Data deposition: The nucleotide sequence of the African clawed frog (Xenopus laevis) DMP1 gene have been deposited in DDBJ under accession no. AB779761.
Identification, characterization, and expression of dentin matrix protein 1 gene in Xenopus laevis
Article first published online: 16 SEP 2013
© 2013 Wiley Periodicals, Inc.
Journal of Experimental Zoology Part B: Molecular and Developmental Evolution
Volume 320, Issue 8, pages 525–537, December 2013
How to Cite
2013. Identification, characterization, and expression of dentin matrix protein 1 gene in Xenopus laevis. J. Exp. Zool. (Mol. Dev. Evol.) 320B:525–537., , , , , , .
- Issue published online: 5 NOV 2013
- Article first published online: 16 SEP 2013
- Manuscript Accepted: 1 AUG 2013
- Manuscript Revised: 31 JUL 2013
- Manuscript Received: 5 APR 2013
- The Japan Society for the Promotion Science (JSPS), Grant-in-Aid for Challenging Exploratory Research. Grant Number: 24659918
Dentin matrix protein 1 (DMP1) is an acidic extracellular matrix protein expressed mainly in bone and dentin, and is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family. The DMP1 gene, however, appears to evolve rapidly in comparison with other SIBLING genes, even though such functionally important molecules usually evolve more slowly than less important ones. The purpose of this study was to identify and characterize an ortholog of the DMP1 gene in an amphibian (Xenopus laevis; X. laevis) to clarify molecular evolutionary alterations in DMP1 associated with calcified tissues in tetrapods. Furthermore, we analyzed the mRNA expression of this gene to elucidate its functional change in bone and developing tooth germ in comparison with amniote DMP1s. The similarities of the deduced amino acid sequence of X. laevis DMP1 to that of the corresponding amniote proteins were low, although they did share several unique features specific to DMP1 and have similar properties. Expression of X. laevis DMP1 mRNA was predominant in osteocytes and odontoblasts, but only transiently observed in ameloblasts, as in amniotes. These results suggest that DMP1 has conserved several functions during tetrapod evolution. This indicates that continuity of biochemical properties has been more important in maintaining DMP1 functionality than that of the sequence of amino acid residues, which has undergone change over the course of molecular evolution. J. Exp. Zool. (Mol. Dev. Evol.) 320B: 525–537, 2013. © 2013 Wiley Periodicals, Inc.