Comparative proteomic analysis of rat juvenile and adult dura  

作　　者：SONG Tao BI Nan PENG Zhe GUI Lai CHEN Bao-sheng 

机构地区：[1]Department of Craniomaxillofacial Surgery, Plastic Surgery Hospital, Chinese Academy of Medical Sciences, Beijing 100144, China [2]Department of Radiotherapy, Cancer Institute and Hospital, Chinese Academy of Medical Sciences, Beijing 100021, China [3]National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Beijing 100005, China

出　　处：《Chinese Medical Journal》2008年第18期1815-1820,共6页中华医学杂志（英文版）

摘　　要：Background It has been widely observed that infants and young children can reossify large calvarial defects when they are younger than 2 years of age; afterwards, they lose this regenerative potential. Previous studies have implicated that the dura mater serves as a key regulator of calvarial regeneration. However, the molecular mechanism of calvarial reossification remains elusive. Methods In order to identify the proteins that may participate in this process, we performed a proteome-wide comparison of the protein expression levels of immature and mature dura using 2D electrophoresis and MALDI-TOF mass spectrometry. The Western blotting was used to verify the results of the 2D electrophoresis/MALDI-TOF mass spectrometry. Results Eleven proteins were found to express with significant differences in the immature and the mature dura. Among them, the emergence of vimentin, tropomyosin, 13-actin and y-actin were further confirmed by the Western blotting analysis. Conclusion The proteins and proteomic profiles provide a better understanding of the molecular mechanism of calvarial regeneration.Background It has been widely observed that infants and young children can reossify large calvarial defects when they are younger than 2 years of age; afterwards, they lose this regenerative potential. Previous studies have implicated that the dura mater serves as a key regulator of calvarial regeneration. However, the molecular mechanism of calvarial reossification remains elusive. Methods In order to identify the proteins that may participate in this process, we performed a proteome-wide comparison of the protein expression levels of immature and mature dura using 2D electrophoresis and MALDI-TOF mass spectrometry. The Western blotting was used to verify the results of the 2D electrophoresis/MALDI-TOF mass spectrometry. Results Eleven proteins were found to express with significant differences in the immature and the mature dura. Among them, the emergence of vimentin, tropomyosin, 13-actin and y-actin were further confirmed by the Western blotting analysis. Conclusion The proteins and proteomic profiles provide a better understanding of the molecular mechanism of calvarial regeneration.

关 键 词：DURA PROTEOME two-dimensional difference gel electrophoresis 

分 类 号：R651.1[医药卫生—外科学]