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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 李明學 | |
dc.contributor.author | Cheng-Fan Lee | en |
dc.contributor.author | 李丞釩 | zh_TW |
dc.date.accessioned | 2021-06-17T07:06:11Z | - |
dc.date.available | 2019-12-31 | |
dc.date.copyright | 2019-08-27 | |
dc.date.issued | 2019 | |
dc.date.submitted | 2019-07-25 | |
dc.identifier.citation | 1 Abedin SA. C-reactive protein is significantly associated with prostate-specific antigen and metastatic disease in prostate cancer. BJU Int 2005; 96: 441; author reply 441.
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/72787 | - |
dc.description.abstract | 近年來臺灣攝護腺癌發生率持續攀高,直追歐美國家。儘管在早期診斷及治療方法的改善,根據美國癌症協會統計,在美國攝護腺癌每一年將造成30,000人死亡及新產生十倍於死亡人數的病歷。根據台灣癌症登錄平台數據,從2008到2014年間,攝護腺癌發生率一直維持在國人第五名,而死亡率則維持在7~8名間。攝護腺癌治療上的主要挑戰是如何克服抗藥性,抗賀爾蒙療法及惡化具轉移性的攝護腺癌。最新研究指出失調的男性賀爾蒙受體訊息,細胞周圍蛋白酶水解作用,發炎或血管新生作用,均是引起攝護腺癌惡化和轉移的主要原因。在抗賀爾蒙療法攝護腺癌腫瘤微環境中,一些發炎相關因子(如脂多醣)或脂肪代謝物(如溶血磷脂酸)常被發現有異常增高的現象,暗示著這些因子及相關代謝物可能參與抗賀爾蒙療法攝護腺癌的產生與促進此疾病的惡化。從臨床攝護腺癌病人的組織中發現高比率的攝護腺癌組織有格蘭氏陰性菌的感染,因此本篇研究進一步地探討格蘭氏陰性細菌產生的脂多醣是否會影響攝護腺癌細胞生長與移動侵襲能力與釐清其分子作用機制。結果發現在脂多醣的刺激下,能增進攝護腺癌細胞移動侵襲的能力。絲氨酸蛋白酶抑制劑能有效地抑制脂多醣所促進攝護腺癌細胞移動侵襲力,但金屬蛋白酶抑制劑較無此效果。初步結果指出絲氨酸蛋白酶在由脂多醣所促進攝護腺癌惡化過程中扮演重要角色。經質譜分析與生化相關研究,發現絲胺酸蛋白酶Matriptase (間質蛋白酶)在脂多醣刺激的攝護腺癌細胞中大量活化並釋放至細胞外並參與由脂多醣促進的攝護腺癌細胞侵襲能力。根據Matriptase活化的促進物中,我們發現到脂多醣刺激攝護腺癌細胞會提升此癌細胞分泌一種脂質結構的訊息傳遞分子鞘胺醇1-磷酸鹽 (Shingosine-1 phosphate, S1P) 至細胞外。在攝護腺癌細胞以及病人組織實驗中,脂多醣刺激會促進磷酸化鞘胺激酶移至細胞膜附近進而將其受質鞘胺醇磷酸化產生鞘胺醇1-磷酸鹽(S1P),並促進Matriptase的活化。由脂多醣所促進攝護腺癌細胞製造的鞘胺醇1-磷酸鹽(S1P)會透過自分泌及旁分泌的方法,活化鞘胺醇1-磷酸鹽的受體 [鞘胺醇1-磷酸鹽受體4 (S1PR4)],刺激癌細胞本身及鄰近周遭的細胞,以增進攝護腺癌細胞的侵襲轉移能力。同樣的現象我們也進一步在動物實驗中確認,當降低鞘胺激酶的表達,可壓制攝護腺癌腫瘤生長與轉移能力。另一方面,我們也分析病人組織切片,發現在具高表達SphK1的攝護腺癌病人,有較差的存活率。我們的結果指出脂多醣可促進鞘胺激酶移動至細胞膜,製造鞘胺醇1-磷酸鹽(S1P),經由鞘胺醇1-磷酸鹽受體4 (S1PR4)與間質蛋白酶活化,提升攝護腺癌細胞侵襲轉移能力。因此,此研究果指出鞘胺激酶未來可以當成一個研發藥物或治療策略的標靶目標,以達到抑制腫瘤生長與轉移的能力。 | zh_TW |
dc.description.abstract | Gram-negative bacteria have been found to be a major bacterial population in prostatitis and prostate cancer (PCa) tissues. A component of antigen in bacterial cell wall is lipopolysaccharide (LPS) which can act a stimulator in inflammation in some cancer types but has not been fully studied in PCa. In this study, we examined the effect of LPS on the invasion of PCa cells. Interestingly, LPS can enhance the invasiveness of PCa but had no significant effect on PCa cell viability. We reveal matriptase, a member of the membrane-anchored serine protease family, plays a key role in LPS-induced PCa cell invasion by using protease inhibitor screening and biochemical analyses. We further demonstrate Toll-like receptor 4 (TLR4, LPS receptor)- sphingosine kinase 1 (SphK1) signaling underlies LPS-induced matriptase activation and PCa cell invasion. Specifically, LPS induced the S225 phosphorylation of SphK1 and the translocation of SphK1 to plasma membrane, leading to the production of sphingosine 1-phosphate (S1P), ERK1/2 and matriptase activation via S1P receptor 4 (S1PR4). This phenomenon is further validated using patient-derived explant (PDE) model. Indeed, there is a significant correlation among the elevated SphK1 levels, the Gleason grades of PCa specimens and the poor survival of PCa patients. Taken together, this study demonstrates a potential impact of LPS on PCa progression. Our results provide a new finding of the role of bacterial infection in PCa progression and a potential therapeutic target(s) associated with PCa metastasis. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T07:06:11Z (GMT). No. of bitstreams: 1 ntu-108-D00442004-1.pdf: 4833420 bytes, checksum: 89fbd2751ab00ff1a026819dedbe79df (MD5) Previous issue date: 2019 | en |
dc.description.tableofcontents | Introduction 6
Section A: Prostate Cancer 6 A.1. Overview of importance of prostate cancer 6 A.2. Prostate organogenesis and tumorigenesis 7 A.3. Inflammation in prostate cancer 8 A.4. Baterial infection in prostate cancer 9 A.5. Prostate cancer diagnosis and treatment strategy 10 A.6. Metastatic prostate cancer 11 A.7. Serine protease in cancers 12 Section B: Lipopolysaccharide 14 B.1. Overview of Lipopolysaccharide 14 B.2. The role of LPS/TLR4 in cancers 15 Section C: Sphinogosine kinase (SphK) and Sphingosine 1-phosphate (S1P) 16 C.1. Overview of Sphingolipid and Sphingosine kinase 16 C.2. Sphingosine kinase 1 (SphK1) in cancers 18 C.3. Overview of Sphingosine 1-phosphate (S1P) and S1P receptors (S1PR) 20 C.4. Sphingosine 1-phosphate receptor (S1PR) in cancers 21 Materials and Methods 24 Cell culture 24 Treatment 24 Tumor Xenografts 24 Patient Derived Explants (PDE) 25 Cell Viability Assay 25 Serine Protease activity 26 Sliver Stain 26 Western Blot 27 Lentiviral Particle Preparation 28 Matriptase activity assay 28 Transfection 28 Site-directed Mutagenesis 28 Quantitative Real-Time PCR (QPCR) 29 ELISA 29 Immunofluorescence 30 Cell Migration, Invasion and Wounding Assay 30 Immunopreceptiation 31 Tissue Microarray 31 Clinical Database 32 Statistical analysis- 32 Results 33 Induction of Prostate Cancer Cell Migration and Invasion by LPS 33 Involvement of Matriptase in LPS-Induced PCa Cell Invasion 34 Involvement of Sphingosine 1-Phosphate and Sphingosine Kinase 1 in LPS-Induced Matriptase Activation and PCa Cell Invasion 35 LPS-Induced Phosphorylation at the Residue Serine 225 of SphK1 in an ERK Independent Manner 37 Involvement of S1P Receptor 4 in LPS-Induced Matriptase Activation and PCa Cell Invasion 40 Correlation of SphK1 Expression Levels with the Gleason Scores and Recurrence-Free Survival of PCa, as well as LPS-Induced SphK1 and Matriptase Activation in Clinical Patient Derived Explant (PDE) 41 SphK1 Contributed to PCa Metastasis to Lung in Mice 42 Discussion 44 Acknowledgments 53 Figures 54 Figure 1 CRP and TLR4 expression level in PCa cells. 54 Figure 2 LPS induces cell migration and invasion of prostate cancer cells by increasing serine protease activities. 56 Figure 3 Identification of matriptase to be involved in LPS-induced PCa cell invasion 58 Figure 4 Effect of LPS on matriptase in prostate cancer cells 60 Figure 5 LPS induced S1P production for PCa cell invasion. (A) ELISA analyses of S1P concentrations in the conditioned media of PC3 cells after 3-hour, 10 μg/ml LPS treatment. 61 Figure 6 Effect of Approtinin on S1P-induced cell invasion and S1P production in SphK1 knock-down PC3 cells. 64 Figure 7 Effects of LPS on the ERK, p38, JNK and Akt in PC3 cells. 65 Figure 8 LPS-induced phosphorylation at the residue serine 225 of SphK1 in an ERK-independent manner in PCa cells. 67 Figure 9 ERK is a downstream molecule of SphK1 after LPS treatment 70 Figure 10 Involvement of S1PR4 in LPS-induced matriptase activation and PCa cell invasion. 71 Figure 11 Examination of S1P receptor expression levels in different prostate cancer cells 73 Figure 12 SphK1 expression level in PCa cell lines and patient survival in SphK2 high/low groups 74 Figure 13 SphK1 expression correlated with PCa grades, poor survival of patients and cancer metastasis. 75 References 77 | |
dc.language.iso | en | |
dc.title | 脂多醣活化鞘氨醇激酶通過鞘氨醇激酶/鞘氨醇激酶受器4/第二型絲氨酸蛋白酶訊息傳遞進而促進前列腺癌細胞的侵襲和轉移 | zh_TW |
dc.title | Activation of Sphingosine Kinase by Lipopolysaccharide Promotes Prostate Cancer Cell Invasion and Metastasis via SphK1/S1PR4/Matriptase | en |
dc.type | Thesis | |
dc.date.schoolyear | 107-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 李心予,陳炳宏,賴志河,徐立中,黃祥博 | |
dc.subject.keyword | 攝護腺癌,轉移,脂多醣,絲胺酸蛋白?,鞘胺激?,鞘胺醇, | zh_TW |
dc.subject.keyword | Prostate cancer,LPS,Matriptase,Sphingosine,Shingosine-1 Phosphate,SphK1,S1PR4, | en |
dc.relation.page | 96 | |
dc.identifier.doi | 10.6342/NTU201901654 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2019-07-25 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 生物化學暨分子生物學研究所 | zh_TW |
顯示於系所單位: | 生物化學暨分子生物學科研究所 |
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