成功大學博碩士論文系統

簡易檢索 / 詳目顯示

回結果列表

研究生：	劉揚民 Liu, Yang-Ming
論文名稱：	轉錄因子CCAAT/Enhancer Binding Protein Delta 與發炎因子Long Pentraxin 3之純化和結晶研究 Purification and Crystallization Studies of Transcription Factor CCAAT/Enhancer Binding Protein delta and Inflammatory Factor Long Pentraxin 3
指導教授：	羅玉枝 Lo, Yu-Chih
學位類別：	碩士 Master
系所名稱：	生物科學與科技學院 - 生物資訊與訊息傳遞研究所 Insitute of Bioinformatics and Biosignal Transduction
論文出版年：	2014
畢業學年度：	102
語文別：	英文
論文頁數：	75
中文關鍵詞：	PTX3 、CEBPD 、表達、純化、結晶
外文關鍵詞：	PTX3, CEBPD, Expression, purification, crystallization
相關次數：	點閱：59 下載：1
分享至:	分享至facebook 分享至twitter

查詢本校圖書館目錄查詢臺灣博碩士論文知識加值系統勘誤回報

中文摘要
Part A CEBPδ
轉錄因子CEBPδ已知參與細胞的分化，遷移，生長休止，增生與凋亡，CEBPδ的功能會因為細胞種類和刺激因子的不同而改變。實驗證實CEBPδ的大量表現會抑制多種癌腫瘤生長，另一方面CEBPδ也會因為其產生的發炎反應，讓多形性膠質母細胞瘤在缺氧環境下存活並轉移。先前的報導指出，CEBPδ N端上有許多轉譯後修飾的位置，並且需要與其他CEBP家族成員或相關蛋白形成二聚體才有正常功能，但詳細的原因和機制目前並不明白。我們的研究希望藉由得到CEBPδ的晶體並以X光繞射取得其結構資訊而能進一步解釋CEBPδ的控制機轉。我們設計了CEBPδ N端transactivation domain和C端bZip domain 與全長的重組蛋白，此三個重組蛋白均能被大量表達。其中CEBPδ全長重組蛋白因其親和力問題無法得到足量蛋白。Transactivation domain 則伴隨著非專一蛋白，且透過膠體滲透層析依然無法移除，最終我們使用利用離子交換的方式將其移除以得到純化蛋白，並且利用結晶條件篩選套件得到可能的結晶條件。針對這些條件進行最佳化期望得到CEBPδ transactivation domain 的結晶。在以膠體滲透層析的過程中，我們發現CEBPδ在缺乏C端bZIP功能域 (domain) 時可能會形成二聚體，進一步推測CEBPδ也會以N端和其他蛋白作用並形成二聚體。
Part B PTX3
PTX3已經被認為是一個發炎的標的因子，因為PTX3會辨認外來的病原 (pattern) 並引起免疫發炎反應。同時PTX3也以它的N端與C端功能域和許多的細胞激素作用，參與細胞凋亡，吞噬作用，補體 (complement)的傳統 (classic)、替代 (alternative)、凝集素 (lectin) 反應，血管新生等功能。當PTX3沉降到凋亡細胞 (apoptotic cell) 上，PTX3會召集C3與C4並進行接下來的補體反應，整個作用表達出一個"eat me"的訊號使得巨噬細胞吞食凋亡細胞。相反地，處於液體中的PTX3會抓住C3並阻止它沉降到凋亡細胞上作為一個抗凋亡的作用。雖然PTX3的SAXS結果提供了我們有關其粗略結構的訊息，但目前依然無法從SAXS的資料去解釋PTX3的對於凋亡細胞的雙重功能與其機轉，因此需要立體結構的資訊來進一步研究。我們設計了PTX3全長，N端，C端的重組蛋白。初步表達的結果顯示N端可溶，但全長與C端不可溶。透過膠體滲透層析純化之N端重組蛋白有特定的裂解現象，我們依然在解決此問題。已純化之PTX3雖有裂解之現象但蛋白穩定，故我們仍然進行結晶條件的篩選，希望透過最佳化形成PTX3 N端之結晶以提供更多結構之資訊。同時我們發現N端在溶液中可能形成一四聚體，此現象與真核生物之PTX3相同。C端與全長兩種重組蛋白會形成不可溶之包涵體 (inclusion body)。為了得到可溶的C端與全長重組蛋白，我們使用胍鹽酸 (GuHCl) 溶解包涵體而後透析取得可溶之蛋白，但由於蛋白的產量過低，故須提高產量方能進行結晶。而透過膠體滲透層析我們也發現C端可能與真核的PTX3相同形成2聚體，但全長 (full length) 卻只形成四聚體與真核的八聚體不同。需要更多的研究來解釋此結果是否與原核,真核生物之修飾系統有關和其對功能之影響。

Abstract
Part A: CEBPδ
Transcription factor CEBPδ is involved in cell differentiation, motility, growth arrest, proliferation, and cell death. Studies also suggested that CEBPδ functions differed depending on cell type and cellular context. CEBPδ has been proved as a tumor suppressor in some cancers, for example, in breast cancer. But CEBPδ also help glioblastoma cell’s survival by inflammation response and induce metastasis. Previous studies had reported CEBPδ has many posttranslational modification sites and need to form a dimer with other family member or different proteins for its function. But the detailed mechanism and function of these modifications and dimerization are still unknown. In our research we try to study and explain these mechanisms by crystallography and X-ray diffraction. So we made constructs including transactivation domain (5-186), bZip domain (190-270) and full length (5-270) of CEBPδ， and all these three proteins can be over expressed. We can’t get enough full length to crystallization because it’s poor binding affinity. Transactivation domain could be pulled down enough, but it contained nonspecific bond. Finally, we use ion exchange and gain pure protein, and screening them for potential condition of crystallization. Once optimize the potential condition it may form a crystal and provide more detail structure conformation. According to size-exclusion chromatography data, we found that CEBPδ without its bZIP domain still formed a homodimer. We supposed that besides bZIP domain, the N-terminus contributed a physical interaction to dimerization.
Part B PTX3
PTX3 has been considered as an inflammatory marker, because PTX3 can recognize the extracellular pathogens and induce inflammation response for immunity. And it interacts with many cytokines within its N-terminus or C-terminus. When PTX3 deposited onto apoptotic cell, it recruited the C3 and C4 on apoptotic cell. This process presents a “eat me” signal for macrophage. But the fluid phase PTX3 would inhibit the C3 deposition for an anti-apoptotic function. Although the SAXS data of PTX3 was reported, the mechanism of these functions can’t be solved, so it need structure study to provide more information. In our study, we made construct of full length (19-381), N-terminal domain (19-182), and C-terminal CRP like domain (180-381) of PTX3. The result of expression presented that the N-terminus from bacterias was soluble the same as form eukaryotic cell, but C-terminus and full length were insoluble. By purification experiment data, we supposed that the PTX3 N-terminus form a tetramer in solution like eukaryotic PTX3, and there was degradation which we still try to remove. Although the N-terminal recombinant protein had degraded, it was stable, so we still screened this protein with degradation, and try optimization for crystal which can provide more detail information of PTX3 mechanism. The full length and C-terminus formed inclusion body. We used Guanidinium-HCl to dissolve the inclusion body and used dialysis for gaining soluble protein. But the protein production was too low to crystallization. According to size-exclusion chromatography data of protein purified by dialysis, we suppose that the C-terminus form a dimer the same as in eukaryotic cell, but full length did not form a octmer. The different between prokaryotic and eukaryotic modification system could be a reason of this result.

Directory
Part A CCAAT/enhancer binding protein delta	1
Chaper1	Introduction	2
1.1	Transcription factor	2
1.2	CCAAT/enhancer-binding protein family	2
1.3	CCAAT/enhancer-binding protein δ	3
1.4	The functions of CEBPDδ in cancer	4
1.5	Aim of CEBPδ	5
Chaper2	Materials & Methods	7
2.1	Materials	7
2.1.1	Competent cells	7
2.1.2	Primers	7
2.1.3	Enzymes	7
2.1.4	Chemicals and reagents	8
2.1.5	Buffers and solutions	8
2.1.6	Kits	11
2.2	Methods	13
2.2.1	DNA Construction of expression vectors	13
2.2.2	Transformation and purification of proteins	13
2.2.3	Size-exclusion chromatography	14
2.2.4	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis	14
2.2.5	Ion exchange chromatography	14
2.2.6	Crystallization	15
Chaper3	Result	16
3.1	Reconstruction of CEBPδ	16
3.2	Expression and purification of CEBPδ	16
3.3	Optimization of CEBPδ expression condition and improvement of the purity	17
3.4	Crystallization of CEBPδ	18
Chaper4	Discussion	20
Part B Long Pentraxin3	23
Chaper1	Introduction	24
1.1	Pentraxin family	24
1.2	PTX3 is an inflammatory factor	24
1.3	PTX3 structure	25
1.4	Aim of PTX3	26
Chaper2	Materials & Methods	28
2.1	Materials	28
2.1.1	Competent cells	28
2.1.2	Primers	28
2.1.3	Enzymes	28
2.1.4	Chemicals and reagents	29
2.1.5	Buffers and solutions	30
2.1.6	Kits	33
2.2	Methods	34
2.2.1	DNA Construction	34
2.2.2	Transformation and purification of proteins	34
2.2.3	Size-exclusion chromatography	35
2.2.4	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis	35
2.2.5	Purification of expressed proteins from inclusion bodies	35
2.2.6	Crystallization	36
Chaper3	Results	38
3.1	Reconstruction of PTX3 expression vectors	38
3.2	Expression of PTX3 recombinant proteins	38
3.3	Expression and purification of PTX3N-his tag 182 (19-182)	39
3.4   Purification of soluble protein of the full-length and C-terminus of PTX3	39
3.5	Crystallization of PTX3	40
Chaper4	Discussion	42
Figures	52
Figure 1.1……………………………………………………...……………...51
Figure 1.2………………………………………………………………...…...52
Figure 2.1………………..................................................................................53
Figure 2.2……………………………………………………………………..54
Figure 2.3……………………………………………………………………..55
Figure 3.1……………………………………………………………………..56
Figure 3.2……………………………………………………………………..57
Figure 4……………………………………………………………………….58
Figure 5……………………………………………………………………….59
Figure 6……………………………………………………………………….60
Figure 7……………………………………………………………………….61
Figure 8……………………………………………………………………….62
Figure 9……………………………………………………………………….63
Figure 10……………………………………………………………………...64
Figure 11……………………………………………………………………...65
Figure 12.1……………………………………………………………………66
Figure 12.2……………………………………………………………………67
Figure 12.3……………………………………………………………………68
Figure 12.4……………………………………………………………………69
Figure 13……………………………………………………………………...70
Figure 14……………………………………………………………………...71
Figure 15……………………………………………………………………...72
Figure 16……………………………………………………………………...73
Figure 17……………………………………………………………………...74

                                    

Alles, V. V., B. Bottazzi, G. Peri, J. Golay, M. Introna and A. Mantovani (1994). "Inducible expression of PTX3, a new member of the pentraxin family, in human mononuclear phagocytes." Blood 84(10): 3483-3493.
Balamurugan, K., J. M. Wang, H. H. Tsai, S. Sharan, M. Anver, R. Leighty and E. Sterneck (2010). "The tumour suppressor C/EBPdelta inhibits FBXW7 expression and promotes mammary tumour metastasis." Embo j 29(24): 4106-4117.
Barresi, V., E. Vitarelli, S. Cerasoli and G. Barresi (2010). "The cell growth inhibitory transcription factor C/EBPdelta is expressed in human meningiomas in association with low histological grade and proliferation index." J Neurooncol 97(2): 233-240.
Baruah, P., I. E. Dumitriu, G. Peri, V. Russo, A. Mantovani, A. A. Manfredi and P. Rovere-Querini (2006). "The tissue pentraxin PTX3 limits C1q-mediated complement activation and phagocytosis of apoptotic cells by dendritic cells." J Leukoc Biol 80(1): 87-95.
Bezy, O., C. Elabd, O. Cochet, R. K. Petersen, K. Kristiansen, C. Dani, G. Ailhaud and E. Z. Amri (2005). "Delta-interacting protein A, a new inhibitory partner of CCAAT/enhancer-binding protein beta, implicated in adipocyte differentiation." J Biol Chem 280(12): 11432-11438.
Borrelli, S., D. Fanoni, D. Dolfini, D. Alotto, M. Ravo, O. M. Grober, A. Weisz, C. Castagnoli, E. Berti, M. A. Vigano and R. Mantovani (2010). "C/EBPdelta gene targets in human keratinocytes." PLoS One 5(11): e13789.
Bottazzi, B., C. Garlanda, A. Cotena, F. Moalli, S. Jaillon, L. Deban and A. Mantovani (2009). "The long pentraxin PTX3 as a prototypic humoral pattern recognition receptor: interplay with cellular innate immunity." Immunological Reviews 227(1): 9-18.
Bottazzi, B., V. Vouret-Craviari, A. Bastone, L. De Gioia, C. Matteucci, G. Peri, F. Spreafico, M. Pausa, C. D'Ettorre, E. Gianazza, A. Tagliabue, M. Salmona, F. Tedesco, M. Introna and A. Mantovani (1997). "Multimer formation and ligand recognition by the long pentraxin PTX3. Similarities and differences with the short pentraxins C-reactive protein and serum amyloid P component." J Biol Chem 272(52): 32817-32823.
Breviario, F., E. M. d'Aniello, J. Golay, G. Peri, B. Bottazzi, A. Bairoch, S. Saccone, R. Marzella, V. Predazzi and M. Rocchi (1992). "Interleukin-1-inducible genes in endothelial cells. Cloning of a new gene related to C-reactive protein and serum amyloid P component." Journal of Biological Chemistry 267(31): 22190-22197.
Cardinaux, J.-R., I. Allaman and P. J. Magistretti (2000). "Pro-inflammatory cytokines induce the transcription factors C/EBPβ and C/EBPδ in astrocytes." Glia 29(1): 91-97.
Cheng, Y. and G. Li (2012). "Role of the ubiquitin ligase Fbw7 in cancer progression." Cancer Metastasis Rev 31(1-2): 75-87.
Chiang, B. T., Y. W. Liu, B. K. Chen, J. M. Wang and W. C. Chang (2006). "Direct interaction of C/EBPdelta and Sp1 at the GC-enriched promoter region synergizes the IL-10 gene transcription in mouse macrophage." J Biomed Sci 13(5): 621-635.
Cooper, L. A., D. A. Gutman, C. Chisolm, C. Appin, J. Kong, Y. Rong, T. Kurc, E. G. Van Meir, J. H. Saltz, C. S. Moreno and D. J. Brat (2012). "The tumor microenvironment strongly impacts master transcriptional regulators and gene expression class of glioblastoma." Am J Pathol 180(5): 2108-2119.
Deban, L., S. Jaillon, C. Garlanda, B. Bottazzi and A. Mantovani (2011). "Pentraxins in innate immunity: lessons from PTX3." Cell and Tissue Research 343(1): 237-249.
Emsley, J., H. E. White, B. P. O'Hara, G. Oliva, N. Srinivasan, I. J. Tickle, T. L. Blundell, M. B. Pepys and S. P. Wood (1994). "Structure of pentameric human serum amyloid P component." Nature 367(6461): 338-345.
Fazzini, F., G. Peri, A. Doni, G. Dell'Antonio, E. D. Cin, E. Bozzolo, F. D'Auria, L. Praderio, G. Ciboddo, M. G. Sabbadini, A. A. Manfredi, A. Mantovani and P. R. Querini (2001). "PTX3 in small-vessel vasculitides: An independent indicator of disease activity produced at sites of inflammation." Arthritis & Rheumatism 44(12): 2841-2850.
Friedman, A. D. (2007). "Transcriptional control of granulocyte and monocyte development." Oncogene 26(47): 6816-6828.
Gao, H., G. Bryzgalova, E. Hedman, A. Khan, S. Efendic, J.-Å. Gustafsson and K. Dahlman-Wright (2006). "Long-Term Administration of Estradiol Decreases Expression of Hepatic Lipogenic Genes and Improves Insulin Sensitivity in ob/ob Mice: A Possible Mechanism Is through Direct Regulation of Signal Transducer and Activator of Transcription 3." Molecular Endocrinology 20(6): 1287-1299.
Goodman, A. R., T. Cardozo, R. Abagyan, A. Altmeyer, H. G. Wisniewski and J. Vilcek (1996). "Long pentraxins: an emerging group of proteins with diverse functions." Cytokine Growth Factor Rev 7(2): 191-202.
Grigoryan, G., A. W. Reinke and A. E. Keating (2009). "Design of protein-interaction specificity gives selective bZIP-binding peptides." Nature 458(7240): 859-864.
Hagedorn, M., M. Delugin, I. Abraldes, N. Allain, M. A. Belaud-Rotureau, M. Turmo, C. Prigent, H. Loiseau, A. Bikfalvi and S. Javerzat (2007). "FBXW7/hCDC4 controls glioma cell proliferation in vitro and is a prognostic marker for survival in glioblastoma patients." Cell Div 2: 9.
Ikezoe, T., S. Gery, D. Yin, J. O'Kelly, L. Binderup, N. Lemp, H. Taguchi and H. P. Koeffler (2005). "CCAAT/Enhancer-Binding Protein δ: A Molecular Target of 1,25-Dihydroxyvitamin D3 in Androgen-Responsive Prostate Cancer LNCaP Cells." Cancer Research 65(11): 4762-4768.
Inforzato, A., C. Baldock, T. A. Jowitt, D. F. Holmes, R. Lindstedt, M. Marcellini, V. Rivieccio, D. C. Briggs, K. E. Kadler, A. Verdoliva, B. Bottazzi, A. Mantovani, G. Salvatori and A. J. Day (2010). "The Angiogenic Inhibitor Long Pentraxin PTX3 Forms an Asymmetric Octamer with Two Binding Sites for FGF2." J Biol Chem 285(23): 17681-17692.
Inforzato, A., G. Peri, A. Doni, C. Garlanda, A. Mantovani, A. Bastone, A. Carpentieri, A. Amoresano, P. Pucci, A. Roos, M. R. Daha, S. Vincenti, G. Gallo, P. Carminati, R. De Santis and G. Salvatori (2006). "Structure and function of the long pentraxin PTX3 glycosidic moiety: fine-tuning of the interaction with C1q and complement activation." Biochemistry 45(38): 11540-11551.
Inforzato, A., P. C. Reading, E. Barbati, B. Bottazzi, C. Garlanda and A. Mantovani (2013). "The “sweet” side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation." Frontiers in Immunology 3.
Inforzato, A., V. Rivieccio, A. P. Morreale, A. Bastone, A. Salustri, L. Scarchilli, A. Verdoliva, S. Vincenti, G. Gallo, C. Chiapparino, L. Pacello, E. Nucera, O. Serlupi-Crescenzi, A. J. Day, B. Bottazzi, A. Mantovani, R. De Santis and G. Salvatori (2008). "Structural Characterization of PTX3 Disulfide Bond Network and Its Multimeric Status in Cumulus Matrix Organization." J Biol Chem 283(15): 10147-10161.
Introna, M., V. V. Alles, M. Castellano, G. Picardi, L. De Gioia, B. Bottazzai, G. Peri, F. Breviario, M. Salmona, L. De Gregorio, T. A. Dragani, N. Srinivasan, T. L. Blundell, T. A. Hamilton and A. Mantovani (1996). "Cloning of mouse ptx3, a new member of the pentraxin gene family expressed at extrahepatic sites." Blood 87(5): 1862-1872.
Jaillon, S., G. Peri, Y. Delneste, I. Fremaux, A. Doni, F. Moalli, C. Garlanda, L. Romani, H. Gascan, S. Bellocchio, S. Bozza, M. A. Cassatella, P. Jeannin and A. Mantovani (2007). "The humoral pattern recognition receptor PTX3 is stored in neutrophil granules and localizes in extracellular traps." J Exp Med 204(4): 793-804.
Johnson, P. F. (2005). "Molecular stop signs: Regulation of cell-cycle arrest by C/EBP transcription factors." Journal of Cell Science 118(12): 2545-2555.
Ko, C.-Y., H.-C. Hsu, M.-R. Shen, W.-C. Chang and J.-M. Wang (2008). "Epigenetic Silencing of CCAAT/Enhancer-binding Protein δ Activity by YY1/Polycomb Group/DNA Methyltransferase Complex." J Biol Chem 283(45): 30919-30932.
Ko, C. Y., H. C. Hsu, M. R. Shen, W. C. Chang and J. M. Wang (2008). "Epigenetic silencing of CCAAT/enhancer-binding protein delta activity by YY1/polycomb group/DNA methyltransferase complex." J Biol Chem 283(45): 30919-30932.
Koschmieder, S., B. Halmos, E. Levantini and D. G. Tenen (2009). "Dysregulation of the C/EBPα differentiation pathway in human cancer." Journal of Clinical Oncology 27(4): 619-628.
Kovacs, K. A., M. Steinmann, P. J. Magistretti, O. Halfon and J. R. Cardinaux (2003). "CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation." J Biol Chem 278(38): 36959-36965.
Leali, D., R. Bianchi, A. Bugatti, S. Nicoli, S. Mitola, L. Ragona, S. Tomaselli, G. Gallo, S. Catello, V. Rivieccio, L. Zetta and M. Presta (2010). "Fibroblast growth factor 2-antagonist activity of a long-pentraxin 3-derived anti-angiogenic pentapeptide." J Cell Mol Med 14(8): 2109-2121.
Li, R., R. Strohmeyer, Z. Liang, L.-F. Lue and J. Rogers (2004). "CCAAT/enhancer binding protein δ (C/EBPδ) expression and elevation in Alzheimer’s disease." Neurobiology of Aging 25(8): 991-999.
Litvak, V., S. A. Ramsey, A. G. Rust, D. E. Zak, K. A. Kennedy, A. E. Lampano, M. Nykter, I. Shmulevich and A. Aderem (2009). "Function of C/EBPdelta in a regulatory circuit that discriminates between transient and persistent TLR4-induced signals." Nat Immunol 10(4): 437-443.
Liu, Y.-W., H.-P. Tseng, L.-C. Chen, B.-K. Chen and W.-C. Chang (2003). "Functional Cooperation of Simian Virus 40 Promoter Factor 1 and CCAAT/Enhancer-Binding Protein β and δ in Lipopolysaccharide-Induced Gene Activation of IL-10 in Mouse Macrophages." The Journal of Immunology 171(2): 821-828.
Liu, Y., M. R. Nonnemacher and B. Wigdahl (2009). "CCAAT/enhancer-binding proteins and the pathogenesis of retrovirus infection." Future Microbiology 4(3): 299-321.
Mantovani, A., C. Garlanda, B. Bottazzi, G. Peri, A. Doni, Y. Martinez de la Torre and R. Latini (2006). "The long pentraxin PTX3 in vascular pathology." Vascular Pharmacology 45(5): 326-330.
Maria Stella, C., L. Wei Keat, A. Mariano Javier, J. B. Robert, Z. Xudong, Y. S. Evan, P. S. Erik, L. A. Sandrine, D. Fiona, C. Howard, L. Anna, A. Ken, C. Andrea and I. Antonio (2009). "The transcriptional network for mesenchymal transformation of brain tumours." Nature 463(7279): 318-325.
Meruvu, S., L. Hugendubler and E. Mueller (2011). "Regulation of adipocyte differentiation by the zinc finger protein ZNF638." J Biol Chem 286(30): 26516-26523.
Morosetti, R., D. J. Park, A. M. Chumakov, I. Grillier, M. Shiohara, A. F. Gombart, T. Nakamaki, K. Weinberg and H. P. Koeffler (1997). "A novel, myeloid transcription factor, C/EBPξ, is upregulated during granulocytic, but not monocytic, differentiation." Blood 90(7): 2591-2600.
Narlikar, G. J., H. Y. Fan and R. E. Kingston (2002). "Cooperation between complexes that regulate chromatin structure and transcription." Cell 108(4): 475-487.
Natsuka, S., S. Akira, Y. Nishio, S. Hashimoto, T. Sugita, H. Isshiki and T. Kishimoto (1992). "Macrophage differentiation-specific expression of NF-IL6, a transcription factor for interleukin-6." Blood 79(2): 460-466.
Nauta, A. J., B. Bottazzi, A. Mantovani, G. Salvatori, U. Kishore, W. J. Schwaeble, A. R. Gingras, S. Tzima, F. Vivanco, J. Egido, O. Tijsma, E. C. Hack, M. R. Daha and A. Roos (2003). "Biochemical and functional characterization of the interaction between pentraxin 3 and C1q." Eur J Immunol 33(2): 465-473.
Nauta, A. J., M. R. Daha, C. van Kooten and A. Roos (2003). "Recognition and clearance of apoptotic cells: a role for complement and pentraxins." Trends Immunol 24(3): 148-154.
Nerlov, C. (2008). "C/EBPs: recipients of extracellular signals through proteome modulation." Current Opinion in Cell Biology 20(2): 180-185.
Nishioka, K., S. Ohshima, M. Umeshita-Sasai, N. Yamaguchi, T. Mima, S. Nomura, N. Murata, M. Shimizu, T. Miyake, K. Yoshizaki, M. Suemura, T. Kishimoto and Y. Saeki (2000). "Enhanced expression and DNA binding activity of two CCAAT/enhancer-binding protein isoforms, C/EBPβ and C/EBPδ, in rheumatoid synovium." Arthritis & Rheumatism 43(7): 1591-1596.
Palmieri, C., M. Monteverde, L. Lattanzio, O. Gojis, B. Rudraraju, M. Fortunato, N. Syed, A. Thompson, O. Garrone, M. Merlano, C. Lo Nigro and T. Crook (2012). "Site-specific CpG methylation in the CCAAT/enhancer binding protein delta (CEBPdelta) CpG island in breast cancer is associated with metastatic relapse." Br J Cancer 107(4): 732-738.
Presta, M., M. Camozzi, G. Salvatori and M. Rusnati (2007). "Role of the soluble pattern recognition receptor PTX3 in vascular biology." Journal of Cellular and Molecular Medicine 11(4): 723-738.
Ptashne, M. (1988). "How eukaryotic transcriptional activators work." Nature 335(6192): 683-689.
Ramji, D. and P. Foka (2002). "CCAAT/enhancer-binding proteins: structure, function and regulation." Biochem. J 365: 561-575.
Roman, C., J. S. Platero, J. Shuman and K. Calame (1990). "Ig/EBP-1: A ubiquitously expressed immunoglobulin enhancer binding protein that is similar to C/EBP and heterodimerizes with C/EBP." Genes and Development 4(8): 1404-1415.
Rovere, P., G. Peri, F. Fazzini, B. Bottazzi, A. Doni, A. Bondanza, V. S. Zimmermann, C. Garlanda, U. Fascio, M. G. Sabbadini, C. Rugarli, A. Mantovani and A. A. Manfredi (2000). "The long pentraxin PTX3 binds to apoptotic cells and regulates their clearance by antigen-presenting dendritic cells." Blood 96(13): 4300-4306.
Sanford, D. C. and J. W. DeWille (2005). "C/EBPδ is a downstream mediator of IL-6 induced growth inhibition of prostate cancer cells." The Prostate 63(2): 143-154.
Suzuki, S., Y. Takeishi, T. Niizeki, Y. Koyama, T. Kitahara, T. Sasaki, M. Sagara and I. Kubota (2008). "Pentraxin 3, a new marker for vascular inflammation, predicts adverse clinical outcomes in patients with heart failure." American Heart Journal 155(1): 75-81.
Takata, Y., Y. Kitami, Z.-H. Yang, M. Nakamura, T. Okura and K. Hiwada (2002). "Vascular Inflammation Is Negatively Autoregulated by Interaction Between CCAAT/Enhancer-Binding Protein-δ and Peroxisome Proliferator-Activated Receptor-γ." Circulation Research 91(5): 427-433.
Tang, D., G. S. Sivko and J. W. DeWille (2006). "Promoter methylation reduces C/EBPdelta (CEBPD) gene expression in the SUM-52PE human breast cancer cell line and in primary breast tumors." Breast Cancer Res Treat 95(2): 161-170.
Tengku-Muhammad, T. S., T. R. Hughes, H. Ranki, A. Cryer and D. P. Ramji (2000). "DIFFERENTIAL REGULATION OF MACROPHAGE CCAAT-ENHANCER BINDING PROTEIN ISOFORMS BY LIPOPOLYSACCHARIDE AND CYTOKINES." Cytokine 12(9): 1430-1436.
Thangaraju, M., M. Rudelius, B. Bierie, M. Raffeld, S. Sharan, L. Hennighausen, A.-M. Huang and E. Sterneck (2005). "C/EBPδ is a crucial regulator of pro-apoptotic gene expression during mammary gland involution." Development 132(21): 4675-4685.
van Rossum, A. P., F. Fazzini, P. C. Limburg, A. A. Manfredi, P. Rovere-Querini, A. Mantovani and C. G. Kallenberg (2004). "The prototypic tissue pentraxin PTX3, in contrast to the short pentraxin serum amyloid P, inhibits phagocytosis of late apoptotic neutrophils by macrophages." Arthritis Rheum 50(8): 2667-2674.
Volanakis, J. E. (2001). "Human C-reactive protein: expression, structure, and function." Molecular Immunology 38(2–3): 189-197.
Wang, J.-M., J. T. Tseng and W.-C. Chang (2005). "Induction of Human NF-IL6β by Epidermal Growth Factor Is Mediated through the p38 Signaling Pathway and cAMP Response Element-binding Protein Activation in A431 Cells." Molecular Biology of the Cell 16(7): 3365-3376.
Wang, J. M., C. Y. Ko, L. C. Chen, W. L. Wang and W. C. Chang (2006). "Functional role of NF-IL6beta and its sumoylation and acetylation modifications in promoter activation of cyclooxygenase 2 gene." Nucleic Acids Res 34(1): 217-231.
Wingfield, P. T., I. Palmer and S. M. Liang (2001). "Folding and purification of insoluble (inclusion body) proteins from Escherichia coli." Curr Protoc Protein Sci Chapter 6: Unit 6.5.
Zhang, J., L. Chang, C. Chen, M. Zhang, Y. Luo, M. Hamblin, L. Villacorta, J. W. Xiong, Y. E. Chen, J. Zhang and X. Zhu (2011). "Rad GTPase inhibits cardiac fibrosis through connective tissue growth factor." Cardiovasc Res 91(1): 90-98.
Zhang, Y., T. Liu, P. Yan, T. Huang and J. Dewille (2008). "Identification and characterization of CCAAT/Enhancer Binding proteindelta (C/EBPdelta) target genes in G0 growth arrested mammary epithelial cells." BMC Mol Biol 9: 83.

校內：2019-03-03公開
校外：不公開電子論文尚未授權公開，紙本請查館藏目錄

簡易檢索 / 詳目顯示

相關論文