Amelogenins: Multi-functional enamel matrix proteins and their binding partners

Naoto Haruyama, Junko Hatakeyama, Keiji Moriyama, Ashok B. Kulkarni

Research output: Contribution to journalReview article

6 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)257-266
Number of pages10
Journaljournal of oral biosciences
Volume53
Issue number3
DOIs
Publication statusPublished - 2011

Fingerprint

Amelogenin
Protein Binding
Tissue
Ameloblasts
Root Resorption
Dental Cementum
Periodontal Ligament
Enamels
Ligaments
Dental Enamel
enamel matrix proteins
Stomatognathic Diseases
Recombinant proteins
Two-Hybrid System Techniques
Extracellular Matrix Proteins
Periodontitis
Cell proliferation
Cell Lineage
Recombinant Proteins
Yeast

All Science Journal Classification (ASJC) codes

  • Medicine (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Dentistry(all)

Cite this

Amelogenins : Multi-functional enamel matrix proteins and their binding partners. / Haruyama, Naoto; Hatakeyama, Junko; Moriyama, Keiji; B. Kulkarni, Ashok.

In: journal of oral biosciences, Vol. 53, No. 3, 2011, p. 257-266.

Research output: Contribution to journalReview article

Haruyama, Naoto ; Hatakeyama, Junko ; Moriyama, Keiji ; B. Kulkarni, Ashok. / Amelogenins : Multi-functional enamel matrix proteins and their binding partners. In: journal of oral biosciences. 2011 ; Vol. 53, No. 3. pp. 257-266.
@article{625bcc05ed2d47ea8de7d997f34c721b,
title = "Amelogenins: Multi-functional enamel matrix proteins and their binding partners",
abstract = "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.",
author = "Naoto Haruyama and Junko Hatakeyama and Keiji Moriyama and {B. Kulkarni}, Ashok",
year = "2011",
doi = "10.2330/joralbiosci.53.257",
language = "English",
volume = "53",
pages = "257--266",
journal = "Journal of Oral Biosciences",
issn = "1349-0079",
publisher = "Japanese Association for Oral Biology",
number = "3",

}

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

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.

UR - http://www.scopus.com/inward/record.url?scp=80052716739&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80052716739&partnerID=8YFLogxK

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 -