TY - JOUR
T1 - Amelogenins
T2 - Multi-functional enamel matrix proteins and their binding partners
AU - Haruyama, Naoto
AU - Hatakeyama, Junko
AU - Moriyama, Keiji
AU - B. Kulkarni, Ashok
N1 - Funding Information:
We would like to acknowledge the great help pro-vided by the NIDCR DNA Sequencing Core. We would also like to thank Dr. Shin-ichi Harashima and Kiyoyuki Torigoe for their useful discussion and tech-nical advice regarding yeast screening. We would like to thank Taduru Sreenath for helpful discussions and Shelagh Powers for expert editorial assistance. These studies were supported by the Divi-sion of Intramural Research, NIDCR, NIH. We are also grateful for the grant given to us by the Japanese Ministry of Education, Global Center of Excellence (GCOE)Program, which supported our research.
PY - 2011
Y1 - 2011
N2 - Amelogenins are the most abundant extracellular matrix proteins secreted by ameloblasts during tooth development and are important for enamel formation. Recently, amelogenins have been detected not only in ameloblasts, which are differentiated from the epithelial cell lineage, but also in other tissues, including mesenchymal tissues at low levels, suggesting that amelogenins possess other functions in these tissues. The therapeutic application of an enamel matrix derivative rich in amelogenins resulted in the regeneration of cementum, alveolar bone, and periodontal ligament (PDL) in the treatment of experimental or human periodontitis, indicating the attractive potential of amelogenin in hard tissue formation. In addition, a full-length amelogenin (M180) and leucine-rich amelogenin peptide (LRAP) regulate cementoblast/PDL cell proliferation and migration in vitro. Interestingly, amelogenin null mice show increased osteoclasto-genesis and root resorption in periodontal tissues. Recombinant amelogenin proteins suppress osteoclasto-genesis in vivo and in vitro, suggesting that amelogenin is involved in preventing idiopathic root resorption. Amelogenins are implicated in tissue-specific epithelial-mesenchymal or mesenchymal-mesenchymal signaling ; however, the precise molecular mechanism has not been characterized. In this review, we first discuss the emerging evidence for the additional roles of M180 and LRAP as signaling molecules in mesenchymal cells. Next, we show the results of a yeast two-hybrid assay aimed at identifying protein-binding partners for LRAP We believe that gaining further insights into the signaling pathway modulated by the multifunctional amelogenin proteins will lead to the development of new therapeutic approaches for treating dental diseases and disorders.
AB - Amelogenins are the most abundant extracellular matrix proteins secreted by ameloblasts during tooth development and are important for enamel formation. Recently, amelogenins have been detected not only in ameloblasts, which are differentiated from the epithelial cell lineage, but also in other tissues, including mesenchymal tissues at low levels, suggesting that amelogenins possess other functions in these tissues. The therapeutic application of an enamel matrix derivative rich in amelogenins resulted in the regeneration of cementum, alveolar bone, and periodontal ligament (PDL) in the treatment of experimental or human periodontitis, indicating the attractive potential of amelogenin in hard tissue formation. In addition, a full-length amelogenin (M180) and leucine-rich amelogenin peptide (LRAP) regulate cementoblast/PDL cell proliferation and migration in vitro. Interestingly, amelogenin null mice show increased osteoclasto-genesis and root resorption in periodontal tissues. Recombinant amelogenin proteins suppress osteoclasto-genesis in vivo and in vitro, suggesting that amelogenin is involved in preventing idiopathic root resorption. Amelogenins are implicated in tissue-specific epithelial-mesenchymal or mesenchymal-mesenchymal signaling ; however, the precise molecular mechanism has not been characterized. In this review, we first discuss the emerging evidence for the additional roles of M180 and LRAP as signaling molecules in mesenchymal cells. Next, we show the results of a yeast two-hybrid assay aimed at identifying protein-binding partners for LRAP We believe that gaining further insights into the signaling pathway modulated by the multifunctional amelogenin proteins will lead to the development of new therapeutic approaches for treating dental diseases and disorders.
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U2 - 10.2330/joralbiosci.53.257
DO - 10.2330/joralbiosci.53.257
M3 - Review article
AN - SCOPUS:80052716739
VL - 53
SP - 257
EP - 266
JO - Journal of Oral Biosciences
JF - Journal of Oral Biosciences
SN - 1349-0079
IS - 3
ER -