請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/40370
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 黃佩欣 | |
dc.contributor.author | Mu-Shiun Tsai | en |
dc.contributor.author | 蔡牧勳 | zh_TW |
dc.date.accessioned | 2021-06-14T16:45:55Z | - |
dc.date.available | 2011-09-11 | |
dc.date.copyright | 2008-09-11 | |
dc.date.issued | 2008 | |
dc.date.submitted | 2008-07-30 | |
dc.identifier.citation | 1. Iglesias T, Cabrera-Poch N, Mitchell MP, Naven TJ, Rozengurt E, Schiavo G. Identification and cloning of Kidins220, a novel neuronal substrate of protein kinase D. J. Biol. Chem. 2000;275:40048-40056.
2. Kong H, Boulter J, Weber JL, Lai C, Chao MV. An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors. J. Neurosci. 2001;21:176-185. 3. Luo S, Chen Y, Lai KO, et al. α-Syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner. J. Cell. Biol. 2005;169:813-824. 4. Riol-Blanco L, Iglesias T, Sanchez-Sanchez N, et al. The neuronal protein Kidins220 localizes in a raft compartment at the leading edge of motile immature dendritic cells. Eur. J. Immunol. 2004;34:108-118. 5. Liao YH, Hsu SM, Huang PH. ARMS depletion facilitates UV irradiation-induced apoptotic cell death in melanoma. Cancer Res. 2007;67:11547-11556. 6. Chang MS, Arevalo JC, Chao MV. Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning protein. J Neurosci Res. 2004;78(2):186-92. 7. Arevalo JC, Yano H, Teng KK, Chao MV. A unique pathway for sustained neurotrophin signaling through an ankyrin-rich membrane-spanning protein. EMBO J. 2004;23(12):2358-68. 8. Bracale A, Cesca F, Neubrand VE, Newsome TP, Way M, Schiavo G. Kidins220/ARMS Is transported by a Kinesin-1-based mechanism likely to be involved in neuronal differentiation. Mol. Biol. Cell. 2007;18:142-152. 9. 廖怡華•2007•國立台灣大學博士論文 10. Hirokawa N, Takemura R. Kinesin superfamily proteins and their various functions and dynamics. Exp. Cell Res. 2004;301(1):50-9. 11. Lawrence CJ, Dawe RK, Christie KR, et al. A standardized kinesin nomenclature. J. Cell Biol. 2004;167(1):19-22. 12. Miki H, Okada Y, Hirokawa N. Analysis of the kinesin superfamily: insights into structure and function. Trends Cell Biol. 2005;15(9):467-76. 13. Scholey JM. Intraflagellar transport motors in cilia: moving along the cell's antenna. J. Cell Biol. 2008;180(1):23-9. 14. Takeda S, Yonekawa Y, Tanaka Y, Okada Y, Nonaka S, Hirokawa N. Left-right asymmetry and kinesin superfamily protein KIF3A: new insights in determination of laterality and mesoderm induction by kif3A-/- mice analysis. J. Cell. Biol. 1999;145:825-836. 15. Lin F, Hiesberger T, Cordes K, et al. Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease. P. Natl. Acad. Sci. USA 2003;100:5286-5291. 16. Ong AC and Harris PC. Molecular pathogenesis of ADPKD: the polycystin complex gets complex. Kidney Int. 2005;67:1234–1247. 17. Yoder BK, Hou X, Guay-Woodford LM. The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia. J Am Soc Nephrol 2002;13:2508–2516. 18. Somlo S, Ehrlich B. Human disease: Calcium signaling in polycystic kidney disease. Curr Biol 2001;11:R356–R360. 19. Koulen P, Cai Y, Geng L, Maeda Y, et al. Polycystin-2 is an intracellular calcium release channel. Nat Cell Biol 2002;4:191–197. 20. Pazour GJ, San Agustin JT, Follit JA, Rosenbaum JL, Witman GB. Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease. Curr Biol 2002;12:R378–R380. 21. Rundle DR, Gorbsky G, Tsiokas L. PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindles. J Biol Chem 2004;279:29728–29739. 22. Chang MY, Ong AC. Autosomal dominant polycystic kidney disease: recent advances in pathogenesis and treatment. Nephron. Physiol. 2008;108(1):p1-7. 23. Cabrera-Poch N, Sanchez-Ruiloba L, Rodriguez-Martinez M, Iglesias T. Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells. J. Biol. Chem. 2004;279:28592-28602. 24. Hirokawa N. Stirring up development with the heterotrimeric kinesin KIF3. Traffic. 2000;1:29-34. 25. Wu Y, Dai XQ, Li Q, Chen CX, et al. Kinesin-2 mediates physical and functional interactions between polycystin-2 and fibrocystin. Hum. Mol. Genet. 2006;15:3280-3292. 26. Tazón-Vega B, Vilardell M, Pérez-Oller L, et al. Study of candidate genes affecting the progression of renal disease in autosomal dominant polycystic kidney disease type 1. Nephrol. Dial. Transplant. 2007;22(6):1567-77. 27. Lin, S.-Y., Makino, K., Xia, W., et al. Nuclear localization of EGF receptorand its potential new role as a transcription factor. Nat. Cell Biol. 2001;3:802–808. 28. Wang SC, Lien HC, Xia W, et al. Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2. Cancer Cell 2004;6:251–261. 29. Offterdinger, M., Schöfer, C., Weipoltshammer, K., and Grunt, T. W. C-erbB-3, a nuclear protein in mammary epithelial cells. J. Cell Biol. 2002;157:929–939. 30. Maher, P. A. Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2. J. Cell Biol. 1996;134:529–536. 31. Lee, D. K., Lanc¸a, A. J., Cheng, R., et al. Agonist-independent nuclear localization of the apelin, angiotensin AT1, and bradykinin B2 receptors. J. Biol. Chem. 2004;279:7901–7908. 32. Boivin, B., Chevalier, D., Villeneuve, L. R., Rousseau, É, and Allen, B. G. Functional endothelin receptors are present on nuclei in cardiac ventricular myocytes. J. Biol. Chem. 2003;278:29153–29163. 33. Hsu SC, Hung MC. Characterization of a novel tripartite nuclear localization sequence in the EGFR family. J. Biol Chem. 2007;282(14):10432-40. 34. MacDonald HS, Kushnaryov VM, Sedmak JJ, Grossberg SE. Transport of gamma-interferon into the cell nucleus may be mediated bynuclear membrane receptors. Biochem. Biophys. Res. Commun. 1986;138:254–260. 35. Lobie PE, Wood TJ, Chen CM, Waters MJ, Norstedt G. Nuclear translocation and anchorage of the growth hormone receptor. J. Biol. Chem. 1994;269(50):31735-46. 36. Buckley AR, Montgomery DW, Hendrix MJ, Zukoski CF, Putnam CW. Identification of prolactin receptors in hepatic nuclei. Arch. Biochem. Biophys. 1992;296(1):198-206. 37. Ni CY, Murphy MP, Golde TE, Carpenter G. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science. 2001;294(5549):2179-81. 38. Carpenter G. Nuclear localization and possible functions of receptor tyrosine kinases. Curr. Opin. Cell. Biol. 2003;15(2):143-8. 39. Bryant DM, Stow JL. Nuclear translocation of cell-surface receptors: lessons from fibroblast growth factor. Traffic. 2005;6(10):947-54. 40. Swanson SM, Kopchick JJ. Nuclear localization of growth hormone receptor: another age of discovery for cytokine action? Sci. STKE. 2007;2007(415):pe69. 41. Liao HJ, Carpenter G. Role of the Sec61 translocation in EGF receptor trafficking to the nucleus and gene expression. Mol. Biol. Cell. 2007;18(3):1064-72. 42. Howe CL, Mobley WC. Signaling endosome hypothesis: A cellular mechanism for long distance communication. J. Neurobiol. 2004;58(2):207-16. 43. Hisata S, Sakisaka T, Baba T, et al. Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late endosomes, leading to sustained activation of Rap1 and ERK and neurite outgrowth. J. Cell. Biol. 2007;178(5):843-60. 44. Mosavi LK, Cammett TJ, Desrosiers DC, Peng ZY. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 2004;13(6):1435-48. 45. Li J, Mahajan A, Tsai MD. Ankyrin repeat: a unique motif mediating protein-protein interactions. Biochemistry. 2006;45(51):15168-78. 46. Qiao F, Bowie JU. The many faces of SAM. Sci. STKE. 2005;2005(286):re7. 47. Cogswell C, Price SJ, Hou X, Guay-Woodford LM, Flaherty L, Bryda EC. Positional cloning of jcpk/bpk locus of the mouse. Mamm. Genome. 2003;14(4):242-9. 48. Bouvrette DJ, Price SJ, Bryda EC. K homology domains of the mouse polycystic kidney disease-related protein, Bicaudal-C (Bicc1), mediate RNA binding in vitro. Nephron. Exp. Nephrol. 2008;108(1):e27-34. 49. Khundmiri SJ, Ahmad A, Bennett RE, et al. Novel regulatory function for NHERF-1 in Npt2a transcription. Am. J. Physiol. Renal. Physiol. 2008;294(4):F840-9. 50. Kato Y, Sai Y, Yoshida K, Watanabe C, Hirata T, Tsuji A. PDZK1 directly regulates the function of organic cation/carnitine transporter OCTN2. Mol. Pharmacol. 2005;67(3):734-43. 51. Tanemoto M, Toyohara T, Abe T, Ito S. MAGI-1a functions as a scaffolding protein for the distal renal tubular basolateral K+ channels. J. Biol. Chem. 2008;283(18):12241-7. 52. Yamamoto T, Harada N, Kano K, et al. The Ras target AF-6 interacts with ZO-1 and serves as a peripheral component of tight junctions in epithelial cells. J. Cell. Biol. 1997;139(3):785-95. 53. Osada H, Hasada K, Inazawa J, et al. Subcellular localization and protein interaction of the human LIMK2 gene expressing alternative transcripts with tissue-specific regulation. Biochem. Biophys. Res. Commun. 1996;229(2):582-9. 54. Sherman DL, Brophy PJ. A tripartite nuclear localization signal in the PDZ-domain protein L-periaxin. J. Biol. Chem. 2000;275(7):4537-40. 55. Hsueh YP, Wang TF, Yang FC, Sheng M. Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2. Nature. 2000;404(6775):298-302. 56. Zhang Y, Kornfeld H, Cruikshank WW, Kim S, Reardon CC, Center DM. Nuclear translocation of the N-terminal prodomain of interleukin-16. J. Biol. Chem. 2001;276(2):1299-303. 57. Islas S, Vega J, Ponce L, González-Mariscal L. Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Exp. Cell. Res. 2002;274(1):138-48. 58. Betanzos A, Huerta M, Lopez-Bayghen E, Azuara E, Amerena J, González-Mariscal L. The tight junction protein ZO-2 associates with Jun, Fos and C/EBP transcription factors in epithelial cells. Exp. Cell. Res. 2004;292(1):51-66. 59. Traweger A, Fuchs R, Krizbai IA, Weiger TM, Bauer HC, Bauer H. The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B. J. Biol. Chem. 2003;278(4):2692-700. 60. Hossain Z, Ali SM, Ko HL, et al. Glomerulocystic kidney disease in mice with a targeted inactivation of Wwtr1. Proc. Natl. Acad. Sci. USA. 2007;104(5):1631-6. 61. Makita R, Uchijima Y, Nishiyama K, Amano T, Chen Q, Takeuchi T, Mitani A, Nagase T, Yatomi Y, Aburatani H, Nakagawa O, Small EV, Cobo-Stark P, et al. Multiple renal cysts, urinary concentration defects, and pulmonary emphysematous changes in mice lacking TAZ. Am. J. Physiol. Renal. Physiol. 2008;294(3):F542-53. 62. Grantham JJ. Acquired cystic kidney disease. Kidney Int. 1991;40:143–152. 63. Mangoo-Karim R, Uchic M, Lechene C, Grantham JJ. Renal epithelial cyst formation and enlargement in vitro: Dependence on cAMP. Proc Natl Acad Sci U.S.A. 1989;86:6007–6011 64. Konda R, Sato H, Hatafuku F, Nozawa T, Ioritani N, Fujioka T. Expression of hepatocyte growth factor and its receptor C-met in acquired renal cystic disease associated with renal cell carcinoma. J. Urol. 2004;171(6 Pt 1):2166-70. 65. Ryuichiro Konda, Jun Sugimura, Fumihiko Sohma, Toyomasa Katagiri, Yusuke Nakamura and Tomoaki Fujioka. Over expression of hypoxia-inducible protein 2, hypoxia-inducible factor-1 and nuclear factor κB is putatively involved in acquired renal cyst formation and subsequent tumor transformation in patients with end stage renal failure. J. Urol. 2008;180(2):481-5. 66. Zen Y, Fujii T, Itatsu K, et al. Biliary cystic tumors with bile duct communication: a cystic variant of intraductal papillary neoplasm of the bile duct. Mod. Pathol. 2006;19(9):1243-54. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/40370 | - |
dc.description.abstract | Ankyrin repeat-rich membrane spanning (簡稱ARMS)為一神經細胞表現之膜蛋白,其功能為調控神經纖維的生長與維持神經肌肉接點。然而對於ARMS在其他正常的、病態的組織或細胞的表現,卻尚未曾被探討過。利用在組織微陣列上進行的ARMS免疫組織染色,我們發現ARMS特別表現在唾液管腺、皮膚汗腺與腎小管。同時,我們發現ARMS和KIF3A在腎小管的表皮細胞上有部分表現在同一位置,其位置是在細胞質與管腔面的細胞膜。由於過去的研究顯示KIF3A基因剔除小鼠會產生多囊性腎病,促使我們進一步探究是否ARMS的表現在人類的多囊性腎病上也有所變化。在二十個多囊性腎病的台大醫院病理部確診之案例中(民國89年至97年),ARMS免疫組織染色發現到ARMS在囊泡的表面細胞出現異常表現並且有在細胞核內表現 (廿個案例中的廿個均有此現象)。相比較之下,單純性腎囊腫只在細胞質有微弱至中等強度的ARMS表現,而表現在細胞核內的情形極為罕見(廿個案例中的五個有此現象)。此等觀察到的現象,使吾等推測ARMS在細胞核的異常性表現在人類的多囊性腎病具有特異性。同時,在另一與多囊性腎病高度相關的疾病:多囊性肝病中,其囊泡表面細胞中,則有新生的ARMS表現,並且也有在細胞核的表現。在其他肝內膽道囊狀腫瘤,其囊泡表面細胞則同樣有ARMS的新生表現情況。因此我們假設,在腎臟或是肝臟囊泡性疾病中,ARMS對於形成泡囊的過程中可能扮演著重要角色。 | zh_TW |
dc.description.abstract | Ankyrin repeat-rich membrane spanning (ARMS) is a tetra-membranous protein enriched in neurons, and it regulates neurite growth and maintenance of neuromuscular junction. Whether ARMS is expressed in other tissue or cell type, diseased or not, is not investigated. By ARMS immunohistochemistry on tissue arrays composed of normal human tissues, we reported that ARMS is specifically expressed in ductal epithelia of salivary gland ducts, of skin eccrine ducts and of renal tubules. We further demonstrated that in renal tubules, ARMS was partially colocalized with KIF3A in the cytoplasm and apical membrane of renal tubular epithelium. Based on the fact that KIF3A-null results in polycystic kidney in mutant mice, we explored whether ARMS was aberrantly expressed in human renal polycystic disease. Immunohistochemistry in 20 cases of human polycystic kidney disease enrolled in Department of Pathology, National Taiwan University (2000-2008) revealed that ARMS was aberrantly and strongly expressed in the nucleus of the epithelium lining the cysts (20/20 cases). Whereas in contrast, almost all cases diagnosed as simple renal cysts showed weak to moderate ARMS-immunoreativity in the cytoplasm, but rarely in the nucleus (5/20). This observation suggests that ectopic nuclear localization of ARMS is specifically correlated with human polycystic kidney disease. Adding into complexity, ARMS could be neo-expressed and localized in the nucleus of those cystic epithelia lining hepatic polycystic liver, which is often associated with polycystic kidney disease. Examination of other intrahepatic biliary cystic neoplasms revealed neo-expression of ARMS in the cells lining these cysts. We hypothesize that ARMS might play an important role in mediating cyst formation originating specifically from renal or biliary tubular epithelium. | en |
dc.description.provenance | Made available in DSpace on 2021-06-14T16:45:55Z (GMT). No. of bitstreams: 1 ntu-97-R95444005-1.pdf: 1064622 bytes, checksum: 353348eaecc9d21bb9be5c6f2a76d237 (MD5) Previous issue date: 2008 | en |
dc.description.tableofcontents | CONTENT 1
FIGURE CONTENT 2 SUPPLEMENTARY FIGURE CONTENT 4 SUPPLEMENTARY TABLE CONTENT 5 ABBREVIATION 6 ABSTRACT 7 ABSTRACT (CHINESE) 9 INTRODUCTION 10 STUDY PURPOSE AND RATIONALE 14 MATERIALS AND METHODS 16 RESULTS 19 DISCUSSION 23 TABLES 36 REFERENCES 39 SUPPLEMENTARY FIGURES 48 SUPPLEMENTARY TABLES 51 | |
dc.language.iso | en | |
dc.title | 探討Ankyrin Repeat-rich Membrane Spanning(ARMS)蛋白在多囊性腎病與肝內膽道疾病之生物功能 | zh_TW |
dc.title | The Role of Ankyrin Repeat-rich Membrane Spanning (ARMS) in Polycystic Kidney Disease and Intrahepatic Biliary Tree Disease | en |
dc.type | Thesis | |
dc.date.schoolyear | 96-2 | |
dc.description.degree | 碩士 | |
dc.contributor.coadvisor | 許世明 | |
dc.contributor.oralexamcommittee | 林中梧,林欽塘,周祖述 | |
dc.subject.keyword | 多囊性腎病,肝內膽道囊狀疾病,組織微陣列,組織免疫染色, | zh_TW |
dc.subject.keyword | ARMS,polycystic kidney,intrahepatic biliary cystic lesion,tissue array,immunohistochemistry, | en |
dc.relation.page | 57 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2008-07-31 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 病理學研究所 | zh_TW |
顯示於系所單位: | 病理學科所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-97-1.pdf 目前未授權公開取用 | 1.04 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。