請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/39356完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 楊性芳(Hsin-Fang Yang-Yen) | |
| dc.contributor.author | Hsuan Liu | en |
| dc.contributor.author | 劉軒 | zh_TW |
| dc.date.accessioned | 2021-06-13T17:26:42Z | - |
| dc.date.available | 2005-02-18 | |
| dc.date.copyright | 2005-02-18 | |
| dc.date.issued | 2005 | |
| dc.date.submitted | 2005-01-17 | |
| dc.identifier.citation | 1. Adams, J. M., and S. Cory. 1998. The Bcl-2 protein family: arbiters of cell survival. Science 281:1322-6.
2. Adams, M. D., A. R. Kerlavage, R. D. Fleischmann, R. A. Fuldner, C. J. Bult, N. H. Lee, E. F. Kirkness, K. G. Weinstock, J. D. Gocayne, O. White, and et al. 1995. Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. Nature 377:3-174. 3. Akgul, C., D. A. Moulding, and S. W. Edwards. 2001. Molecular control of neutrophil apoptosis. FEBS Lett 487:318-22. 4. Altmeyer, A., R. C. Simmons, S. Krajewski, J. C. Reed, G. W. Bornkamm, and S. Chen-Kiang. 1997. Reversal of EBV immortalization precedes apoptosis in IL-6-induced human B cell terminal differentiation. Immunity 7:667-77. 5. Ashkenazi, A., and V. M. Dixit. 1998. Death receptors: signaling and modulation. Science 281:1305-8. 6. Bae, J., C. P. Leo, S. Y. Hsu, and A. J. Hsueh. 2000. MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. J Biol Chem 275:25255-61. 7. Baudet, C., E. Perret, B. Delpech, M. Kaghad, P. Brachet, D. Wion, and D. Caput. 1998. Differentially expressed genes in C6.9 glioma cells during vitamin D-induced cell death program. Cell Death Differ 5:116-25. 8. Benndorf, R., P. Nurnberg, and H. Bielka. 1988. Growth phase-dependent proteins of the Ehrlich ascites tumor analyzed by one- and two-dimensional electrophoresis. Exp Cell Res 174:130-8. 9. Bheekha-Escura, R., D. W. MacGlashan, J. M. Langdon, and S. M. MacDonald. 2000. Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line, AML14-3D10. Blood 96:2191-8. 10. Bhisutthibhan, J., M. A. Philbert, H. Fujioka, M. Aikawa, and S. R. Meshnick. 1999. The Plasmodium falciparum translationally controlled tumor protein: subcellular localization and calcium binding. Eur J Cell Biol 78:665-70. 11. Bingle, C. D., R. W. Craig, B. M. Swales, V. Singleton, P. Zhou, and M. K. Whyte. 2000. Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death. J Biol Chem 275:22136-46. 12. Bohm, H., R. Benndorf, M. Gaestel, B. Gross, P. Nurnberg, R. Kraft, A. Otto, and H. Bielka. 1989. The growth-related protein P23 of the Ehrlich ascites tumor: translational control, cloning and primary structure. Biochem Int 19:277-86. 13. Bommer, U. A., A. V. Borovjagin, M. A. Greagg, I. W. Jeffrey, P. Russell, K. G. Laing, M. Lee, and M. J. Clemens. 2002. The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR. Rna 8:478-96. 14. Bommer, U. A., A. Lazaris-Karatzas, A. De Benedetti, P. Nurnberg, R. Benndorf, H. Bielka, and N. Sonenberg. 1994. Translational regulation of the mammalian growth-related protein P23: involvement of eIF-4E. Cell Mol Biol Res 40:633-41. 15. Bonnet, C., E. Perret, X. Dumont, A. Picard, D. Caput, and G. Lenaers. 2000. Identification and transcription control of fission yeast genes repressed by an ammonium starvation growth arrest. Yeast 16:23-33. 16. Boucher, M. J., J. Morisset, P. H. Vachon, J. C. Reed, J. Laine, and N. Rivard. 2000. MEK/ERK signaling pathway regulates the expression of Bcl-2, Bcl-X(L), and Mcl-1 and promotes survival of human pancreatic cancer cells. J Cell Biochem 79:355-69. 17. Cans, C., B. J. Passer, V. Shalak, V. Nancy-Portebois, V. Crible, N. Amzallag, D. Allanic, R. Tufino, M. Argentini, D. Moras, G. Fiucci, B. Goud, M. Mirande, R. Amson, and A. Telerman. 2003. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Proc Natl Acad Sci U S A 100:13892-7. 18. Chao, D. T., and S. J. Korsmeyer. 1998. BCL-2 family: regulators of cell death. Annu Rev Immunol 16:395-419. 19. Chao, J. R., J. M. Wang, S. F. Lee, H. W. Peng, Y. H. Lin, C. H. Chou, J. C. Li, H. M. Huang, C. K. Chou, M. L. Kuo, J. J. Yen, and H. F. Yang-Yen. 1998. mcl-1 is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling pathway and is one component of the GM-CSF viability response. Mol Cell Biol 18:4883-98. 20. Chitpatima, S. T., S. Makrides, R. Bandyopadhyay, and G. Brawerman. 1988. Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells. Nucleic Acids Res 16:2350. 21. Craig, R. W. 2002. MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis. Leukemia 16:444-54. 22. Croxton, R., Y. Ma, L. Song, E. B. Haura, and W. D. Cress. 2002. Direct repression of the Mcl-1 promoter by E2F1. Oncogene 21:1359-69. 23. Cuconati, A., C. Mukherjee, D. Perez, and E. White. 2003. DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells. Genes Dev 17:2922-32. 24. Domina, A. M., J. H. Smith, and R. W. Craig. 2000. Myeloid cell leukemia 1 is phosphorylated through two distinct pathways, one associated with extracellular signal-regulated kinase activation and the other with G2/M accumulation or protein phosphatase 1/2A inhibition. J Biol Chem 275:21688-94. 25. Domina, A. M., J. A. Vrana, M. A. Gregory, S. R. Hann, and R. W. Craig. 2004. MCL1 is phosphorylated in the PEST region and stabilized upon ERK activation in viable cells, and at additional sites with cytotoxic okadaic acid or taxol. Oncogene 23:5301-15. 26. Epling-Burnette, P. K., B. Zhong, F. Bai, K. Jiang, R. D. Bailey, R. Garcia, R. Jove, J. Y. Djeu, T. P. Loughran, Jr., and S. Wei. 2001. Cooperative regulation of Mcl-1 by Janus kinase/stat and phosphatidylinositol 3-kinase contribute to granulocyte-macrophage colony-stimulating factor-delayed apoptosis in human neutrophils. J Immunol 166:7486-95. 27. Fiucci, G., A. Lespagnol, P. Stumptner-Cuvelette, S. Beaucourt, D. Duflaut, L. Susini, R. Amson, and A. Telerman. 2003. Genomic organization and expression of mouse Tpt1 gene. Genomics 81:570-8. 28. Fujise, K., D. Zhang, J. Liu, and E. T. Yeh. 2000. Regulation of apoptosis and cell cycle progression by MCL1. Differential role of proliferating cell nuclear antigen. J Biol Chem 275:39458-65. 29. Gachet, Y., S. Tournier, M. Lee, A. Lazaris-Karatzas, T. Poulton, and U. A. Bommer. 1999. The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle. J Cell Sci 112 (Pt 8):1257-71. 30. Gojo, I., B. Zhang, and R. G. Fenton. 2002. The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in multiple myeloma cells through transcriptional repression and down-regulation of Mcl-1. Clin Cancer Res 8:3527-38. 31. Gross, A., J. M. McDonnell, and S. J. Korsmeyer. 1999. BCL-2 family members and the mitochondria in apoptosis. Genes Dev 13:1899-911. 32. Gross, B., M. Gaestel, H. Bohm, and H. Bielka. 1989. cDNA sequence coding for a translationally controlled human tumor protein. Nucleic Acids Res 17:8367. 33. Gupta, S. 2000. Molecular and biochemical pathways of apoptosis in lymphocytes from aged humans. Vaccine 18:1596-601. 34. Gupta, S. 2000. Molecular steps of cell suicide: an insight into immune senescence. J Clin Immunol 20:229-39. 35. Haghighat, N. G., and L. Ruben. 1992. Purification of novel calcium binding proteins from Trypanosoma brucei: properties of 22-, 24- and 38-kilodalton proteins. Mol Biochem Parasitol 51:99-110. 36. Haldar, S., J. Chintapalli, and C. M. Croce. 1996. Taxol induces bcl-2 phosphorylation and death of prostate cancer cells. Cancer Res 56:1253-5. 37. Haldar, S., N. Jena, and C. M. Croce. 1994. Antiapoptosis potential of bcl-2 oncogene by dephosphorylation. Biochem Cell Biol 72:455-62. 38. Haldar, S., N. Jena, and C. M. Croce. 1995. Inactivation of Bcl-2 by phosphorylation. Proc Natl Acad Sci U S A 92:4507-11. 39. Herrant, M., A. Jacquel, S. Marchetti, N. Belhacene, P. Colosetti, F. Luciano, and P. Auberger. 2004. Cleavage of Mcl-1 by caspases impaired its ability to counteract Bim-induced apoptosis. Oncogene 23:7863-73. 40. Huang, H. M., C. J. Huang, and J. J. Yen. 2000. Mcl-1 is a common target of stem cell factor and interleukin-5 for apoptosis prevention activity via MEK/MAPK and PI-3K/Akt pathways. Blood 96:1764-71. 41. Inoshita, S., K. Takeda, T. Hatai, Y. Terada, M. Sano, J. Hata, A. Umezawa, and H. Ichijo. 2002. Phosphorylation and inactivation of myeloid cell leukemia 1 by JNK in response to oxidative stress. J Biol Chem 277:43730-4. 42. Ito, T., X. Deng, B. Carr, and W. S. May. 1997. Bcl-2 phosphorylation required for anti-apoptosis function. J Biol Chem 272:11671-3. 43. Jamil, S., R. Sobouti, P. Hojabrpour, M. Raj, J. Kast, and V. Duronio. 2004. A proteolytic fragment of Mcl-1 exhibits nuclear localization and regulates cell growth via interaction with Cdk1. Biochem J. 44. Jourdan, M., J. De Vos, N. Mechti, and B. Klein. 2000. Regulation of Bcl-2-family proteins in myeloma cells by three myeloma survival factors: interleukin-6, interferon-alpha and insulin-like growth factor 1. Cell Death Differ 7:1244-52. 45. Jung, J., M. Kim, M. J. Kim, J. Kim, J. Moon, J. S. Lim, M. Kim, and K. Lee. 2004. Translationally controlled tumor protein interacts with the third cytoplasmic domain of Na,K-ATPase alpha subunit and inhibits the pump activity in HeLa cells. J Biol Chem 279:49868-75. 46. Kang, H. S., M. J. Lee, H. Song, S. H. Han, Y. M. Kim, J. Y. Im, and I. Choi. 2001. Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor. J Immunol 166:6545-54. 47. Karsan, A., E. Yee, K. Kaushansky, and J. M. Harlan. 1996. Cloning of human Bcl-2 homologue: inflammatory cytokines induce human A1 in cultured endothelial cells. Blood 87:3089-96. 48. Kim, M., Y. Jung, K. Lee, and C. Kim. 2000. Identification of the calcium binding sites in translationally controlled tumor protein. Arch Pharm Res 23:633-6. 49. Klampfer, L., J. Zhang, and S. D. Nimer. 1999. GM-CSF rescues TF-1 cells from growth factor withdrawal-induced, but not differentiation-induced apoptosis: the role of BCL-2 and MCL-1. Cytokine 11:849-55. 50. Kluck, R. M., E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer. 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275:1132-6. 51. Korsmeyer, S. J. 1999. Programmed cell death and the regulation of homeostasis. Harvey Lect 95:21-41. 52. Kozopas, K. M., H. L. Buchan, and R. W. Craig. 1990. Improved coupling between proliferation-arrest and differentiation-induction in ML-1 human myeloblastic leukemia cells. J Cell Physiol 145:575-86. 53. Kozopas, K. M., T. Yang, H. L. Buchan, P. Zhou, and R. W. Craig. 1993. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2. Proc Natl Acad Sci U S A 90:3516-20. 54. Krajewski, S., S. Bodrug, M. Krajewska, A. Shabaik, R. Gascoyne, K. Berean, and J. C. Reed. 1995. Immunohistochemical analysis of Mcl-1 protein in human tissues. Differential regulation of Mcl-1 and Bcl-2 protein production suggests a unique role for Mcl-1 in control of programmed cell death in vivo. Am J Pathol 146:1309-19. 55. Kuo, M. L., S. E. Chuang, M. T. Lin, and S. Y. Yang. 2001. The involvement of PI 3-K/Akt-dependent up-regulation of Mcl-1 in the prevention of apoptosis of Hep3B cells by interleukin-6. Oncogene 20:677-85. 56. Letai, A., M. C. Bassik, L. D. Walensky, M. D. Sorcinelli, S. Weiler, and S. J. Korsmeyer. 2002. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2:183-92. 57. Leu, C. M., C. Chang, and C. Hu. 2000. Epidermal growth factor (EGF) suppresses staurosporine-induced apoptosis by inducing mcl-1 via the mitogen-activated protein kinase pathway. Oncogene 19:1665-75. 58. Li, F., D. Zhang, and K. Fujise. 2001. Characterization of fortilin, a novel antiapoptotic protein. J Biol Chem 276:47542-9. 59. Lin, E. Y., A. Orlofsky, M. S. Berger, and M. B. Prystowsky. 1993. Characterization of A1, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2. J Immunol 151:1979-88. 60. Lin, Y. H., C. J. Huang, J. R. Chao, S. T. Chen, S. F. Lee, J. J. Yen, and H. F. Yang-Yen. 2000. Coupling of osteopontin and its cell surface receptor CD44 to the cell survival response elicited by interleukin-3 or granulocyte-macrophage colony-stimulating factor. Mol Cell Biol 20:2734-42. 61. Liu, H., H. Perlman, L. J. Pagliari, and R. M. Pope. 2001. Constitutively activated Akt-1 is vital for the survival of human monocyte-differentiated macrophages. Role of Mcl-1, independent of nuclear factor (NF)-kappaB, Bad, or caspase activation. J Exp Med 194:113-26. 62. Lomo, J., E. B. Smeland, S. Krajewski, J. C. Reed, and H. K. Blomhoff. 1996. Expression of the Bcl-2 homologue Mcl-1 correlates with survival of peripheral blood B lymphocytes. Cancer Res 56:40-3. 63. MacDonald, S. M., J. Bhisutthibhan, T. A. Shapiro, S. J. Rogerson, T. E. Taylor, M. Tembo, J. M. Langdon, and S. R. Meshnick. 2001. Immune mimicry in malaria: Plasmodium falciparum secretes a functional histamine-releasing factor homolog in vitro and in vivo. Proc Natl Acad Sci U S A 98:10829-32. 64. MacDonald, S. M., T. Rafnar, J. Langdon, and L. M. Lichtenstein. 1995. Molecular identification of an IgE-dependent histamine-releasing factor. Science 269:688-90. 65. Mak, C. H., K. W. Su, and R. C. Ko. 2001. Identification of some heat-induced genes of Trichinella spiralis. Parasitology 123:293-300. 66. Michels, J., J. W. O'Neill, C. L. Dallman, A. Mouzakiti, F. Habens, M. Brimmell, K. Y. Zhang, R. W. Craig, E. G. Marcusson, P. W. Johnson, and G. Packham. 2004. Mcl-1 is required for Akata6 B-lymphoma cell survival and is converted to a cell death molecule by efficient caspase-mediated cleavage. Oncogene 23:4818-27. 67. Moulding, D. A., C. Akgul, M. Derouet, M. R. White, and S. W. Edwards. 2001. BCL-2 family expression in human neutrophils during delayed and accelerated apoptosis. J Leukoc Biol 70:783-92. 68. Newton, K., and A. Strasser. 1998. The Bcl-2 family and cell death regulation. Curr Opin Genet Dev 8:68-75. 69. Nielsen, H. V., A. H. Johnsen, J. C. Sanchez, D. F. Hochstrasser, and P. O. Schiotz. 1998. Identification of a basophil leukocyte interleukin-3-regulated protein that is identical to IgE-dependent histamine-releasing factor. Allergy 53:642-52. 70. Nijhawan, D., M. Fang, E. Traer, Q. Zhong, W. Gao, F. Du, and X. Wang. 2003. Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. Genes Dev 17:1475-86. 71. Norbeck, J., and A. Blomberg. 1997. Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins. Yeast 13:1519-34. 72. Oikawa, K., T. Ohbayashi, J. Mimura, Y. Fujii-Kuriyama, S. Teshima, K. Rokutan, K. Mukai, and M. Kuroda. 2002. Dioxin stimulates synthesis and secretion of IgE-dependent histamine-releasing factor. Biochem Biophys Res Commun 290:984-7. 73. Okita, H., A. Umezawa, A. Suzuki, and J. Hata. 1998. Up-regulated expression of murine Mcl1/EAT, a bcl-2 related gene, in the early stage of differentiation of murine embryonal carcinoma cells and embryonic stem cells. Biochim Biophys Acta 1398:335-41. 74. Opferman, J. T., A. Letai, C. Beard, M. D. Sorcinelli, C. C. Ong, and S. J. Korsmeyer. 2003. Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1. Nature 426:671-6. 75. Puthier, D., R. Bataille, and M. Amiot. 1999. IL-6 up-regulates mcl-1 in human myeloma cells through JAK / STAT rather than ras / MAP kinase pathway. Eur J Immunol 29:3945-50. 76. Puthier, D., W. Thabard, M. Rapp, M. Etrillard, J. Harousseau, R. Bataille, and M. Amiot. 2001. Interferon alpha extends the survival of human myeloma cells through an upregulation of the Mcl-1 anti-apoptotic molecule. Br J Haematol 112:358-63. 77. Raff, M. C. 1992. Social controls on cell survival and cell death. Nature 356:397-400. 78. Reynolds, J. E., T. Yang, L. Qian, J. D. Jenkinson, P. Zhou, A. Eastman, and R. W. Craig. 1994. Mcl-1, a member of the Bcl-2 family, delays apoptosis induced by c-Myc overexpression in Chinese hamster ovary cells. Cancer Res 54:6348-52. 79. Rinkenberger, J. L., S. Horning, B. Klocke, K. Roth, and S. J. Korsmeyer. 2000. Mcl-1 deficiency results in peri-implantation embryonic lethality. Genes Dev 14:23-7. 80. Sage-Ono, K., M. Ono, H. Harada, and H. Kamada. 1998. Dark-induced accumulation of mRNA for a homolog of translationally controlled tumor protein (TCTP) in Pharbitis. Plant Cell Physiol 39:357-60. 81. Sanchez, J. C., D. Schaller, F. Ravier, O. Golaz, S. Jaccoud, M. Belet, M. R. Wilkins, R. James, J. Deshusses, and D. Hochstrasser. 1997. Translationally controlled tumor protein: a protein identified in several nontumoral cells including erythrocytes. Electrophoresis 18:150-5. 82. Snowden, R. T., X. M. Sun, M. J. Dyer, and G. M. Cohen. 2003. Bisindolylmaleimide IX is a potent inducer of apoptosis in chronic lymphocytic leukaemic cells and activates cleavage of Mcl-1. Leukemia 17:1981-9. 83. Steller, H. 1995. Mechanisms and genes of cellular suicide. Science 267:1445-9. 84. Sturzenbaum, S. R., P. Kille, and A. J. Morgan. 1998. Identification of heavy metal induced changes in the expression patterns of the translationally controlled tumour protein (TCTP) in the earthworm Lumbricus rubellus1. Biochim Biophys Acta 1398:294-304. 85. Teshima, S., K. Rokutan, T. Nikawa, and K. Kishi. 1998. Macrophage colony-stimulating factor stimulates synthesis and secretion of a mouse homolog of a human IgE-dependent histamine-releasing factor by macrophages in vitro and in vivo. J Immunol 161:6356-66. 86. Thaw, P., N. J. Baxter, A. M. Hounslow, C. Price, J. P. Waltho, and C. J. Craven. 2001. Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones. Nat Struct Biol 8:701-4. 87. Thiele, H., M. Berger, C. Lenzner, H. Kuhn, and B. J. Thiele. 1998. Structure of the promoter and complete sequence of the gene coding for the rabbit translationally controlled tumor protein (TCTP) P23. Eur J Biochem 257:62-8. 88. Thiele, H., M. Berger, A. Skalweit, and B. J. Thiele. 2000. Expression of the gene and processed pseudogenes encoding the human and rabbit translationally controlled tumour protein (TCTP). Eur J Biochem 267:5473-81. 89. Thomas, G., and G. Thomas. 1986. Translational control of mRNA expression during the early mitogenic response in Swiss mouse 3T3 cells: identification of specific proteins. J Cell Biol 103:2137-44. 90. Thomas, G., G. Thomas, and H. Luther. 1981. Transcriptional and translational control of cytoplasmic proteins after serum stimulation of quiescent Swiss 3T3 cells. Proc Natl Acad Sci U S A 78:5712-6. 91. Thompson, C. B. 1995. Apoptosis in the pathogenesis and treatment of disease. Science 267:1456-62. 92. Townsend, K. J., J. L. Trusty, M. A. Traupman, A. Eastman, and R. W. Craig. 1998. Expression of the antiapoptotic MCL1 gene product is regulated by a mitogen activated protein kinase-mediated pathway triggered through microtubule disruption and protein kinase C. Oncogene 17:1223-34. 93. Townsend, K. J., P. Zhou, L. Qian, C. K. Bieszczad, C. H. Lowrey, A. Yen, and R. W. Craig. 1999. Regulation of MCL1 through a serum response factor/Elk-1-mediated mechanism links expression of a viability-promoting member of the BCL2 family to the induction of hematopoietic cell differentiation. J Biol Chem 274:1801-13. 94. Tuynder, M., G. Fiucci, S. Prieur, A. Lespagnol, A. Geant, S. Beaucourt, D. Duflaut, S. Besse, L. Susini, J. Cavarelli, D. Moras, R. Amson, and A. Telerman. 2004. Translationally controlled tumor protein is a target of tumor reversion. Proc Natl Acad Sci U S A 101:15364-9. 95. Tuynder, M., L. Susini, S. Prieur, S. Besse, G. Fiucci, R. Amson, and A. Telerman. 2002. Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1. Proc Natl Acad Sci U S A 99:14976-81. 96. Umezawa, A., T. Maruyama, J. Inazawa, S. Imai, T. Takano, and J. Hata. 1996. Induction of mcl1/EAT, Bcl-2 related gene, by retinoic acid or heat shock in the human embryonal carcinoma cells, NCR-G3. Cell Struct Funct 21:143-50. 97. Vaux, D. L., and S. J. Korsmeyer. 1999. Cell death in development. Cell 96:245-54. 98. Wang, J. M., J. R. Chao, W. Chen, M. L. Kuo, J. J. Yen, and H. F. Yang-Yen. 1999. The antiapoptotic gene mcl-1 is up-regulated by the phosphatidylinositol 3-kinase/Akt signaling pathway through a transcription factor complex containing CREB. Mol Cell Biol 19:6195-206. 99. Wang, J. M., M. Z. Lai, and H. F. Yang-Yen. 2003. Interleukin-3 stimulation of mcl-1 gene transcription involves activation of the PU.1 transcription factor through a p38 mitogen-activated protein kinase-dependent pathway. Mol Cell Biol 23:1896-909. 100. Xu, A., A. R. Bellamy, and J. A. Taylor. 1999. Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level. Biochem J 342 Pt 3:683-9. 101. Yan, L., K. Fei, D. Bridge, and M. P. Sarras, Jr. 2000. A cnidarian homologue of translationally controlled tumor protein (P23/TCTP). Dev Genes Evol 210:507-11. 102. Yang, J., X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang. 1997. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275:1129-32. 103. Yang, T., H. L. Buchan, K. J. Townsend, and R. W. Craig. 1996. MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation. J Cell Physiol 166:523-36. 104. Yang, T., K. M. Kozopas, and R. W. Craig. 1995. The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2. J Cell Biol 128:1173-84. 105. Yarm, F. R. 2002. Plk phosphorylation regulates the microtubule-stabilizing protein TCTP. Mol Cell Biol 22:6209-21. 106. Yenofsky, R., I. Bergmann, and G. Brawerman. 1982. Messenger RNA species partially in a repressed state in mouse sarcoma ascites cells. Proc Natl Acad Sci U S A 79:5876-80. 107. Yenofsky, R., S. Cereghini, A. Krowczynska, and G. Brawerman. 1983. Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide. Mol Cell Biol 3:1197-203. 108. Yoon, T., J. Jung, M. Kim, K. M. Lee, E. C. Choi, and K. Lee. 2000. Identification of the self-interaction of rat TCTP/IgE-dependent histamine-releasing factor using yeast two-hybrid system. Arch Biochem Biophys 384:379-82. 109. Zhang, D., F. Li, D. Weidner, Z. H. Mnjoyan, and K. Fujise. 2002. Physical and functional interaction between myeloid cell leukemia 1 protein (MCL1) and Fortilin. The potential role of MCL1 as a fortilin chaperone. J Biol Chem 277:37430-8. 110. Zhou, P., L. Qian, K. M. Kozopas, and R. W. Craig. 1997. Mcl-1, a Bcl-2 family member, delays the death of hematopoietic cells under a variety of apoptosis-inducing conditions. Blood 89:630-43. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/39356 | - |
| dc.description.abstract | Mcl-1 屬於Bcl-2 家族之一，其功能在發育過程中扮演了重要的角色。Mcl-1之極短半衰期及其蛋白質含量為許多細胞存活路徑之重要調控者，因此我們推測，細胞內調控Mcl-1蛋白的穩定性以及調控其合成的機制對於Mcl-1的功能同等重要。細胞受到許多生理刺激均會引發Mcl-1蛋白質含量之增加，此過程在轉錄機制方面有許多詳細的研究，但對於其穩定性的調控機制卻不是很清楚。此篇論文中，我們發現Translationally Controlled Tumor Protein (TCTP)會和Mcl-1作用而進一步調控Mcl-1蛋白的穩定性。當細胞內大量表現TCTP可以增加Mcl-1的半衰期，相反的，利用RNA干擾的方式來降低TCTP的表現則會降低Mcl-1蛋白的穩定性。研究TCTP基因愓除的老鼠則發現，Mcl-1的含量在TCTP+/-的老鼠中明顯的比TCTP+/+的低。我們的結果顯示，TCTP主要是藉由抑制Mcl-1的ubiqutinalation而影響Mcl-1的分解，因此而增加蛋白的半衰期。研究在TCTP結合上有缺失的Mcl-1突變蛋白(K257V)則發現其分解的速度加快, 且抗細胞凋亡的能力也相對降低。因此，我們推測，TCTP透過調控Mcl-1蛋白的穩定性，而影響其抗細胞凋亡的能力。其中可能牽涉之作用機轉，將在此論文中討論。
此外，我們的結果也顯示，生長訊號會同時調控Mcl-1和TCTP的蛋白表現量和細胞內的位置。 當細胞處於去除血清的情況之下，二者蛋白質都會在核中出現，而再使用血清刺激細胞時，二者則都會位於細胞質中。我們初步的結果顯示，TCTP可能會調控Mcl-1在細胞中的的位置，但此種現象對Mcl-1功能上的重要性並不清楚，需待更進一步的研究。 | zh_TW |
| dc.description.abstract | Mcl-1 is one Bcl-2 family member that plays a pivotal role in animal development. The extremely labile nature of the Mcl-1 protein itself and the fact that the Mcl-1 level is a critical determinant in various cell survival pathways suggest that cellular processes that regulate Mcl-1 stability are as important as those regulate Mcl-1 synthesis. While transcriptional stimulation of Mcl-1 synthesis in response to various stimuli has been well documented, regulation of Mcl-1 stability has been hardly explored. In this study, we identified that the Translationally Controlled Tumor Protein (TCTP) was one cellular factor that interacted with Mcl-1 and modulated Mcl-1 stability. While over-expression of TCTP augmented the protein stability of Mcl-1, knockdown expression of TCTP by RNA interference destabilized Mcl-1. Consistently, targeted ablation of the TCTP gene led to a reduced level of Mcl-1. Furthermore, TCTP stabilized Mcl-1 through interfering with Mcl-1’s degradation by the ubiquitin-dependent proteasome degradation pathway, and the TCTP binding-defective mutant of Mcl-1 (K257V) was much more susceptible to degradation and manifested a compromised anti-apoptotic activity. Taken together, these results suggest that TCTP modulates Mcl-1’s anti-apoptotic activity by modulating its protein stability. The possible mechanism(s) involved in TCTP’s modulation process is discussed.
Additionally, our results demonstrated an involvement of growth signaling in modulating the expression and subcellular localization of Mcl-1 and TCTP. Both proteins, which generally locate in the cytosol of rapidly growing cells, could be detected in the nuclear compartment when cells were deprived of serum. Furthermore, interaction with TCTP may be an important determinant in regulating the localization of Mcl-1. However, the functional significance of the nuclear localization of these proteins is not fully understood and awaits further investigation. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T17:26:42Z (GMT). No. of bitstreams: 1 ntu-94-D88448004-1.pdf: 4349653 bytes, checksum: ad9519589e976fc882395b0d8083be21 (MD5) Previous issue date: 2005 | en |
| dc.description.tableofcontents | 中文摘要………………………………………………….……….……….………………….4
Abstract……...…………………………………….…...……………….…….…………….…5 Introduction………………………………………...………….………………….................6 Material and method Yeast Two-Hybrid Screening………………………………………………….…………………21 Antibodies…………………………………………………………………………......................21 Cell culture and generation of stable cell lines…………….…………………….………………22 Expression vectors……………………………………………………………………………….23 In vitro GST pull-down assay …………………………………………………….……………..25 Co-immunoprecipitation of TCTP and mMcl-1…………….………………….…......................25 Binding of endogenous mouse Mc-l and TCTP…………….………………...……....................26 Indirect mmunofluorescence and confocal laser scanning microscopy.………….………..…….27 Determination of Mcl-1 protein half-life…………….…………………………….…………….27 Determination of Mcl-1 synthesis rate…………….…………………………..…………………28 In vivo ubiquitination of mMcl-1………………………………………………..……………....29 Knockdown of TCTP expression with small interfering RNA (siRNA)..………….....................29 Results Interaction between Mcl-1 and TCTP…………….……………………………….……………..31 TCTP enhances the protein stability of Mcl-1 but not vice versa…………………......................33 Knockdown expression of TCTP destabilizes Mcl-1…………….……………............................35 The TCTP binding-defective Mcl-1 mutant is much less stable and manifests a compromised anti-apoptotic activity …………….……………………………….……………….……………36 TCTP blocks ubiquitination of Mcl-1…………….……………………………….......................37 Mcl-1 expression level is altered in TCTP+/- mice…………….………………….…………..…38 The expression and subcellular localization of Mcl-1 and TCTP are both regulated in response to serum stimulation in the mouse NIH3T3 fibroblasts and human HeLa cells…………….….......39 The faster-migrating form of Mcl-1 is localized in the nucleus…………………...……….……40 Interaction with TCTP may be an important determinant in Mcl-1’s subcellular localization…..41 Microtubule-association of Mcl-1 and TCTP in mitotic cells…………….………......................41 Discussion…………….………………………………………….…………………………..43 Figures…………….……………………………….………………………...…………...…..49 References…………….……………………………………………………………………..72 Appendix 1: notification of acceptance…………………………..…..…………81 Appendix 2: submitted manuscript………………………………..…83 | |
| dc.language.iso | en | |
| dc.subject | 細胞凋亡 | zh_TW |
| dc.subject | 訊號傳遞 | zh_TW |
| dc.subject | signal transduction | en |
| dc.subject | apoptosis | en |
| dc.title | Mcl-1和TCTP交互作用之功能探討 | zh_TW |
| dc.title | Functional Characterization of Mcl-1 and TCTP Interaction | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 93-1 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | ?一蘋(Yi-Ping Hsueh),譚琬玉(WY Tarn,),施修明(HM Shih),李芳仁(Fang-Jen Lee) | |
| dc.subject.keyword | 訊號傳遞,細胞凋亡, | zh_TW |
| dc.subject.keyword | signal transduction,apoptosis, | en |
| dc.relation.page | 132 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2005-01-17 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 分子醫學研究所 | zh_TW |
| 顯示於系所單位： | 分子醫學研究所 | |
文件中的檔案：
| 檔案 | 大小 | 格式 | |
|---|---|---|---|
| ntu-94-1.pdf 未授權公開取用 | 4.25 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。