近年來，PA與p8在細胞內的功能已逐漸被解構，其中較受矚目的是兩者皆具有抗細胞凋亡的活性，且根據文獻指出，PA是由111胺基酸所組成的酸性(pl=3.55)胜肽，分子量約12.5 kDa；p8則是由82個胺基酸所組成的小分子核蛋白，分子量約 8~9 kDa。兩者因分子總電荷相異，故彼此間會相互作用而形成穩定之複合體，並提升兩者抗細胞凋亡之活性；然而兩者彼此進行交互作用的位置所在至今尚未被任何研究證實。為了瞭解PA與p8間交互作用位置，本研究分別建構PA及p8或tPA及p8過度表現穩定轉殖細胞株，以免疫共沉澱法分析PA與p8間交互作用位置之所在，並以西方墨點法分析PA與p8共同表現時，胞內凋亡相關蛋白之表現。 Recently, the biological functions of prothymosin and p8 in cells have been gradually deconstructed. In particular, both protein possess anti-apoptotic activity. Prothymosin , a acidic (pl = 3.55) peptide, is composed of 111 amino acids and its molecular weight is about 12.5 kDa.; p8 is a nucleoprotein, is composed of 82 amino acids and its molecular weight is about 8 ~ 9 kDa. Due to the opposite net charge of both molecules, prothymosin and p8 may interact to form a stable complex and enhance their anti-apoptotic activity. However, the interaction sites of both molecules during complex formation has not yet been characterized, and this problem is also the main target in this study. To investigate the interaction site of PA and p8 during complex formation, stable cell lines that express full length prothymosin and p8 or truncated prothymosin and p8 have been established. Immunopreciptation was performed to characterize the interaction sites of prothymosin and p8. Western blotting analysis was also performed to analyze the expression profiles of apoptosis-related proteins within the constructed stable cell lines.
