- Volume 4 Issue 1
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A NELL-1 Binding Protein: Vimentin
- Chae, Hwa-Sung (Department of Orthodontics, The Institute of Oral Health Science, Samsung Medical Center, Sung kyunkwan University School of Medicine) ;
- Kim, Young-Ho (Department of Orthodontics, The Institute of Oral Health Science, Samsung Medical Center, Sung kyunkwan University School of Medicine)
- Received : 2011.02.04
- Accepted : 2011.04.20
- Published : 2011.06.30
Purpose: Craniosynostosis (CS), one of the most common congenital craniofacial deformities, is the premature closure of cranial sutures. NELL-1 is a novel molecule overexpressed during premature cranial suture closure in human CS. From a functional perspective, NELL-1 has been reported to accelerate chondrocyte maturation and modulate calvarial osteoblast differentiation and apoptosis pathways. The mechanism through which NELL-1 induces these phenomena, however, remains unclear. The purpose of this study is to identify the NELL-1 binding protein(s) through which the biologic mechanism of NELL-1 can be further investigated. Materials and Methods: Far-Western and Immunoprecipitation (IP) assays were performed, independently and in sequence, followed by mass spectrometry to identify the NELL-1 binding proteins. Reverse IP was used to verify and confirm candidate binding protein. Results: The only confirmative protein from current experimentation was vimentin. Vimentin is the major structural component of the intermediate filaments. Conclusion: The present study identified and confirmed vimentin as a NELL-1 binding protein, which opened up a new window to mechanistically facilitate studies on this CS-associated molecule.
NELL-1 protein;Vimentin;Far-Western blotting;Mass spectrometry
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