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Çѱ¹ÇÏõȣ¼öÇÐȸ / v.36, no.3, 2003³â, pp.369-374
Proteomics¸¦ ÀÌ¿ëÇÑ ³»ºÐºñ°èÀå¾Ö¹°ÁúÀÎ nonylphenol¿¡ ³ëÃâµÈ ¹«´ç°³±¸¸®ÀÇ ´Ü¹éÁú ¹ßÇö ºñ±³ ¿¬±¸
( Proteomics of Liver Tissues of Bombina orientalis Following Exposure to Nonylphenol )
±èÈ£½Â;°è¸íÂù; ÇѾç´ëÇб³ ÀÚ¿¬°úÇдëÇÐ »ý¸í°úÇаú;ÇѾç´ëÇб³ ÀÚ¿¬°úÇдëÇÐ »ý¸í°úÇаú;
 
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³»ºÐºñ°èÀå¾Ö¹°Áú (ȯ°æÈ£¸£¸ó)ÀÇ ÀÏÁ¾ÀÎ ³ë´ÒÆä³î(nonylphenol, NP)¿¡ ÀÇÇÑ ¼ö¼­ ȯ°æ ³» »ýŵ¶¼º Æò°¡ÀÇ ÀÏȯÀ¸·Î Çѱ¹¿¡ ¼­½ÄÇÏ´Â ¹«´ç°³±¸¸® (Bombina orientalis) ¼öÄÆ¿¡¼­ NP¿¡ ÀÇÇÑ °£Á¶Á÷ ³» ¹ßÇö ´Ü¹éÁúÀÇ º¯È­¸¦ ÃßÀûÇÏ¿´´Ù. üÁß 10${pm}$0.1gÀÇ ¼öÄÆ ¹«´ç°³±¸¸®¿¡ NPÀ» 10mg/kg ³óµµ·Î º¹°­ ÁÖ»çÇÑ ÈÄ 48 ¹× 96½Ã°£ ÈÄ¿¡ °£À» ÀýÃë ÇÑ µÚ ¸¶¼âÇÏ¿© 2Â÷¿ø Àü±â¿µµ¿À» ¼öÇàÇÏ¿´´Ù. Coomassie brilliant blue·Î ¿°»öÇÑ gel »ó¿¡¼­ ÀüüÀûÀ¸·Î 50${sim}$60°³ Á¤µµÀÇ protein spotsÀ» È®ÀÎÇÒ ¼ö ÀÖ¾úÀ¸¸ç ´Ü¹éÁú spotsÀÇ º¯È­¸¦ ºñ±³ ºÐ¼®ÇÑ °á°ú NPó¸® 48½Ã°£ ÈÄ 8°³ÀÇ spotsÀÌ Áõ°¡ÇÑ ¹Ý¸é 12°³ÀÇ spotsÀÌ °¨¼ÒÇÏ¿´´Ù. 96½Ã°£ ÈÄ¿¡´Â 30°³ÀÇ spotsÀÌ Áõ°¡µÇ¾ú°í 8°³ÀÇ spotsÀÌ °¨¼ÒÇÏ¿´´Ù. ÀüüÀûÀ¸·Î´Â ¾à20%Á¤µµÀÇ ´Ü¹éÁúÀÇ º¯È­°¡ ÀÖ¾ú´Ù. ´Ü¹éÁú ¹ßÇöÀÇ µ¿Å´ Åõ¿© ÈÄ 2ÀÏ ±îÁö´Â ´Ü¹éÁú »ý»êÀÌ ÀϽÃÀûÀ¸·Î °¨¼ÒÇÏÁö¸¸ ´Ù½Ã »õ·Î¿î ´Ü¹éÁúÀ» »ý¼ºÇÏ´Â °ÍÀ¸·Î »ç·áµÈ´Ù. NP ³ëÃâ¿¡ µû¸¥ ¹«´ç°³±¸¸® °£Á¶Á÷ ³» ´Ü¹éÁú ¹ßÇöÀÇ º¯È­´Â Çѱ¹ÀÇ ¼ö¼­È¯°æ¿¡¼­ ³»ºÐºñ°è Àå¾Ö¹°ÁúÀÇÀ§Çؼº Æò°¡¿¡ ¿ä±¸µÇ´Â ´Ü¹éÁú biomakerÀÇ °³¹ß¿¡ ÀÌ¿ë ÇÒ ¼ö ÀÖÀ» °ÍÀÌ´Ù.
Nonylphenol (NP), an well known aquatic contaminant, has been known to induce abnormalities in various aquatic animals. In an effort to develop proteome in the study of aquatic contamination of NP and its impact on the amphibia, protein changes in liver tissues of Korean red bellied frog, Bombina orientalis was investigated following the NP exposure. NP was administered intraperitoneally to male B. orientalis at 10 mg/kg body weight. At 48 and 96h after the treatment, the frog livers were sampled, and the protein fraction was separated using two dimensional gel electrophoresis (2D/E) and visualized with Coomassie brilluant blue staining. The 2D/E Images of the tissue from the animals treated with NP showed marked changes of protein spots (about 20% of total protein spots). Analysis of the 50-60 separated spots allowed identification of the major protein changes in the overall pattern for the stressor (NP) by time (0,48 and 96 h). At 48h after treatment, 8 spots were increased and 12 spots were reduced. Then, at 96h after treatment, 10 spots were increased and 8 spots were reduced. In total, approximately 29% of liver proteins showed the altered expression following the NP treatment. It is suggested that protein expression was repressed by blocking of certain metabolisms at 48 hand induced by the synthesis of new proteins for adaptation at 96 h following NP exposure. This application for 2D/E analysis may show promise in searching biomarkers for environmental proteomics in amphibians.
 
Ű¿öµå
2D/E;Nonylphenol;liver;Bombina orientalis;
 
Çѱ¹ÇÏõȣ¼öÇÐȸÁö / v.36, no.3, 2003³â, pp.369-374
Çѱ¹ÇÏõȣ¼öÇÐȸ
ISSN : 1976-8087
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200318317181664)
¾ð¾î : Çѱ¹¾î
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