細胞穿透性p53蛋白促進血癌細胞凋亡但具有血漿不穩定性

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研究生：	盧宗祺 Tsung-Chi Lu
論文名稱：	細胞穿透性p53蛋白促進血癌細胞凋亡但具有血漿不穩定性 Cell-penetrating p53 protein promotes leukemia cell apoptosis but is unstable in plasma
指導教授：	陳盛良 Shen-Liang Chen 劉俊揚 Jun-Yang Liou
口試委員:
學位類別：	博士 Doctor
系所名稱：	生醫理工學院 - 生命科學系 Department of Life Science
論文出版年：	2021
畢業學年度：	109
語文別：	英文
論文頁數：	141
中文關鍵詞：	p53 、血癌細胞、細胞穿透
外文關鍵詞：	p53, leukemia, Cell-penetrating
相關次數：	點閱：13 下載：0
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在人類的腫瘤細胞，特別是高級別癌症或轉移性腫瘤中，TP53基因的突變或缺陷尤為常見。p53是一個重要的轉錄因子，能調控細胞中許多基因的表現，其中其扮演抑癌基因的角色更是眾所矚目。p53蛋白可藉由參與控制細胞週期及促進細胞凋亡以預防細胞癌化的發生。因此，讓具突變型或缺陷型TP53基因的癌細胞重新獲得並恢復正常的 p53功能成為對抗癌症的一種積極性治療策略。在本研究中，我們開發一種重組的嵌合型p53蛋白，在其N端融合能促進轉錄活性的MyoD轉錄活化域，在其C端則鏈接具有細胞穿透能力的聚精氨酸多肽，並將其命名為M3-p53-R12 蛋白。該嵌合型p53蛋白以大腸桿菌作為表現宿主，並透過固定化金屬離子親和性層析法及透析取得重新折疊的蛋白質。研究證明，嵌合型p53蛋白具有穿過細胞膜並擁有遷移至細胞核的能力。此外該蛋白亦保留著p53蛋白的DNA結合及寡聚化等重要的轉錄因子特性。在細胞試驗中，嵌合型 p53 蛋白能抑制包含HL-60、Jurkat和K-562這三種血癌在內的多種TP53基因突變型腫瘤細胞的生長。在軟瓊脂細胞群落形成能力試驗表明嵌合型p53蛋白不僅能誘導血癌細胞的凋亡，還能抑制血癌細胞的生長。在Annexin V/PI 染色實驗中，更顯示嵌合型p53蛋白能選擇性誘導血癌細胞死亡，且不對間質幹細胞造成影響。這突顯出嵌合型p53蛋白具有選擇性對癌細胞造成傷害的能力。與此同時，我們成功建立了可用於研究嵌合型p53蛋白治療功效的異種血癌移植小鼠模型。然而，在嵌合型p53蛋白的血漿內代謝動力學研究中顯示，該蛋白對血漿中的蛋白酶非常敏感以致於其半衰期極短。這使得若想將嵌合型p53蛋白開發展成靜脈注射藥物，開發具有抗蛋白酶特性的次世代p53蛋白應為當務之急。

TP53 mutants or defectives are commonly occurred in tumor cells, especially metastatic tumors. p53 protein is the most famous transcription factor, which plays a tumor suppressor role in regulating the cell cycle and promoting apoptosis of cancer cells. Therefore, restoring normal p53 activity in TP53-mutant cancer cells may be an aggressive strategy against cancer. In this study, we designed a chimeric p53 protein which N-and C-terminal fused with MyoD transcriptional activation domain and poly-arginine cell-penetrating peptide respectively. The chimeric p53 protein used E. coli as the expression host and was obtained by immobilized metal ion chromatography purification followed by a serial refolding process. The purified chimeric p53 protein gain-of-function of cell-penetration and preserves abilities of DNA binding and oligomerization. In addition, the chimeric p53 protein, named M3-p53-R12 protein, suppressed the growth of human TP53-mutated tumor cell lines, including three hematopoietic malignancy cell lines, HL-60, Jurkat, and K-562. The soft-agar assay demonstrated that the chimeric p53 protein does not only induce apoptosis but also arrests the cell cycle of leukemia cell lines. The Annexin V/PI staining revealed that the chimeric p53 protein induces the death of leukemia cell lines but has no apoptotic effect on mesenchymal stem cells, highlighting its selective impact on normal and tumor cells. A leukemia xenograft murine model has also been successfully developed for investigated the in vivo efficacy of the chimeric p53 protein. However, the metabolism kinetics in plasma showed the rapid biodegradation of the chimeric p53 protein, suggesting prevent hydrolysis from serine protease of chimeric p53 in the future is imperative.

中文摘要    I
Abstract    II
Declaration    III
Acknowledgement    IV
Publications arising from this thesis    V
Table of Contents    VI
List of Figures    IX
List of Tables    X
Abbreviations    XI
Chapter I. General Introduction    1
1.1 General introduction to TP53 gene    1
1.1.1 The brief history of p53    1
1.1.2 The functional domain of p53    2
1.1.3 p53 maintains genomic integrity    3
1.1.4 Mutant TP53    4
1.1.5 p53 and zinc ions    5
1.1.6 Epithelial-mesenchymal transition and p53    6
1.1.7 p53 and hematologic malignancies    6
1.1.8 p53-related gene therapy    7
1.1.8.1 Gendicine    7
1.1.8.2 Oncorine (H101)    9
1.2 General introduction to traditional cancer therapy for hematologic malignancies    10
1.2.1 Radiotherapy    10
1.2.2 Chemotherapy    11
1.2.3 Targeted therapy    11
1.3 General introduction to modern cancer therapy for hematologic malignancies    12
1.3.1 Hematopoietic stem cell transplantation    12
1.3.2 Cellular therapy    12
1.3.3 Cell-based gene therapy    13
1.3.3.1 Zalmoxis    14
1.3.3.2 Kymriah (tisagenlecleucel)    15
1.3.3.3 Yescarta (Axicabtagene Ciloleucel; axi-cel)    17
1.3.3.4 Tecartus (brexucabtagene autoleucel)    18
1.3.3.5 Breyanzi (lisocabtagene maraleucel)    19
1.3.3.6 Abecma (Idecabtagene vicleucel)    19
1.4 Introduction to current in vitro cancer gene therapy products    20
1.4.1 Rexin-G    21
1.4.2 Imlygic (T-VEC)    22
1.4.3 Rigvir (ECHO-7)    24
1.5 Introduction to protein transduction platform    25
1.6 Aim of this thesis    26
Chapter II. Materials and methods    29
Plasmids    29
Cell Lines and cell culture    29
Protein expression and purification    30
Protein oligomerization assay    31
Electrophoretic mobility shift assay (EMSA)    31
M3-p53-R12 transduction ability and translocation analysis    32
MTT assay    32
Annexin V /PI apoptosis detection    33
Soft agar assay    33
Mesenchymal stem cell (MSC) isolation and culture    33
Pick up reporter stable clones from soft agar    34
Busulfex® conditioning in NOD-SCID mice    34
Statistical analysis    34
Chapter III. Results    36
3.1 Small scale expression and solubility test of chimeric p53 proteins    36
3.2 Purification strategy of chimeric proteins in this study    37
3.3 Characterization of the refolded M3-p53-R12 protein    37
3.3.1 No interchain disulfide bond was formed during the M3-p53-R12 protein purification    37
3.3.2 Purified M3-p53-R12 protein has oligomerization potency    38
3.3.3 Purified M3-p53-R12 protein retains its DNA binding ability    38
3.3.4 Purified M3-p53-R12 protein could penetrate through the cell membrane and import to the nucleus    39
3.3.5 Durable stability analysis of purified M3-p53-R12 protein    39
3.4 M3-p53-R12 protein is cytotoxicity to p53 mutant cancer cell line    40
3.5 M3-p53-R12 has cytotoxic effect on leukemia cell lines    41
3.6 M3-p53-R12 has an apoptotic effect on leukemia cell lines    42
3.7 M3-p53-R12 protein suppresses leukemia cell proliferation    42
3.8 M3-p53-R12 protein has no apoptotic effect on normal cells    43
3.9 Jurkat-GFP and K-562-GFP stable cell lines can be used for tracking    43
3.10 In vitro analysis of fluorescence leukemia cell lines for preliminary study    44
3.11 The hematopoietic malignancy xenograft mouse model had developed    45
3.12 M3-p53-R12 protein is highly sensitive to enzymes in the plasma    47
3.13 Proline-endopeptidase and thrombin may be involved in the degradation of M3-p53-R12 protein in plasma    47
Chapter IV. Discussion and Conclusion    49
References    58
Figures    75
Tables    113
Appendices    116
Appendix A. The brief timeline and main findings of the p53 research.    116
Appendix B. Schematic diagram for the location and functional domain of p53.    117
Appendix C. Schematic diagram for the functional domain and PTM sites of the p53 protein    118
Appendix D. Schematic diagram for the p53-MDM2 negative feedback loop    119
Appendix E. TP53 mutations prevalence in sporadic cancers    120
Appendix F. Global cancer statistical analysis in 2020    121
Appendix G. Protein identification report of the N-terminal peptide sequencing of purified protein fragments.    123


                                

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