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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 許弘明(Hong-Ming Hsu) | |
| dc.contributor.author | Jing-Yang Chang | en |
| dc.contributor.author | 張景翔 | zh_TW |
| dc.date.accessioned | 2022-11-24T03:17:15Z | - |
| dc.date.available | 2021-11-05 | |
| dc.date.available | 2022-11-24T03:17:15Z | - |
| dc.date.copyright | 2021-11-05 | |
| dc.date.issued | 2021 | |
| dc.date.submitted | 2021-10-05 | |
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Janota CS, Calero-Cuenca FJ, Gomes ER. The role of the cell nucleus in mechanotransduction. Curr Opin Cell Biol. 2020 Apr;63:204-11. 26. Pollard TD, Goldman RD. Overview of the Cytoskeleton from an Evolutionary Perspective. Cold Spring Harb Perspect Biol. 2018 Jul 2;10(7):a030288. 27. Eriksson JE, Opal P, Goldman RD. Intermediate filament dynamics. Curr Opin Cell Biol. 1992 Feb;4(1):99-104. 28. Goodson HV, Jonasson EM. Microtubules and Microtubule-Associated Proteins. Cold Spring Harb Perspect Biol. 2018 Jun 1;10(6):a022608. 29. Dominguez R, Holmes KC. Actin structure and function. Annu Rev Biophys. 2011;40:169-86. 30. Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC. The evolution of compositionally and functionally distinct actin filaments. J Cell Sci. 2015 Jun 1;128(11):2009-19. 31. DesMarais V, Macaluso F, Condeelis J, Bailly M. Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension. J Cell Sci. 2004 Jul 15;117(Pt 16):3499-510. 32. Pizarro-Cerdá J, Chorev DS, Geiger B, Cossart P. The Diverse Family of Arp2/3 Complexes. Trends Cell Biol. 2017 Feb;27(2):93-100. 33. Gungabissoon RA, Bamburg JR. Regulation of growth cone actin dynamics by ADF/cofilin. J Histochem Cytochem. 2003 Apr;51(4):411-20. 34. Brugerolle G, Bricheux G, Coffe G. Actin cytoskeleton demonstration in Trichomonas vaginalis and in other trichomonads. Biol Cell. 1996;88(1-2):29-36. 35. Kusdian G, Woehle C, Martin WF, Gould SB. The actin-based machinery of Trichomonas vaginalis mediates flagellate-amoeboid transition and migration across host tissue. Cell Microbiol. 2013 Oct;15(10):1707-21. 36. Bricheux G, Coffe G, Pradel N, Brugerolle G. Evidence for an uncommon alpha-actinin protein in Trichomonas vaginalis. Mol Biochem Parasitol. 1998 Sep 15;95(2):241-9. 37. Agarwal S, Anand G, Sharma S, Parimita Rath P, Gourinath S, Bhattacharya A. EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica. PLoS Pathog. 2019 May 16;15(5):e1007789. 38. Maun NA, Speicher DW, DiNubile MJ, Southwick FS. Purification and properties of a Ca(2+)-independent barbed-end actin filament capping protein, CapZ, from human polymorphonuclear leukocytes. Biochemistry. 1996 Mar 19;35(11):3518-24. 39. Yamashita A, Maeda K, Maéda Y. Crystal structure of CapZ: structural basis for actin filament barbed end capping. EMBO J. 2003 Apr 1;22(7):1529-38. 40. Takeda S, Minakata S, Koike R, Kawahata I, Narita A, Kitazawa M, Ota M, Yamakuni T, Maéda Y, Nitanai Y. Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition. PLoS Biol. 2010 Jul 6;8(7):e1000416. 41. Wear MA, Cooper JA. Capping protein binding to S100B: implications for the tentacle model for capping the actin filament barbed end. J Biol Chem. 2004 Apr 2;279(14):14382-90. 42. Wear MA, Yamashita A, Kim K, Maéda Y, Cooper JA. How capping protein binds the barbed end of the actin filament. Curr Biol. 2003 Sep 2;13(17):1531-7. 43. Kilby PM, Van Eldik LJ, Roberts GC. Identification of the binding site on S100B protein for the actin capping protein CapZ. Protein Sci. 1997 Dec;6(12):2494-503. 44. Edwards M, Zwolak A, Schafer DA, Sept D, Dominguez R, Cooper JA. Capping protein regulators fine-tune actin assembly dynamics. Nat Rev Mol Cell Biol. 2014 Oct;15(10):677-89. 45. Stark BC, Lanier MH, Cooper JA. CARMIL family proteins as multidomain regulators of actin-based motility. Mol Biol Cell. 2017 Jul 1;28(13):1713-23. 46. Canton DA, Olsten ME, Kim K, Doherty-Kirby A, Lajoie G, Cooper JA, Litchfield DW. The pleckstrin homology domain-containing protein CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein. Mol Cell Biol. 2005 May;25(9):3519-34. 47. The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein. J Biol Chem. 2006 Nov 24;281(47):36347-59. 48. Kai-Hsuan Wang. The functional study of an F-actin capping protein in the protozoan parasite, Trichomonas vaginalis. Graduate Institute of Microbiology College of Medicine National Taiwan University Master Thesis. 2019;10.6342/NTU201903329 49. Tsai CD, Liu HW, Tai JH. Characterization of an iron-responsive promoter in the protozoan pathogen Trichomonas vaginalis. J Biol Chem. 2002 Feb 15;277(7):5153-62. 50. Ryu JS, Choi HK, Min DY, Ha SE, Ahn MH. Effect of iron on the virulence of Trichomonas vaginalis. J Parasitol. 2001 Apr;87(2):457-60. 51. Katanaev VL, Wymann MP. Microquantification of cellular and in vitro F-actin by rhodamine phalloidin fluorescence enhancement. Anal Biochem. 1998 Nov 15;264(2):185-90. 52. Skillman KM, Diraviyam K, Khan A, Tang K, Sept D, Sibley LD. Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites. PLoS Pathog. 2011 Oct;7(10):e1002280. 53. Friederich E, Vancompernolle K, Louvard D, Vandekerckhove J. Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro. J Biol Chem. 1999 Sep 17;274(38):26751-60. 54. Yokota E, Tominaga M, Mabuchi I, Tsuji Y, Staiger CJ, Oiwa K, Shimmen T. Plant villin, lily P-135-ABP, possesses G-actin binding activity and accelerates the polymerization and depolymerization of actin in a Ca2+-sensitive manner. Plant Cell Physiol. 2005 Oct;46(10):1690-703. 55. Khurana S, George SP. Regulation of cell structure and function by actin-binding proteins: villin's perspective. FEBS Lett. 2008 Jun 18;582(14):2128-39. 56. Bhattacharya N, Ghosh S, Sept D, Cooper JA. Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. J Biol Chem. 2006 Oct 13;281(41):31021-30. 57. Pinna LA. Protein kinase CK2: a challenge to canons. J Cell Sci. 2002 Oct 15;115(Pt 20):3873-8. 58. Meggio F, Pinna LA. One-thousand-and-one substrates of protein kinase CK2? FASEB J. 2003 Mar;17(3):349-68. 59. Zhao X, Jiang M, Wang Z. TPM4 promotes cell migration by modulating F-actin formation in lung cancer. Onco Targets Ther. 2019 May 31;12:4055-4063. 60. Zhao K, Wang D, Zhao X, Wang C, Gao Y, Liu K, Wang F, Wu X, Wang X, Sun L, Zang J, Mei Y. WDR63 inhibits Arp2/3-dependent actin polymerization and mediates the function of p53 in suppressing metastasis. EMBO Rep. 2020 Apr 3;21(4):e49269. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/80806 | - |
| dc.description.abstract | "陰道滴蟲感染引起的陰道滴蟲症是最常見的非病毒源性傳染疾病之一，與上皮細胞貼附是其感染宿主的關鍵。在高等真核細胞中，肌動蛋白 (α-Actin) 主導的細胞骨架重組，可以調控細胞型態的轉變，例如利用偽足來進行胞吞作用、貼附爬行等等，而這些相關機制在陰道滴蟲中尚未被深入的探討。根據實驗室前人的發現，陰道滴蟲細胞中肌動加帽蛋白 (F-actin capping protein, TvFACP) 可能藉由抑制肌動蛋白聚合成束，進而造成陰道滴蟲細胞轉型與貼附能力受阻。在本研究中，目標再進一步分析TvFACP蛋白上潛在的肌動蛋白結合觸手 (tentacle) 與酪蛋白激酶 (Casein kinase II) 磷酸化調控位點功能。研究結果顯示，TvFACP蛋白質C端 (237-261胺基酸) 區域刪除，在免疫沉澱實驗中大幅降低與肌動蛋白的結合；若將此蛋白過量表現於陰道滴蟲中，則會降低抑制肌動蛋白重組的能力。而TvFACP蛋白質Ser2與Ser4進行點突變後，在免疫沉澱實驗中仍與肌動蛋白維持高度的結合；將此蛋白過量表現於陰道滴蟲時，卻同樣降低抑制肌動蛋白的重組能力。後續利用固相結合酵素鏈結免疫吸附與共沉降試驗分析，推測TvFACP可同時結合F-actin與G-actin共同調控F-actin聚合。最後以細胞遷移試驗，發現TvFACP過量表現使陰道滴蟲移動能力上升。表示TvFACP藉由結合α-Actin調控細胞骨架重組，影響陰道滴蟲變形與貼附能力。" | zh_TW |
| dc.description.provenance | Made available in DSpace on 2022-11-24T03:17:15Z (GMT). No. of bitstreams: 1 U0001-0510202117144100.pdf: 4163268 bytes, checksum: d2b2f715ef55cf6967ac17ad8c046fbf (MD5) Previous issue date: 2021 | en |
| dc.description.tableofcontents | "目錄 口試委員審定書 i 誌謝 ii 摘要 iii Abstract iv 第一章 前言 1 第一節、陰道滴蟲簡介 1 第二節、陰道滴蟲型態 1 第三節、陰道滴蟲致病機轉 2 第四節、細胞骨架與變形能力 2 第五節、陰道滴蟲肌動蛋白系統 3 第六節、肌動加帽蛋白之調控 4 第七節、陰道滴蟲肌動加帽蛋白探討 5 第八節、研究目的 5 第二章 材料與方法 6 第一節、陰道滴蟲培養 6 第二節、陰道滴蟲保存與活化 6 第三節、質體轉染 6 第四節、重組蛋白pET28a-TvFACP純化 7 第五節、免疫螢光染色 (Immunofluorescence , IFA) 8 第六節、細胞分萃試驗 (Fractionation) 8 第七節、免疫沉澱法 (Immunoprecipitation, IP) 9 第八節、西方墨點法 (Western blot) 10 第九節、重組蛋白GST-actin純化 11 第十節、GST沉降試驗 (GST pull down) 11 第十一節、固相酶聯免疫吸附試驗 (Solid-phase plate binding) 12 第十二節、共沉澱試驗 (Co-sedimentation) 12 第十三節、細胞遷移試驗 (Transwell) 13 第三章 結果 14 第一節、陰道滴蟲anti-sense系統測試 14 第二節、陰道滴蟲序列分析 14 第三節、重組蛋白His-TvFACP與GST-actin放大純化 15 第四節、各組TvFACP與α-Actin親和力差異 15 第五節、HA-TvFACP 轉染組與蟲株內α-Actin親和力差異 16 第六節、TvFACP △237對F-actin表現量影響 16 第七節、TvFACP S2AS4A對F-actin表現量影響 17 第八節、TvFACP對G-actin與F-actin結合能力 17 第九節、陰道滴蟲各HA-TvFACP 轉染組細胞遷移 18 第四章 討論 19 第一節、陰道滴蟲F-actin表現觀察 19 第二節、FACP功能探討 19 第三節、TvFACP的α-Actin結合區域 20 第四節、TvFACP的CKII鄰酸化位點 20 第五節、TvFACP對陰道滴蟲遷移能力的影響 21 第六節、目前TvFACP於陰道滴蟲內調控機制 21 附錄 53 附錄一、TYI-S33培養液 53 附錄二、本研究使用之DNA引子 54 附錄三、本研究使用之抗體 55 附錄四、本研究使用之蛋白酶抑制劑 58 附錄五、G-buffer與F-buffer 59 附錄六、陰道滴蟲TvFACP兩個α subunit胺基酸序列比對 60 參考資料 61 附圖目錄 圖一、陰道滴蟲anti-sense系統測試 24 圖二、陰道滴蟲TvActin與TvFACP胺基酸序列分析 26 圖三、重組蛋白His-TvFACP與GST-actin放大純化 29 圖四、重組蛋白His-TvFACP與GST-actin的親和力 (in vitro) 31 圖五、陰道滴蟲轉染──HA-TvFACP △237與S2AS4A 33 圖六、陰道滴蟲T1轉染組與蟲株內Actin親和力差異 35 圖七、陰道滴蟲TH17轉染組與蟲株內Actin親和力差異 37 圖八、過量表現HA-TvFACP △237對F-actin表現量影響 39 圖九、過量表現HA-TvFACP S2AS4A對F-actin表現量影響 41 圖十、G-actin與F-actin收集 43 圖十一、His-TvFACP對G-actin與F-actin結合能力 45 圖十二、TvFACP對F-actin結合能力 47 圖十三、陰道滴蟲各HA-TvFACP 轉染組細胞遷移 50 圖十四、推測TvFACP △237與S2AS4A對陰道滴蟲F-actin聚合能力影響 52" | |
| dc.language.iso | zh-TW | |
| dc.subject | 陰道滴蟲 | zh_TW |
| dc.subject | 肌動蛋白結合觸手 | zh_TW |
| dc.subject | 肌動加帽蛋白 | zh_TW |
| dc.subject | 肌動蛋白 | zh_TW |
| dc.subject | 酪蛋白激酶磷酸化調控 | zh_TW |
| dc.subject | F-actin capping protein | en |
| dc.subject | α-actin-binding domain | en |
| dc.subject | Trichomonas vaginalis | en |
| dc.subject | F-actin assembly | en |
| dc.subject | CKII phosphorylation sites | en |
| dc.title | 陰道滴蟲中肌動加帽蛋白之功能區域分析 | zh_TW |
| dc.title | The functional domain analysis for an F-actin capping protein of Trichomonas vaginalis | en |
| dc.date.schoolyear | 109-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 許書豪(Hsin-Tsai Liu),蔡欣祐(Chih-Yang Tseng) | |
| dc.subject.keyword | 陰道滴蟲,肌動蛋白,肌動加帽蛋白,肌動蛋白結合觸手,酪蛋白激酶磷酸化調控, | zh_TW |
| dc.subject.keyword | Trichomonas vaginalis,F-actin assembly,F-actin capping protein,α-actin-binding domain,CKII phosphorylation sites, | en |
| dc.relation.page | 67 | |
| dc.identifier.doi | 10.6342/NTU202103559 | |
| dc.rights.note | 同意授權(限校園內公開) | |
| dc.date.accepted | 2021-10-06 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 微生物學研究所 | zh_TW |
| 顯示於系所單位： | 微生物學科所 | |
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