賴型鈣離子通道之C端交互作用。然而，當此突變CaV2.2上，已知與調鈣素接合的高保留性氨基酸的片段時，調鈣素或型無法失去與之交互作用。調鈣素接合位置的突變導致此CaV2.2的的電流減小但能被調鈣素Ｎ端突變型拯救。然而，我們發現N-端突變型的調鈣素可以增加CaV2.2的的總體表現量，卻不會增加細胞膜上的表現比例。總的來看，我們的結果認為調鈣素不只能調節CaV2.2的不活化；同時，藉由調控其表現量，已達控制細胞內鈣離子濃度對生理活動的影響。
實驗室之前的研究發現與調鈣素結構類似的鈣離子結合蛋白，Calneuron 1 (Caln1)，能夠抑制腎上腺髓質嗜鉻細胞上的電壓依賴型鈣離子電流。此外，酵母菌雙雜交實驗中發現，Caln1在能與Scyl1交互作用。本篇研究發現，Caln1能夠抑制表現於胚胎腎臟細胞中的電壓依賴型鈣離子通道CaV1.3、CaV2.2、CaV3.1以及電壓依賴型鈉離子通道NaV1.4之電流。此外，若將Caln1表現於初級培養之胚胎大腦皮質神經細胞中，由鈣離子影像實驗與動作電位紀錄發現，Caln1同樣能導致神經細胞活性受到抑制。此外，Caln1的表現並不會影響到CaV2.2的總體蛋白質表現量，卻能增加其在細胞膜上的表現量，而且在體外培養14日之初級培養的大腦皮質神經細胞中，Caln1的表現可以透過化學誘導之長期增強作用下被增強表現。然而，透過免疫沈澱試驗發現，Caln1並沒有辦法與CaV2.2或CaV3.1直接作用。前人研究發現，Caln1與Scyl1都會參與細胞內小泡的運輸，且分別影響由高基氏體到細胞膜上的運輸以及內質網到高基氏體的運輸過程。綜合之前的研究，此篇研究發現，Scyl1與Caln1皆能抑制CaV2.2之鈣離子電流，且共同表現於胚胎腎臟細胞中時，具有協同作用，使鈣離子電流完全被抑制。此外，也透過免疫染色實驗發現，Caln1與Scyl1能同時座落在細胞內部形成小泡狀構造，猜測此一構造是在高基氏體上。當同時將Caln1上激素相似構造與自體聚集構造突變時，Caln1與Scyl1共同表現時造成的小泡堆積結構便不存在。因此，Caln1對於調節細胞內電壓依賴型通道的運輸與電流控制進而影響神經細胞活性皆扮演重要的角色。然而，Caln1在電壓依賴型通道的運輸與電流調控上之關係仍需要更多的研究與發現。 | zh_TW |
| dc.description.abstract | The Ca2+ influx through the voltage-gated Ca2+ channels (CaVs) at the plasma membrane is the major extracellular factor responsible for the elevation in intracellular Ca2+ concentration ([Ca2+]i), which activates various physiological activities. The inactivation phase of CaVs determines the amount of Ca2+ that enters the cell, and calmodulin (CaM) is known to be involved in the Ca2+-dependent inactivation process. However, how CaM modulates CaV2.2 is still unclear. Here, we expressed CaV2.2 with CaM or CaM mutants in HEK293T cells and measured the currents to characterize the inactivation. The results showed that CaV2.2 had a fast inactivation with Ca2+, but not Ba2+, as the charge carrier; when it was co-expressed with CaM mutants with a Ca2+-binding deficiency, the levels of inactivation decreased. Using GST-tagged CaM or CaM mutants as the bait, we found that CaM could interact with the intracellular C-terminal fragment of CaV2.2 in the presence or absence of Ca2+. However, CaM and its mutants could not interact with this fragment when mutations were generated in the conserved amino acid residues of the CaM-binding site. The mutations in the CaM-binding site greatly reduced the current of CaV2.2 but could be rescued by CaM12 (Ca2+-binding deficiency at the N-lobe) overexpression; in addition, CaM12 enhanced the total expression level of CaV2.2, but the ratios between the membrane and total fractions remained unchanged. Together, our data suggest that CaM not only modulates the inactivation of CaV2.2 but also regulates its expression to control [Ca2+]i elevation for physiological activities.
Previous studies in our lab showed that calneuron 1 (Caln1), a Ca2+ binding protein with structure similar to CaM, inhibits the inward current of CaVs in chromaffin cells and interacts with Scyl1 verified by yeast-2-hybrid. Here we showed Caln1 inhibited the inward currents of CaV1.3, 2.2, 3.1, and NaV1.4 expressed in HEK293T cells, also, its overexpression suppressed neuronal activities in primary cultured cortical neurons. Caln1 did not directly interact with CaV2.2 and CaV3.1, however, the chemical LTP decreased the presence of channel proteins on the plasma membrane. Caln1 also can be upregulated in primary cortical neuron. Both Caln1 and Scyl1 has been reported to regulate the vesicle tracking from Golgi to plasma membrane and ER to Golgi, respectively. Here, the patch clamping results showed that Scyl1 inhibited the currents of CaV2.2 with Caln1. In the immunostaining experiment, Scyl1 and Caln1 colocalized and accumulated at the intracellular vesicles, considered to be the Golgi apparatus, however, Scyl1ΔKLHT, lacking kinase function and self-associated manner, eliminated this appearance. Therefore, Caln1 is important in the trafficking of CaV2.2 and inward current regulation of VGICs (voltage-gated ion channels), however, the correlation between trafficking and modulation of VGICs in controlling neuronal activities still remains the open questions. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-08T02:46:02Z (GMT). No. of bitstreams: 1 ntu-106-F97B41032-1.pdf: 22820699 bytes, checksum: 799d069a4d1a48a7ba7b49713350ece6 (MD5) Previous issue date: 2017 | en |
| dc.description.tableofcontents | 口試委員會審定書 #
誌謝 i 中文摘要 ii ABSTRACT iv CONTENTS vi Chapter 1 Introduction 1 1.1 Voltage-gated calcium channels (CaVs) 1 1.2 Calcium binding proteins (CaBPs) 3 1.3 Calmodulin (CaM) 3 1.4 The CDI correlated disease and therapies 7 1.5 Calneuron 1 8 1.6 Scyl-like 1 9 1.7 Calcium signaling and synaptic transmission 11 Chapter 2 Aims 13 2.1 To verify the CDI of CaV2.2 13 2.2 To characterize the role of CaM in CDI of CaV2.2 13 2.3 To investigate the interaction between CaV2.2 IQ-motif and CaM 13 2.4 To characterize the direct interaction between CaV2.2 and CaM 13 2.5 To verify the CaV2.2 expression through CaM modulation 13 2.6 To verify the Caln1 modulate CaVs in HEK293T 13 2.7 To verify the Caln1 modulate NaV1.4 in HEK293T 13 2.8 To identify Caln1 regulate CaV2.2 membrane trafficking 13 2.9 To characterize the effects of Caln1 in cortical neuron 13 2.10 To investigate the localization between Caln1 and Scyl1 13 2.11 To verify the effect of Scyl1 on CaV2.2 13 Chapter 3 Materials and Methods 14 3.1 Chemicals 14 3.2 Solution/ Buffer 16 3.3 Cell preparation 18 3.4 Plasmid preparation 19 3.5 List of primers 20 3.6 Mutagenesis 21 3.7 Transfection of HEK293T cells 22 3.8 Protein preparation 22 3.9 GST pulldown assays 22 3.10 Immunoprecipitation 23 3.11 Biotinylation 23 3.12 Western blot 24 3.13 Immunocytochemistry 24 3.14 Electrophysiological recording 24 3.15 Calcium imaging 25 3.16 Chem-LTP 26 3.17 RNA extraction and cDNA synthesis 26 3.18 Statistical analysis 28 Chapter 4 Results 29 4.1 Bovine CaV2.2 shows Ca2+-dependent inactivation 29 4.2 Both lobes of CaM modulate the CDI effect 29 4.3 Mutating the IF residues reduces the current amplitude 30 4.4 The IF amino acid residues are important for current inactivation 31 4.5 CaM12 enhances the attenuated current density 31 4.6 CaM mutants affect differential binding to the C-terminal fragment of CaV2.2 32 4.7 CaM12 enhances the expression level of CaV2.2 33 4.8 Caln1 colocalizes to CaV2.2 in HEK293T 33 4.9 Caln1 inhibits the currents of CaVs expressed in HEK293T 34 4.10 Caln1 decreases the current of NaV1.4 in HEK293T cells 36 4.11 Caln1 increases the localization of CaV2.2 but not Caln1DE2AQ and Caln1ΔHT 36 4.12 Caln1 does not interact with CaV2.2-CT 37 4.13 Caln1 regulated CaV3.1 not through directly binding. 38 4.14 Caln1 suppresses the action potential and neurotransmission 39 4.15 Chem-LTP induction attenuates the expression of Caln1 40 4.16 Scyl1 exchanges the localization of Caln1 41 4.17 Scyl1 inhibits the current of CaV2.2 with Caln1 41 Chapter 5 Discussion 43 5.1 CaM12 regulates CaV2.2 by enhancing peak current density and ongoing CDI 43 5.2 Caln1 inhibits the current of voltage-gated channels and affects the neuron activities 46 Chapter 6 Conclusion 53 Chapter 7 References 54 Chapter 8 Table 74 Chapter 9 Figures 75 | |
| dc.language.iso | en | |
| dc.title | 調鈣素與Calneuron 1對電壓依賴性離子通道之調控 | zh_TW |
| dc.title | Regulation of Voltage-gated Ion Channels by Calmodulin and Calneuron 1 | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 106-1 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 湯志永,陳建彰,鄭瓊娟,姚季光,周銘翊 | |
| dc.subject.keyword | 電壓依賴型鈣離子通道,電壓依賴型鈉離子通道,調鈣素,鈣離子依賴型不活化,Calneuron 1,Scyl-like 1, | zh_TW |
| dc.subject.keyword | CaV,NaV,Calmodulin,Calcium-dependent inactivation,Calneuron 1,Scyl-like 1, | en |
| dc.relation.page | 125 | |
| dc.identifier.doi | 10.6342/NTU201704249 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2017-10-18 | |
| 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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