Abstract
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. 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. Eleven proteins were found to express with significant differences in the immature and the mature dura. Among them, the emergence of vimentin, tropomyosin, beta-actin and gamma-actin were further confirmed by the Western blotting analysis. The proteins and proteomic profiles provide a better understanding of the molecular mechanism of calvarial regeneration.
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