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研究生:邱琦鑑
研究生(外文):Chi-Chien Chiu
論文名稱:香魚Pit-1基因的選殖,表現及其對生長激素基因的調控
論文名稱(外文):Cloning and Expression of Ayu (Plecoglossus altivelis) Pit-1 and Its Regulation on Growth Hormone Gene
指導教授:許宗雄許宗雄引用關係張繼堯張繼堯引用關係
指導教授(外文):Tzong-Hsiung HseuChi-Yao Chang
學位類別:博士
校院名稱:國立清華大學
系所名稱:生命科學系
學門:生命科學學門
學類:生物學類
論文種類:學術論文
論文出版年:2002
畢業學年度:90
語文別:英文
論文頁數:79
中文關鍵詞:生長激素香魚單株抗體
外文關鍵詞:growth hormonePit-1ayumonoclonal antibody
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腦下垂體專一性轉錄分子Pit-1屬於POU 功能區蛋白質家族,其在腦下垂體細胞的分化及生長激素、泌乳激素以及甲狀腺刺激激素的表現扮演重要角色。香魚完整的Pit-1 cDNA已選殖出來,核苷酸序列包含1910個鹼基對,其中開放讀架區佔1074 鹼基對,可轉譯出358個胺基酸,包含一個POU 特異功能區,一個POU相似功能區以及STA 異活化功能區。將轉譯區的DNA片段構築於pET-20b(+) 的質體轉形到大腸桿菌 [BL21 DE3(pLysS)]宿主表現,藉由IPTG的誘發得到重組蛋白,而此重組蛋白會堆積在大腸桿菌形成包含體,將此非溶性蛋白在變性的條件下經由單一步驟親合性層析純化出。此方法可在200 ml的細菌培養液中得到0.7 mg高純度且安定的重組蛋白,其分子量約40 kDa。此純化的重組蛋白可被其單株抗體認知,而且此單株抗體亦能認知正在發育中的腦下垂體細胞的細胞核,顯示此單株抗體能應用於組織學上Pit-1蛋白的偵測。比較香魚的Pit-1基因與鮭魚,火雞及鼠類的Pit-1基因結構,特別是在POU特異功能區及POU相似功能區仍保留高度的相似性,相反的,在異活化功能區則存在高度的變異性。比較結果發現在此三個物種中,有三個插入子的變異存在,且其變異是利用選擇性的剪切及不同的轉錄起始位置。在魚類Pit-1的插入子仍然高度保留於鳥類exon 2a,而此區域不存在於哺乳動物的Pit-1基因 ; 魚類Pit-1基因的插入子相似於鳥類Pit-1  的28個胺基酸插入子及哺乳動物Pit-1  的26個胺基酸插入子。有趣的是鳥類跟魚類都含有7個胺基酸的插入子,而此插入子不存在於哺乳動物Pit-1基因。藉由直接位置突變的技術,分別將, 及7個胺基酸插入子做不同組合的刪除,並將其送入NIH3T3細胞中表現,結果顯示, 及7個胺基酸的插入子對斑馬魚生長激素啟動子的調控是非常重要。香魚Pit-1基因的組織專一性及胚胎時期的表現模式也是很有趣的,藉由西方轉漬法檢視,發現Pit-1蛋白只表現在成魚的腦下垂體。而以西方轉漬法及RT-PCR技術檢視不同時期香魚胚胎,其蛋白質及mRNA首先在胚胎第四天被偵測到,並高度的表現在第五天且持續到孵化。
The pituitary specific transcription factor Pit-1 belongs to the family of POU domain proteins and is known to play an important role in the differentiation of pituitary cells and regulates the expression of growth hormone, prolactin and thyroid stimulating hormone- genes. The complete nucleotide sequence of cDNA encoding Pit-1 from amphidromous water fish, ayu (Plecoglossus altivelis) is reported here. Nucleotide sequence analysis of the 1910 bp of ayu Pit-1 cDNA revealed an open reading frame of 1074 bp that encodes a protein of 358 amino acids containing a POU-specific domain, POU-homeo domain and a STA (Ser/Thr-rich Activation) transactivation domain. Insertion of the coding region of Pit-1 cDNA, obtained by PCR, into a pET-20b(+) plasmid produce recombinant Pit-1 in E. coli BL21 (DE3) pLysS cells. Upon induction with isopropyl β-D-thiogalactopyranoside, Pit-1 was expressed and accumulated as inclusion bodies in E. coli. The protein was then purified in one-step purification by affinity chromatography on a nickel-nitrilotriacetic acid agarose column under denaturing conditions. This method yielded 0.7 mg of highly pure and stable protein per 200 ml of bacterial culture. A band of 40 kilodalton, resolved in recombinant ayu Pit-1 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, agrees well with the molecular mass calculated from the translated cDNA sequence. The purified recombinant Pit-1 was confirmed in vitro through Western blot analysis, using its monoclonal antibody. This monoclonal antibody detected Pit-1 in the nuclei of ayu developing pituitary by immunohistochemical reaction. It serves as a good reagent for the detection of ayu Pit-1 in situ. Comparison of ayu Pit-1 with that of salmon, turkey and rodent, revealed that the Pit-1 structure is highly conserved through vertebrates, especially in POU-specific and POU-homeo domains. The variation among fish, bird and mammal are mainly found in transactivation domain by alternative splicing and initiation. Three insertions were found. The -insert in fish Pit-1 is homologous to the exon 2a of avian Pit-1, which is not found in mammals. The -insert of fish Pit-1 is homologous to the 28 amino acids (a.a.) and 26 a.a. insert of avian Pit-1* and mammalian Pit-1, respectively. An additional similarity was noticed between fish and bird, as both of them contain 7 a.a. insert that is not present in mammalian Pit-1. By site directed mutagenesis, I demonstrated that the   and the 7 a.a. inserts of ayu Pit-1 are critical for activation of zebrafish growth hormone promoter. The tissue specificity and expression pattern of ayu Pit-1 is also interesting. The tissue specific expression of Pit-1 was detected in pituitary gland of adult ayu by Western blot analysis. To study the expression pattern of Pit-1 during development, ayu embryos from fertilization (day 1) through hatching (day 8) were collected daily for Western blot analysis and RT-PCR. Pit-1 transcripts could be detected as early as embryonic day 4, and significantly increased at embryonic day 5, then sustained to the time of hatching at day 8.
Contents
中文摘要 1
Abstract 3
1. Introduction 5
2. Materials and methods 11
2.1 Construction of ayu pituitary cDNA library 11
2.2 Isolation of ayu Pit-1 cDNA 11
2.3 Bacterial expression of recombinant ayu Pit-1 and plasmid construction 12
2.4 Preparation of monoclonal antibody 13
2.5 Enzyme linked immunosorbent assay 14
2.6 SDS-PAGE and Western blot 15
2.7 Immunohistochemistry 15
2.8 Experimental fish and cells 16
2.9 Fluorescent microscopic observation and imaging 17
2.10 Multisite-directed mutagenesis 17
2.11 Transient cotransfection analysis 18
2.12 RNA preparation, RT -PCR, Southern blotting and hybridization 18
2.13 Whole-mount in situ hybridization 19
2.14 Microinjection of zebrafish embryos 20
2.15 In vitro transcription and translation 20
3. Results 22
3.1 Cloning and characterization of ayu Pit-1 22
3.2 Comparison of the deduced amino acid sequence of ayu Pit-1 with that of other species 23
3.3 Expression and purification of recombinant ayu Pit-1 23
3.4 Enzyme linked immunosorbent assay 25
3.5 SDS-PAGE and Western blot analysis 25
3.6 Immunohistochemistry 25
3.7 Structure comparison of fish, bird and mammal Pit-1 variants 26
3.8 Activation of zebrafish GH promoter by ayu Pit-1 26
3.9 Domain analysis of ayu Pit-1 on zebrafish GH promoter 27
3.10 Tissue specific expression of ayu Pit-1 28
3.11 Appearance of Pit-1 during ayu development 28
3.12 NLS of Pit-1 is sufficient to direct green fluorescence protein to cell nucleus 29
3.13 Oct-1 could suppress Pit-1 activation on GH promoter 29
3.14 Expression pattern of zebrafish GH transcripts during embryonic stage 30
3.15 Cloning and characterization of grouper Pit-1 promoter 31
4. Discussion 33
5. Conclusion 39
6. References 40
7. Tables 50
Table 1 Purification of recombinant ayu Pit-1 by affinity chromatography on a nickel-nitrilotriacetic acid agarose column 50
Table 2 Oligonucleotide sequences designed for multisite-directed mutagenesis 51
Table 3 Sequence identity of ayu Pit-1 with that of Chinook salmon, rat, mouse and turkey 52
8. Figures 53
Figure 1 Nucleotide sequence of ayu Pit-1 cDNA 55
Figure 2 Comparison of deduced amino acid sequence 57
Figure 3 Pit-1 expression vector. A. PCR for ayu Pit-1 coding region 58
Figure 4 SDS-PAGE analysis of recombinant Pit-1 expression and purification 59
Figure 5 Western blot analysis 60
Figure 6 Immunohistochemistry of Pit-1 protein in the pituitary gland of ayu 61
Figure 7 Schematic comparison of Pit-1 gene between fish, bird and mammal 63
Figure 8 Transient transfection analysis of zebrafish GH promoter activity by ayu Pit-1 expression 64
Figure 9 Transcriptional activity of various ayu Pit-1 deletion clones on the 1.6 kb zebrafish GH promoter in NIH 3T3 cells 66
Figure 10 Western blot analysis of ayu Pit-1 from various tissues 67
Figure 11 RT-PCR analysis of Pit-1 gene during ayu embryonic development 68
Figure 12 SDS-PAGE and Western blot analysis of Pit-1 during ayu development 69
Figure 13 Functional analysis of the NLS (nucleus localization signal) from Pit-1 70
Figure 14 oct-1 could influence the transcriprional activation on zebrafish GH promoter activity in NIH3T3 cells 71
Figure 15 The appearance of GH gene during zebrafish embryogenesis 72
Figure 16 Expression pattern of GH in the zebrafish embryo 74
Figure 17 Nucleotide sequence of ayu Pit-1 promoter 77
Figure 18 Analysis for Pit-1 promoter activity, using luciferase reporter gene 78
Figure 19 Tissue specific expression of Pit-1 promoter using EGFP reporter gene 79
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