請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/65594完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張?仁(Ching-Jin Chang,) | |
| dc.contributor.author | Pei-Yu Chiang | en |
| dc.contributor.author | 江佩鈺 | zh_TW |
| dc.date.accessioned | 2021-06-16T23:52:43Z | - |
| dc.date.available | 2012-07-27 | |
| dc.date.copyright | 2012-07-27 | |
| dc.date.issued | 2012 | |
| dc.date.submitted | 2012-07-19 | |
| dc.identifier.citation | 1. Pinol-Roma S, Choi YD, Matunis MJ, Dreyfuss G (1988) Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins. Genes Dev 2: 215-227.
2. Choi YD, Dreyfuss G (1984) Isolation of the heterogeneous nuclear RNA-ribonucleoprotein complex (hnRNP): a unique supramolecular assembly. Proc Natl Acad Sci U S A 81: 7471-7475. 3. Dreyfuss G, Matunis MJ, Pinol-Roma S, Burd CG (1993) hnRNP proteins and the biogenesis of mRNA. Annu Rev Biochem 62: 289-321. 4. Dejgaard K, Leffers H, Rasmussen HH, Madsen P, Kruse TA, et al. (1994) Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing. J Mol Biol 236: 33-48. 5. Makeyev AV, Liebhaber SA (2002) The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms. RNA 8: 265-278. 6. Siomi H, Matunis MJ, Michael WM, Dreyfuss G (1993) The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res 21: 1193-1198. 7. Braddock DT, Baber JL, Levens D, Clore GM (2002) Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA. EMBO J 21: 3476-3485. 8. Thisted T, Lyakhov DL, Liebhaber SA (2001) Optimized RNA targets of two closely related triple KH domain proteins, heterogeneous nuclear ribonucleoprotein K and alphaCP-2KL, suggest Distinct modes of RNA recognition. J Biol Chem 276: 17484-17496. 9. Ostrowski J, Wyrwicz L, Rychlewski L, Bomsztyk K (2002) Heterogeneous nuclear ribonucleoprotein K protein associates with multiple mitochondrial transcripts within the organelle. J Biol Chem 277: 6303-6310. 10. Paziewska A, Wyrwicz LS, Bujnicki JM, Bomsztyk K, Ostrowski J (2004) Cooperative binding of the hnRNP K three KH domains to mRNA targets. FEBS Lett 577: 134-140. 11. Ostrowski J, Van Seuningen I, Seger R, Rauch CT, Sleath PR, et al. (1994) Purification, cloning, and expression of a murine phosphoprotein that binds the kappa B motif in vitro identifies it as the homolog of the human heterogeneous nuclear ribonucleoprotein K protein. Description of a novel DNA-dependent phosphorylation process. J Biol Chem 269: 17626-17634. 12. Michelotti EF, Michelotti GA, Aronsohn AI, Levens D (1996) Heterogeneous nuclear ribonucleoprotein K is a transcription factor. Mol Cell Biol 16: 2350-2360. 13. Baber JL, Libutti D, Levens D, Tjandra N (1999) High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor. J Mol Biol 289: 949-962. 14. Backe PH, Messias AC, Ravelli RB, Sattler M, Cusack S (2005) X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids. Structure 13: 1055-1067. 15. Klimek-Tomczak K, Wyrwicz LS, Jain S, Bomsztyk K, Ostrowski J (2004) Characterization of hnRNP K protein-RNA interactions. J Mol Biol 342: 1131-1141. 16. Bomsztyk K, Denisenko O, Ostrowski J (2004) hnRNP K: one protein multiple processes. Bioessays 26: 629-638. 17. Mikula M, Dzwonek A, Karczmarski J, Rubel T, Dadlez M, et al. (2006) Landscape of the hnRNP K protein-protein interactome. Proteomics 6: 2395-2406. 18. Kim JH, Hahm B, Kim YK, Choi M, Jang SK (2000) Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm. J Mol Biol 298: 395-405. 19. Shnyreva M, Schullery DS, Suzuki H, Higaki Y, Bomsztyk K (2000) Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein. J Biol Chem 275: 15498-15503. 20. Melnikova IN, Yang Y, Gardner PD (2000) Interactions between regulatory proteins that bind to the nicotinic receptor beta4 subunit gene promoter. Eur J Pharmacol 393: 75-83. 21. Miau LH, Chang CJ, Shen BJ, Tsai WH, Lee SC (1998) Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBPbeta-mediated gene activation. J Biol Chem 273: 10784-10791. 22. Denisenko ON, O'Neill B, Ostrowski J, Van Seuningen I, Bomsztyk K (1996) Zik1, a transcriptional repressor that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein. J Biol Chem 271: 27701-27706. 23. Denisenko ON, Bomsztyk K (1997) The product of the murine homolog of the Drosophila extra sex combs gene displays transcriptional repressor activity. Mol Cell Biol 17: 4707-4717. 24. Dzwonek A, Mikula M, Ostrowski J (2006) The diverse involvement of heterogeneous nuclear ribonucleoprotein K in mitochondrial response to insulin. FEBS Lett 580: 1839-1845. 25. Adolph D, Flach N, Mueller K, Ostareck DH, Ostareck-Lederer A (2007) Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site. Mol Cell Biol 27: 1758-1770. 26. Hobert O, Jallal B, Schlessinger J, Ullrich A (1994) Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction. J Biol Chem 269: 20225-20228. 27. Romero F, Germani A, Puvion E, Camonis J, Varin-Blank N, et al. (1998) Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C. Evidence for Vav-hnRNP interactions in an RNA-dependent manner. J Biol Chem 273: 5923-5931. 28. Michael WM, Eder PS, Dreyfuss G (1997) The K nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J 16: 3587-3598. 29. Ostrowski J, Kawata Y, Schullery DS, Denisenko ON, Bomsztyk K (2003) Transient recruitment of the hnRNP K protein to inducibly transcribed gene loci. Nucleic Acids Res 31: 3954-3962. 30. Tomonaga T, Levens D (1995) Heterogeneous nuclear ribonucleoprotein K is a DNA-binding transactivator. J Biol Chem 270: 4875-4881. 31. Ritchie SA, Pasha MK, Batten DJ, Sharma RK, Olson DJ, et al. (2003) Identification of the SRC pyrimidine-binding protein (SPy) as hnRNP K: implications in the regulation of SRC1A transcription. Nucleic Acids Res 31: 1502-1513. 32. Lynch M, Chen L, Ravitz MJ, Mehtani S, Korenblat K, et al. (2005) hnRNP K binds a core polypyrimidine element in the eukaryotic translation initiation factor 4E (eIF4E) promoter, and its regulation of eIF4E contributes to neoplastic transformation. Mol Cell Biol 25: 6436-6453. 33. Li H, Liu J (2010) Identification of heterogeneous nuclear ribonucleoprotein K as a transactivator for human low density lipoprotein receptor gene transcription. J Biol Chem 285: 17789-17797. 34. Takimoto M, Tomonaga T, Matunis M, Avigan M, Krutzsch H, et al. (1993) Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro. J Biol Chem 268: 18249-18258. 35. Sakai N, Sakamoto KQ, Fujita S, Ishizuka M (2009) The importance of heterogeneous nuclear ribonucleoprotein K on cytochrome P450 2D2 gene regulation: its binding is reduced in Dark Agouti rats. Drug Metab Dispos 37: 1703-1710. 36. Da Silva N, Bharti A, Shelley CS (2002) hnRNP-K and Pur(alpha) act together to repress the transcriptional activity of the CD43 gene promoter. Blood 100: 3536-3544. 37. Du Q, Melnikova IN, Gardner PD (1998) Differential effects of heterogeneous nuclear ribonucleoprotein K on Sp1- and Sp3-mediated transcriptional activation of a neuronal nicotinic acetylcholine receptor promoter. J Biol Chem 273: 19877-19883. 38. Stains JP, Lecanda F, Towler DA, Civitelli R (2005) Heterogeneous nuclear ribonucleoprotein K represses transcription from a cytosine/thymidine-rich element in the osteocalcin promoter. Biochem J 385: 613-623. 39. Lee MH, Mori S, Raychaudhuri P (1996) trans-Activation by the hnRNP K protein involves an increase in RNA synthesis from the reporter genes. J Biol Chem 271: 3420-3427. 40. Lin JY, Li ML, Huang PN, Chien KY, Horng JT, et al. (2008) Heterogeneous nuclear ribonuclear protein K interacts with the enterovirus 71 5' untranslated region and participates in virus replication. J Gen Virol 89: 2540-2549. 41. Mukhopadhyay NK, Kim J, Cinar B, Ramachandran A, Hager MH, et al. (2009) Heterogeneous nuclear ribonucleoprotein K is a novel regulator of androgen receptor translation. Cancer Res 69: 2210-2218. 42. Ostareck DH, Ostareck-Lederer A, Wilm M, Thiele BJ, Mann M, et al. (1997) mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end. Cell 89: 597-606. 43. Skalweit A, Doller A, Huth A, Kahne T, Persson PB, et al. (2003) Posttranscriptional control of renin synthesis: identification of proteins interacting with renin mRNA 3'-untranslated region. Circ Res 92: 419-427. 44. Ostrowski J, Klimek-Tomczak K, Wyrwicz LS, Mikula M, Schullery DS, et al. (2004) Heterogeneous nuclear ribonucleoprotein K enhances insulin-induced expression of mitochondrial UCP2 protein. J Biol Chem 279: 54599-54609. 45. Thyagarajan A, Szaro BG (2004) Phylogenetically conserved binding of specific K homology domain proteins to the 3'-untranslated region of the vertebrate middle neurofilament mRNA. J Biol Chem 279: 49680-49688. 46. Yano M, Okano HJ, Okano H (2005) Involvement of Hu and heterogeneous nuclear ribonucleoprotein K in neuronal differentiation through p21 mRNA post-transcriptional regulation. J Biol Chem 280: 12690-12699. 47. Lee PT, Liao PC, Chang WC, Tseng JT (2007) Epidermal growth factor increases the interaction between nucleolin and heterogeneous nuclear ribonucleoprotein K/poly(C) binding protein 1 complex to regulate the gastrin mRNA turnover. Mol Biol Cell 18: 5004-5013. 48. Shanmugam N, Reddy MA, Natarajan R (2008) Distinct roles of heterogeneous nuclear ribonuclear protein K and microRNA-16 in cyclooxygenase-2 RNA stability induced by S100b, a ligand of the receptor for advanced glycation end products. J Biol Chem 283: 36221-36233. 49. Naarmann IS, Harnisch C, Flach N, Kremmer E, Kuhn H, et al. (2008) mRNA silencing in human erythroid cell maturation: heterogeneous nuclear ribonucleoprotein K controls the expression of its regulator c-Src. J Biol Chem 283: 18461-18472. 50. White MC, Gao R, Xu W, Mandal SM, Lim JG, et al. (2010) Inactivation of hnRNP K by expanded intronic AUUCU repeat induces apoptosis via translocation of PKCdelta to mitochondria in spinocerebellar ataxia 10. PLoS Genet 6: e1000984. 51. Expert-Bezancon A, Le Caer JP, Marie J (2002) Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken beta-tropomyosin pre-mRNA. J Biol Chem 277: 16614-16623. 52. Bomsztyk K, Van Seuningen I, Suzuki H, Denisenko O, Ostrowski J (1997) Diverse molecular interactions of the hnRNP K protein. FEBS Lett 403: 113-115. 53. Ostareck DH, Ostareck-Lederer A, Shatsky IN, Hentze MW (2001) Lipoxygenase mRNA silencing in erythroid differentiation: The 3'UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104: 281-290. 54. Evans JR, Mitchell SA, Spriggs KA, Ostrowski J, Bomsztyk K, et al. (2003) Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo. Oncogene 22: 8012-8020. 55. Laury-Kleintop LD, Gleason M, Tulenko TN (1999) Expression of the heterogenous nuclear ribonucleoprotein complex K protein and the prolyl-4-hydroxylase alpha-subunit in atherosclerotic arterial smooth muscle cells. Biochem Biophys Res Commun 260: 382-389. 56. Laury-Kleintop LD, Tresini M, Hammond O (2005) Compartmentalization of hnRNP-K during cell cycle progression and its interaction with calponin in the cytoplasm. J Cell Biochem 95: 1042-1056. 57. Balasubramani M, Day BW, Schoen RE, Getzenberg RH (2006) Altered expression and localization of creatine kinase B, heterogeneous nuclear ribonucleoprotein F, and high mobility group box 1 protein in the nuclear matrix associated with colon cancer. Cancer Res 66: 763-769. 58. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, et al. (2009) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem 81: 4493-4501. 59. Liu Q, Dreyfuss G (1995) In vivo and in vitro arginine methylation of RNA-binding proteins. Mol Cell Biol 15: 2800-2808. 60. Ostareck-Lederer A, Ostareck DH, Rucknagel KP, Schierhorn A, Moritz B, et al. (2006) Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src. J Biol Chem 281: 11115-11125. 61. Chiou YY, Lin WJ, Fu SL, Lin CH (2007) Direct mass-spectrometric identification of Arg296 and Arg299 as the methylation sites of hnRNP K protein for methyltransferase PRMT1. Protein J 26: 87-93. 62. Ostareck-Lederer A, Ostareck DH, Cans C, Neubauer G, Bomsztyk K, et al. (2002) c-Src-mediated phosphorylation of hnRNP K drives translational activation of specifically silenced mRNAs. Mol Cell Biol 22: 4535-4543. 63. Ostrowski J, Schullery DS, Denisenko ON, Higaki Y, Watts J, et al. (2000) Role of tyrosine phosphorylation in the regulation of the interaction of heterogenous nuclear ribonucleoprotein K protein with its protein and RNA partners. J Biol Chem 275: 3619-3628. 64. Mikula M, Karczmarski J, Dzwonek A, Rubel T, Hennig E, et al. (2006) Casein kinases phosphorylate multiple residues spanning the entire hnRNP K length. Biochim Biophys Acta 1764: 299-306. 65. Messias AC, Harnisch C, Ostareck-Lederer A, Sattler M, Ostareck DH (2006) The DICE-binding activity of KH domain 3 of hnRNP K is affected by c-Src-mediated tyrosine phosphorylation. J Mol Biol 361: 470-481. 66. Habelhah H, Shah K, Huang L, Ostareck-Lederer A, Burlingame AL, et al. (2001) ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation. Nat Cell Biol 3: 325-330. 67. Habelhah H, Shah K, Huang L, Burlingame AL, Shokat KM, et al. (2001) Identification of New JNK Substrate Using ATP Pocket Mutant JNK and a Corresponding ATP Analogue. Journal of Biological Chemistry 276: 18090-18095. 68. Schullery DS, Ostrowski J, Denisenko ON, Stempka L, Shnyreva M, et al. (1999) Regulated interaction of protein kinase Cdelta with the heterogeneous nuclear ribonucleoprotein K protein. J Biol Chem 274: 15101-15109. 69. Malik P, Clements JB (2004) Protein kinase CK2 phosphorylation regulates the interaction of Kaposi's sarcoma-associated herpesvirus regulatory protein ORF57 with its multifunctional partner hnRNP K. Nucleic Acids Res 32: 5553-5569. 70. Chen RQ, Yang QK, Lu BW, Yi W, Cantin G, et al. (2009) CDC25B mediates rapamycin-induced oncogenic responses in cancer cells. Cancer Res 69: 2663-2668. 71. Nagano K, Shinkawa T, Mutoh H, Kondoh O, Morimoto S, et al. (2009) Phosphoproteomic analysis of distinct tumor cell lines in response to nocodazole treatment. Proteomics 9: 2861-2874. 72. Bennetzen MV, Larsen DH, Bunkenborg J, Bartek J, Lukas J, et al. (2010) Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response. Mol Cell Proteomics 9: 1314-1323. 73. Park H, No AL, Lee JM, Chen L, Lee SY, et al. (2010) PDE4 inhibitor upregulates PTH-induced osteoclast formation via CRE-mediated COX-2 expression in osteoblasts. FEBS Lett 584: 173-180. 74. Kimura Y, Nagata K, Suzuki N, Yokoyama R, Yamanaka Y, et al. (2010) Characterization of multiple alternative forms of heterogeneous nuclear ribonucleoprotein K by phosphate-affinity electrophoresis. Proteomics 10: 3884-3895. 75. Li T, Evdokimov E, Shen RF, Chao CC, Tekle E, et al. (2004) Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis. Proc Natl Acad Sci U S A 101: 8551-8556. 76. Tan F, Lu L, Cai Y, Wang J, Xie Y, et al. (2008) Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells. Proteomics 8: 2885-2896. 77. Moumen A, Masterson P, O'Connor MJ, Jackson SP (2005) hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage. Cell 123: 1065-1078. 78. Smith WL, DeWitt DL, Garavito RM (2000) Cyclooxygenases: structural, cellular, and molecular biology. Annu Rev Biochem 69: 145-182. 79. Rouzer CA, Marnett LJ (2009) Cyclooxygenases: structural and functional insights. J Lipid Res 50 Suppl: S29-34. 80. Smith WL (2008) Nutritionally essential fatty acids and biologically indispensable cyclooxygenases. Trends Biochem Sci 33: 27-37. 81. Funk CD (2001) Prostaglandins and leukotrienes: advances in eicosanoid biology. Science 294: 1871-1875. 82. Kobayashi T, Narumiya S (2002) Function of prostanoid receptors: studies on knockout mice. Prostaglandins Other Lipid Mediat 68-69: 557-573. 83. Herschman HR (1996) Prostaglandin synthase 2. Biochim Biophys Acta 1299: 125-140. 84. Tanabe T, Tohnai N (2002) Cyclooxygenase isozymes and their gene structures and expression. Prostaglandins Other Lipid Mediat 68-69: 95-114. 85. Kang YJ, Mbonye UR, DeLong CJ, Wada M, Smith WL (2007) Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation. Prog Lipid Res 46: 108-125. 86. Zhang Y, Shaffer A, Portanova J, Seibert K, Isakson PC (1997) Inhibition of cyclooxygenase-2 rapidly reverses inflammatory hyperalgesia and prostaglandin E2 production. J Pharmacol Exp Ther 283: 1069-1075. 87. Samad TA, Moore KA, Sapirstein A, Billet S, Allchorne A, et al. (2001) Interleukin-1beta-mediated induction of Cox-2 in the CNS contributes to inflammatory pain hypersensitivity. Nature 410: 471-475. 88. Leahy KM, Ornberg RL, Wang Y, Zweifel BS, Koki AT, et al. (2002) Cyclooxygenase-2 inhibition by celecoxib reduces proliferation and induces apoptosis in angiogenic endothelial cells in vivo. Cancer Res 62: 625-631. 89. Sinicrope FA (2006) Targeting cyclooxygenase-2 for prevention and therapy of colorectal cancer. Mol Carcinog 45: 447-454. 90. Yamamoto M, Sato S, Hemmi H, Uematsu S, Hoshino K, et al. (2003) TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat Immunol 4: 1144-1150. 91. Jiang Z, Georgel P, Du X, Shamel L, Sovath S, et al. (2005) CD14 is required for MyD88-independent LPS signaling. Nat Immunol 6: 565-570. 92. Takeda K, Akira S (2004) TLR signaling pathways. Semin Immunol 16: 3-9. 93. Barton GM, Medzhitov R (2003) Toll-like receptor signaling pathways. Science 300: 1524-1525. 94. Hwang D (2001) Modulation of the expression of cyclooxygenase-2 by fatty acids mediated through toll-like receptor 4-derived signaling pathways. FASEB J 15: 2556-2564. 95. Caivano M, Gorgoni B, Cohen P, Poli V (2001) The induction of cyclooxygenase-2 mRNA in macrophages is biphasic and requires both CCAAT enhancer-binding protein beta (C/EBP beta ) and C/EBP delta transcription factors. J Biol Chem 276: 48693-48701. 96. Gorgoni B, Caivano M, Arizmendi C, Poli V (2001) The transcription factor C/EBPbeta is essential for inducible expression of the cox-2 gene in macrophages but not in fibroblasts. J Biol Chem 276: 40769-40777. 97. Kang YJ, Wingerd BA, Arakawa T, Smith WL (2006) Cyclooxygenase-2 gene transcription in a macrophage model of inflammation. J Immunol 177: 8111-8122. 98. Chen CY, Shyu AB (1994) Selective degradation of early-response-gene mRNAs: functional analyses of sequence features of the AU-rich elements. Mol Cell Biol 14: 8471-8482. 99. Chen CY, Chen TM, Shyu AB (1994) Interplay of two functionally and structurally distinct domains of the c-fos AU-rich element specifies its mRNA-destabilizing function. Mol Cell Biol 14: 416-426. 100. Dixon DA, Kaplan CD, McIntyre TM, Zimmerman GA, Prescott SM (2000) Post-transcriptional control of cyclooxygenase-2 gene expression. The role of the 3'-untranslated region. J Biol Chem 275: 11750-11757. 101. Cok SJ, Morrison AR (2001) The 3'-untranslated region of murine cyclooxygenase-2 contains multiple regulatory elements that alter message stability and translational efficiency. J Biol Chem 276: 23179-23185. 102. Boutaud O, Dixon DA, Oates JA, Sawaoka H (2003) Tristetraprolin binds to the COX-2 mRNA 3' untranslated region in cancer cells. Adv Exp Med Biol 525: 157-160. 103. Dixon DA, Tolley ND, King PH, Nabors LB, McIntyre TM, et al. (2001) Altered expression of the mRNA stability factor HuR promotes cyclooxygenase-2 expression in colon cancer cells. J Clin Invest 108: 1657-1665. 104. Cok SJ, Acton SJ, Sexton AE, Morrison AR (2004) Identification of RNA-binding proteins in RAW 264.7 cells that recognize a lipopolysaccharide-responsive element in the 3-untranslated region of the murine cyclooxygenase-2 mRNA. J Biol Chem 279: 8196-8205. 105. Mukhopadhyay D, Houchen CW, Kennedy S, Dieckgraefe BK, Anant S (2003) Coupled mRNA stabilization and translational silencing of cyclooxygenase-2 by a novel RNA binding protein, CUGBP2. Mol Cell 11: 113-126. 106. Dixon DA, Balch GC, Kedersha N, Anderson P, Zimmerman GA, et al. (2003) Regulation of cyclooxygenase-2 expression by the translational silencer TIA-1. J Exp Med 198: 475-481. 107. Lasa M, Mahtani KR, Finch A, Brewer G, Saklatvala J, et al. (2000) Regulation of cyclooxygenase 2 mRNA stability by the mitogen-activated protein kinase p38 signaling cascade. Mol Cell Biol 20: 4265-4274. 108. Lasa M, Brook M, Saklatvala J, Clark AR (2001) Dexamethasone destabilizes cyclooxygenase 2 mRNA by inhibiting mitogen-activated protein kinase p38. Mol Cell Biol 21: 771-780. 109. Fernau NS, Fugmann D, Leyendecker M, Reimann K, Grether-Beck S, et al. (2010) Role of HuR and p38MAPK in ultraviolet B-induced post-transcriptional regulation of COX-2 expression in the human keratinocyte cell line HaCaT. J Biol Chem 285: 3896-3904. 110. Chakrabarty A, Tranguch S, Daikoku T, Jensen K, Furneaux H, et al. (2007) MicroRNA regulation of cyclooxygenase-2 during embryo implantation. Proc Natl Acad Sci U S A 104: 15144-15149. 111. Hall-Pogar T, Zhang H, Tian B, Lutz CS (2005) Alternative polyadenylation of cyclooxygenase-2. Nucleic Acids Res 33: 2565-2579. 112. Hall-Pogar T, Liang S, Hague LK, Lutz CS (2007) Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3'-UTR. RNA 13: 1103-1115. 113. Shao J, Sheng H, Inoue H, Morrow JD, DuBois RN (2000) Regulation of constitutive cyclooxygenase-2 expression in colon carcinoma cells. J Biol Chem 275: 33951-33956. 114. Rockwell P, Yuan H, Magnusson R, Figueiredo-Pereira ME (2000) Proteasome inhibition in neuronal cells induces a proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE(2). Arch Biochem Biophys 374: 325-333. 115. Figueiredo-Pereira ME, Li Z, Jansen M, Rockwell P (2002) N-acetylcysteine and celecoxib lessen cadmium cytotoxicity which is associated with cyclooxygenase-2 up-regulation in mouse neuronal cells. J Biol Chem 277: 25283-25289. 116. Mbonye UR, Wada M, Rieke CJ, Tang HY, Dewitt DL, et al. (2006) The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system. J Biol Chem 281: 35770-35778. 117. Bashkirov VI, Scherthan H, Solinger JA, Buerstedde JM, Heyer WD (1997) A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J Cell Biol 136: 761-773. 118. van Dijk E, Cougot N, Meyer S, Babajko S, Wahle E, et al. (2002) Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J 21: 6915-6924. 119. Sheth U, Parker R (2003) Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300: 805-808. 120. Cougot N, Babajko S, Seraphin B (2004) Cytoplasmic foci are sites of mRNA decay in human cells. J Cell Biol 165: 31-40. 121. Sheth U, Parker R (2006) Targeting of aberrant mRNAs to cytoplasmic processing bodies. Cell 125: 1095-1109. 122. Brengues M, Teixeira D, Parker R (2005) Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 310: 486-489. 123. Bhattacharyya SN, Habermacher R, Martine U, Closs EI, Filipowicz W (2006) Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 125: 1111-1124. 124. Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T (2002) The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8: 1489-1501. 125. Lykke-Andersen J (2002) Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol Cell Biol 22: 8114-8121. 126. Eulalio A, Rehwinkel J, Stricker M, Huntzinger E, Yang SF, et al. (2007) Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencing. Genes Dev 21: 2558-2570. 127. Parker R, Sheth U (2007) P bodies and the control of mRNA translation and degradation. Mol Cell 25: 635-646. 128. Thomas MG, Martinez Tosar LJ, Desbats MA, Leishman CC, Boccaccio GL (2009) Mammalian Staufen 1 is recruited to stress granules and impairs their assembly. J Cell Sci 122: 563-573. 129. Loschi M, Leishman CC, Berardone N, Boccaccio GL (2009) Dynein and kinesin regulate stress-granule and P-body dynamics. J Cell Sci 122: 3973-3982. 130. Buchan JR, Muhlrad D, Parker R (2008) P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 183: 441-455. 131. Kedersha N, Anderson P (2009) Regulation of translation by stress granules and processing bodies. Prog Mol Biol Transl Sci 90: 155-185. 132. Lin NY, Lin CT, Chen YL, Chang CJ (2007) Regulation of tristetraprolin during differentiation of 3T3-L1 preadipocytes. FEBS J 274: 867-878. 133. Lin NY, Lin CT, Chang CJ (2008) Modulation of immediate early gene expression by tristetraprolin in the differentiation of 3T3-L1 cells. Biochem Biophys Res Commun 365: 69-74. 134. Smith WL, Garavito RM, DeWitt DL (1996) Prostaglandin Endoperoxide H Synthases (Cyclooxygenases)-1 and −2. Journal of Biological Chemistry 271: 33157-33160. 135. Sataranatarajan K, Lee M-J, Mariappan MM, Feliers D (2008) PKCδ regulates the stimulation of vascular endothelial factor mRNA translation by angiotensin II through hnRNP K. Cell Signal 20: 969-977. 136. Naarmann IS, Harnisch C, Muller-Newen G, Urlaub H, Ostareck-Lederer A, et al. (2010) DDX6 recruits translational silenced human reticulocyte 15-lipoxygenase mRNA to RNP granules. RNA 16: 2189-2204. 137. Daikoku T, Hirota Y, Tranguch S, Joshi AR, DeMayo FJ, et al. (2008) Conditional loss of uterine Pten unfailingly and rapidly induces endometrial cancer in mice. Cancer Res 68: 5619-5627. 138. Surh YJ (2003) Cancer chemoprevention with dietary phytochemicals. Nat Rev Cancer 3: 768-780. 139. Wilgus TA, Koki AT, Zweifel BS, Kusewitt DF, Rubal PA, et al. (2003) Inhibition of cutaneous ultraviolet light B-mediated inflammation and tumor formation with topical celecoxib treatment. Mol Carcinog 38: 49-58. 140. Yip-Schneider MT, Barnard DS, Billings SD, Cheng L, Heilman DK, et al. (2000) Cyclooxygenase-2 expression in human pancreatic adenocarcinomas. Carcinogenesis 21: 139-146. 141. Muller-Decker K, Neufang G, Berger I, Neumann M, Marks F, et al. (2002) Transgenic cyclooxygenase-2 overexpression sensitizes mouse skin for carcinogenesis. Proc Natl Acad Sci U S A 99: 12483-12488. 142. Neufang G, Furstenberger G, Heidt M, Marks F, Muller-Decker K (2001) Abnormal differentiation of epidermis in transgenic mice constitutively expressing cyclooxygenase-2 in skin. Proc Natl Acad Sci U S A 98: 7629-7634. 143. Oshima H, Oshima M, Inaba K, Taketo MM (2004) Hyperplastic gastric tumors induced by activated macrophages in COX-2/mPGES-1 transgenic mice. EMBO J 23: 1669-1678. 144. Oshima M, Dinchuk JE, Kargman SL, Oshima H, Hancock B, et al. (1996) Suppression of intestinal polyposis in Apc delta716 knockout mice by inhibition of cyclooxygenase 2 (COX-2). Cell 87: 803-809. 145. Tiano HF, Loftin CD, Akunda J, Lee CA, Spalding J, et al. (2002) Deficiency of either cyclooxygenase (COX)-1 or COX-2 alters epidermal differentiation and reduces mouse skin tumorigenesis. Cancer Res 62: 3395-3401. 146. Howe LR, Chang SH, Tolle KC, Dillon R, Young LJ, et al. (2005) HER2/neu-induced mammary tumorigenesis and angiogenesis are reduced in cyclooxygenase-2 knockout mice. Cancer Res 65: 10113-10119. 147. Oyama K, Fujimura T, Ninomiya I, Miyashita T, Kinami S, et al. (2005) A COX-2 inhibitor prevents the esophageal inflammation-metaplasia-adenocarcinoma sequence in rats. Carcinogenesis 26: 565-570. 148. Tsujii M, DuBois RN (1995) Alterations in cellular adhesion and apoptosis in epithelial cells overexpressing prostaglandin endoperoxide synthase 2. Cell 83: 493-501. 149. Scorrano L, Penzo D, Petronilli V, Pagano F, Bernardi P (2001) Arachidonic acid causes cell death through the mitochondrial permeability transition. Implications for tumor necrosis factor-alpha aopototic signaling. J Biol Chem 276: 12035-12040. 150. Arico S, Pattingre S, Bauvy C, Gane P, Barbat A, et al. (2002) Celecoxib induces apoptosis by inhibiting 3-phosphoinositide-dependent protein kinase-1 activity in the human colon cancer HT-29 cell line. J Biol Chem 277: 27613-27621. 151. Liu CH, Chang SH, Narko K, Trifan OC, Wu MT, et al. (2001) Overexpression of cyclooxygenase-2 is sufficient to induce tumorigenesis in transgenic mice. J Biol Chem 276: 18563-18569. 152. Dube C, Rostom A, Lewin G, Tsertsvadze A, Barrowman N, et al. (2007) The use of aspirin for primary prevention of colorectal cancer: a systematic review prepared for the U.S. Preventive Services Task Force. Ann Intern Med 146: 365-375. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/65594 | - |
| dc.description.abstract | 當病原體感染發生在生物體中，許多細胞因子或即早基因，應迅速，準確地打開和關閉以進行免疫反應。嚴格地控制這些基因表現對預防免疫系統疾病是非常重要的。而利用RNA結合蛋白參與的轉錄後調控則是細胞用來操縱基因表達的策略之一。異質性核核糖核蛋白K，擁有三個可與RNA結合的KH（K-homology）結構域，並常涉及在調控後轉錄和轉譯的過程。為了研究hnRNP K在免疫反應中可能的功能，在脂多醣（LPS）處理過的小鼠RAW264.7巨噬細胞萃取物中以hnRNP K抗體進行RNA免疫沉澱。兩個即早基因：Tistetraproline（TTP）和腫瘤壞死因子- | zh_TW |
| dc.description.abstract | When pathogen infection occurrs in organism, many cytokines or immediate genes (IEGs) are rapidly and precisely expressed and/or repressed for performing immune responses. Tight control of these genes is very important for preventing immune disorders. Post-transcriptional regulation involving in trans-acting RNA-binding proteins is one of the favorite strategies of cells to manipulate gene expression. Heterogeneous nuclear ribonucleoprotein K (hnRNP K), containing three KH (K-homology) domains that mediate RNA binding, is involved in the regulation of post-transcription and translation processes. To study the possible functions of hnRNP K in immune response, I performed anti-hnRNP K RNA immunoprecipitation assay with cell extracts from lipopolysaccharide (LPS)-treated mouse RAW264.7 macrophages. Two IEGs, Tistetraproline (TTP) and Tumor necrosis factor | en |
| dc.description.provenance | Made available in DSpace on 2021-06-16T23:52:43Z (GMT). No. of bitstreams: 1 ntu-101-D94b46007-1.pdf: 2995327 bytes, checksum: d4f707b64c59947ce1300ae5490c759b (MD5) Previous issue date: 2012 | en |
| dc.description.tableofcontents | 口試委員會審定書 i
誌謝 ii 中文摘要 iv ABSTRACT vi CONTENTS viii LIST OF FIGURES xi LIST OF TABLES xii ABBREVIATIONS xiii INTRODUCTION 1 1. hnRNP K 1 2. The post-translational modification of hnRNP K 4 3. COX-2 6 4. Processing body (P-body) 10 MATERIAS AND METHODS 12 1. Plasmid Constructs 12 2. Cell Culture and Transfection 12 3. Cell Extract Preparation 13 4. Determination of mRNA half-life 13 5. RNA extraction and reverse transcription 14 6. Real-time PCR 14 7. SDS-PAGE and Western Blotting Analysis 15 8. RNA-immunoprecipitation (RNA-IP) 15 9. RNA pull-down assay 16 10. Dual-Luciferase reporter assay 16 11. shRNA 17 12. Lentiviral knockdown 17 13. Expression and Purification of Recombinant Protein 18 14. In Vitro Phosphorylation Assay 18 15. Coimmunoprecipitation (Co-IP) Assays 18 16. Indirect Immunofluorescence and Confocal Microscopy 19 17. Rabbit anti-Phospho-hnRNP K/Ser116 and Ser284 Antibody Generation 19 RESULTS 20 LPS induces COX-2 expression and modulates COX-2 mRNA stability in RAW264.7 cells. 20 COX-2 mRNA is identified as one of the hnRNP K binding targets in LPS activated RAW264.7 cells. 20 hnRNP K downregulated COX-2 3’UTR-containing luciferase activity. 21 hnRNP K plays distinct roles in modulating COX-2 mRNA stability during LPS-stimulation. 22 LPS-induced ERK-signaling phosphorylates Ser116 on hnRNP K 23 Phosphorylation of Ser116 on hnRNP K arises in cytoplasm. 25 Phosphorylation of Ser116 on hnRNP K regulates COX-2 mRNA stability. 25 Phosphorylation of Ser116 is required for cytoplasmic localization of hnRNP K 26 hnRNP K interacts with DDX6, HuR and TTP 27 DDX6 is involved in the Ser116-mediated downregulation of COX-2 expression. 28 DISCUSSION 30 FIGURES 37 TABLE 64 REFERENCE 66 | |
| dc.language.iso | en | |
| dc.subject | 2、轉錄後調控。 | zh_TW |
| dc.subject | 脂多醣、巨噬細胞、RAW264.7 cell、異質性核核糖核蛋白K、環氧化酶 | zh_TW |
| dc.subject | LPS | en |
| dc.subject | macrophage | en |
| dc.subject | RAW264.7 | en |
| dc.subject | hnRNP K | en |
| dc.subject | COX-2 | en |
| dc.subject | post-transcriptional regulation | en |
| dc.title | 小鼠巨噬細胞RAW264.7中hnRNP K磷酸化對COX-2 mRNA穩定度的調控 | zh_TW |
| dc.title | The regulatory role of hnRNP K phosphorylation to COX-2 mRNA stability in mouse macrophage RAW264.7 cells | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 100-2 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 呂勝春,朱善德,李玉梅,譚賢明 | |
| dc.subject.keyword | 脂多醣、巨噬細胞、RAW264.7 cell、異質性核核糖核蛋白K、環氧化酶,2、轉錄後調控。, | zh_TW |
| dc.subject.keyword | LPS, macrophage, RAW264.7, hnRNP K, COX-2, post-transcriptional regulation, | en |
| dc.relation.page | 84 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2012-07-20 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科學研究所 | zh_TW |
| 顯示於系所單位： | 生化科學研究所 | |
文件中的檔案：
| 檔案 | 大小 | 格式 | |
|---|---|---|---|
| ntu-101-1.pdf 未授權公開取用 | 2.93 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。