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Analysis of factors influencing reprogramming in cloned mammalian embryos by proteomic method
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哺乳動物之複製效率至今仍然不高，可能造成此低產製效率之因素很多，如供核細胞（donor cells）之種類、供核細胞與受核卵子（recipient oocytes）細胞週期之協調性、複製操作流程，以及未臻完善之體外培養系統等，都可能導致體細胞再程式化（reprogramming）不完全而無法產製複製動物。先前之研究發現，去核之成熟卵母細胞（metaphase II, MII）較原泡核期（germinal vesicle stage, GV stage）卵子或受精卵適於作為體細胞核移置（somatic cell nuclear transfer, SCNT）之受核卵子。因此，本研究之目的為利用蛋白質體學方法，比較位於不同細胞週期之卵子或細胞其蛋白質之差異性表現，以期找出可幫助供核細胞進行再程式化之可能因子，並比較分析蟾卵/蛋萃取物之蛋白質表現與其對已分化體細胞再程式化之影響。試驗一，從豬卵巢濾泡內取出原泡核期（germinal vesicle stage, GV stage）卵子，而部分GV卵子經體外成熟後可得成熟卵母細胞。將各300顆GV與MII期豬卵母細胞，經二維蛋白質聚丙烯醯胺膠體電泳法（two-dimensional polyacrylamide gel electrophoresis, 2D PAGE）分析與銀染（silver staining）呈色後，初步分析並取其中5個差異明顯之蛋白質點以胜肽質量指紋分析（peptide mass fingerprinting）進行身份鑑定，將所得到的質譜進入NCBInr資料庫比對後可鑑定4種蛋白質之身份，其分別為proliferating cell nuclear antigen（PCNA）、calreticulin（CRT）、kinase 5（RIPK 5）與apolipoprotein A-I（Apo A-I），其中PCNA在MII期表現量較高，而其他三種則在GV期有較高的表現量。試驗二，以秋水仙素（colchicine）過夜處理，使90%以上之小鼠NIH-3T3細胞與豬耳成纖維細胞（pig ear fibroblast, PEF）停留於M期，並與未經秋水仙素處理而90%以上停留於G1期之NIH-3T3與PEF，細胞分別以lysis buffer取得細胞蛋白質後進行2D PAGE分析與CBB (coomassie blue)染色。結果顯示，M期細胞之蛋白質表現明顯多於G1期細胞。試驗三，分別取出非洲爪蟾（Xenopus）卵/蛋之萃取物，並與經通透性處理（permeabilized）之小鼠NIH-3T3細胞共培養後，以免疫細胞螢光染色法觀察NIH-3T3細胞表現發育多能性標記（pluripotency marker）蛋白質Oct4，以及只表現於分化細胞之lamin A/C之情形。結果顯示，經蟾卵或蟾蛋萃取物共培養後之少部分細胞失去lamin A/C之表現，且部分細胞表現Oct4，證實蟾卵與蛋萃取物可幫助體細胞再程式化。因此，本研究分析所得之位於不同細胞週期之豬卵母細胞與體細胞差異表現之蛋白質，需進一步分析其對體細胞再程式化之影響，而蟾卵或蟾蛋萃取物中可調控體細胞再程式化之因子亦需再進一步分析。
The low efficiency in the production of cloned mammalian animals could be caused by the donor cell types, the cell cycle co-ordination between donor cells and recipient oocytes, the cloning procedure and defective culture system for cloned embryos. Any of thses would result in incomplete reprogramming of donor cells, and consequently failure of cloned animal production. It has been shown that the enucleated mature oocytes (the metaphase II stage, MII) are more suitable to be used as the recipient oocytes for somatic cell nuclear transfer (SCNT) to produce cloned mammalian animals than the enucleated immature oocytes at the germinal vesicle (GV) stage or zygotes are. Therefore, the aims of this study were to find out the protein molecules which might be involved in reprogramming by comparing the differential protein expressions in the oocytes/cells at different cell cycle stages. Additionally, the effect of Xenopus oocyte/egg extracts on the reprogramming was analysed. In Experiment 1, the porcine GV oocytes were aspirated from follicles on the ovaries collected from the local slaughter house. In vitro maturation was conducted to a part of the GV oocytes to obtain the mature oocyte. A total of 300 oocytes form each stage were subjected to proteomic analysis. Proteins were resolved by two-dimensional polyacrylamide gel electrophoresis (2D PAGE) and silver staining. Preliminary analysis revealed that there was a substantial difference in protein levels between the GV and MII stages. Five spots were chosen for protein identification using peptide mass fingerprinting, among which 4 spots were positively identified by searching the mass spectra against NCBInr database. The identified proteins were proliferating cell nuclear antigen (PCNA), calreticulin (CRT), kinase 5 (RIPK 5) and apolipoprotein A-I (Apo A-I). The expression level of PCNA was higher at the MII stage and the other three were higher at the GV stage. In Experiment 2, the mouse NIH-3T3 cells and pig ear fibroblasts (PEFs) treated with colchicines for overnight would result in more than 90% of the cells at the M phase, while most of the untreated cells would stay at the G1 phase. The cells at different cell cycle stages were lysed and subjected to 2D PAGE and coomassie blue staining. The results showed that the protein expression level in the cells was higher at the M phase than that at the G1 phase. In Experiment 3, the permeablilzed mouse NIH-3T3 cells were co-cultured with Xenopus oocyte/egg extracts. The expressions of pluripotency marker, Oct4 and lamin A/C which was expressed strictly in the differentiated cells were analyed by immunocytofluorescent staining. Although only few cells re-expressed Oct4 or lost the expression of lamin A/C, the reprogramming capability of Xenopus oocyte/egg extracts was approved. In conclusion, the effects of those identified proteins by comparison of oocytes or cells at the different cell cycles on reprogramming have to be further evaluated. Also, the factors in the Xenopus oocyte/egg extracts involved in reprogramming need to be analysed.
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