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Molecular Metabolism of Ameloblasts in Tooth Development
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Molecular Metabolism of Ameloblasts in Tooth Development

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 31 October 2024 | Viewed by 2603

Special Issue Editors

Dr. Maiko Suzuki

E-Mail Website
Guest Editor
Department of Oral Science and Translational Research, Cell Therapy Institute, Center for Collaborative Research, Nova Southeastern University, College of Dental Medicine, Fort Lauderdale, FL 33314, USA
Interests: periodontitis; periodontal bone resorption; fluoride toxicity; molecular biology; dentistry; tooth development; environmental health sciences
Dr. Yong Hee Patricia Chun

E-Mail Website
Guest Editor
Department of Periodontics, University of Texas Health Science Center San Antonio, San Antonio, TX 78229, USA
Interests: tooth development; ameloblasts; enamel; enamel proteins; molar-incisor hypomineralization; amelogenesis imperfecta; periodontium; periodontal attachment; periodontitis

Special Issue Information

Dear Colleagues,

Ameloblasts are the cells responsible for tooth enamel formation (called amelogenesis) and only present during tooth development. After protein secretion and enamel maturation, ameloblasts subsequently undergo apoptosis. The unique life cycle of ameloblasts is divided into sequential stages defined by cell morphology; however, the molecular mechanisms that govern each stage of amelogenesis are not fully understood.

We invite researchers studying the mechanisms and pathways of tooth enamel to contribute to this Special Issue, entitled "Molecular Metabolism of Ameloblasts in Tooth Development". The present topic aims to collect and disseminate original research papers, reviews, and case reports that provide new insights in the field of amelogenesis and enamel studies. Potential fields include, but are not limited to, the following: molecular mechanisms of metabolism, cell signaling pathways, genetic and epigenetic regulation of amelogenesis, enamel proteins (e.g., secreted calcium-binding phosphoproteins, SCPP) and related amelogenesis imperfecta (AI), ameloblast and enamel regeneration, tooth epithelial stem cells, enamel hypomineralization (dental fluorosis and molar incisor hypomineralization), and aberrant amelogenesis (e.g., ameloblastoma).

Dr. Maiko Suzuki
Dr. Yong Hee Patricia Chun
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • ameloblasts
  • amelogenesis
  • metabolism
  • gene regulation
  • amelogenesis imperfecta
  • SCPP
  • enamel hypomineralization
  • tooth epithelial stem cells

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Published Papers (2 papers)

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Research

16 pages, 16507 KiB  
Article
Fluoride Alters Gene Expression via Histone H3K27 Acetylation in Ameloblast-like LS8 Cells
by Shohei Yamashita, Motoki Okamoto, Melanie Mendonca, Natsumi Fujiwara, Eiko Kitamura, Chang-Sheng Sam Chang, Susanne Brueckner, Satoru Shindo, Nanako Kuriki, Marion A. Cooley, Navi Gill Dhillon, Toshihisa Kawai, John D. Bartlett, Eric T. Everett and Maiko Suzuki
Int. J. Mol. Sci. 2024, 25(17), 9600; https://doi.org/10.3390/ijms25179600 - 4 Sep 2024
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Abstract
Excessive fluoride ingestion during tooth development can cause dental fluorosis. Previously, we reported that fluoride activates histone acetyltransferase (HAT) to acetylate p53, promoting fluoride toxicity in mouse ameloblast-like LS8 cells. However, the roles of HAT and histone acetylation status in fluoride-mediated gene expression [...] Read more.
Excessive fluoride ingestion during tooth development can cause dental fluorosis. Previously, we reported that fluoride activates histone acetyltransferase (HAT) to acetylate p53, promoting fluoride toxicity in mouse ameloblast-like LS8 cells. However, the roles of HAT and histone acetylation status in fluoride-mediated gene expression remain unidentified. Here, we demonstrate that fluoride-mediated histone modification causes gene expression alterations in LS8 cells. LS8 cells were treated with or without fluoride followed by ChIP-Seq analysis of H3K27ac. Genes were identified by differential H3K27ac peaks within ±1 kb from transcription start sites. The levels of mRNA of identified genes were assessed using rea-time PCR (qPCR). Fluoride increased H3K27ac peaks associated with Bax, p21, and Mdm2 genes and upregulated their mRNA levels. Fluoride decreased H3K27ac peaks and p53, Bad, and Bcl2 had suppressed transcription. HAT inhibitors (Anacardic acid or MG149) suppressed fluoride-induced mRNA of p21 and Mdm2, while fluoride and the histone deacetylase (HDAC) inhibitor sodium butyrate increased Bad and Bcl2 expression above that of fluoride treatment alone. To our knowledge, this is the first study that demonstrates epigenetic regulation via fluoride treatment via H3 acetylation. Further investigation is required to elucidate epigenetic mechanisms of fluoride toxicity in enamel development. Full article
(This article belongs to the Special Issue Molecular Metabolism of Ameloblasts in Tooth Development)
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16 pages, 16286 KiB  
Article
AMELX Mutations and Genotype–Phenotype Correlation in X-Linked Amelogenesis Imperfecta
by Shih-Kai Wang, Hong Zhang, Hua-Chieh Lin, Yin-Lin Wang, Shu-Chun Lin, Figen Seymen, Mine Koruyucu, James P. Simmer and Jan C.-C. Hu
Int. J. Mol. Sci. 2024, 25(11), 6132; https://doi.org/10.3390/ijms25116132 - 1 Jun 2024
Viewed by 990
Abstract
AMELX mutations cause X-linked amelogenesis imperfecta (AI), known as AI types IE, IIB, and IIC in Witkop’s classification, characterized by hypoplastic (reduced thickness) and/or hypomaturation (reduced hardness) enamel defects. In this study, we conducted whole exome analyses to unravel the disease-causing mutations for [...] Read more.
AMELX mutations cause X-linked amelogenesis imperfecta (AI), known as AI types IE, IIB, and IIC in Witkop’s classification, characterized by hypoplastic (reduced thickness) and/or hypomaturation (reduced hardness) enamel defects. In this study, we conducted whole exome analyses to unravel the disease-causing mutations for six AI families. Splicing assays, immunoblotting, and quantitative RT-PCR were conducted to investigate the molecular and cellular effects of the mutations. Four AMELX pathogenic variants (NM_182680.1:c.2T>C; c.29T>C; c.77del; c.145-1G>A) and a whole gene deletion (NG_012494.2:g.307534_403773del) were identified. The affected individuals exhibited enamel malformations, ranging from thin, poorly mineralized enamel with a “snow-capped” appearance to severe hypoplastic defects with minimal enamel. The c.145-1G>A mutation caused a -1 frameshift (NP_001133.1:p.Val35Cysfs*5). Overexpression of c.2T>C and c.29T>C AMELX demonstrated that mutant amelogenin proteins failed to be secreted, causing elevated endoplasmic reticulum stress and potential cell apoptosis. This study reveals a genotype–phenotype relationship for AMELX-associated AI: While amorphic mutations, including large deletions and 5′ truncations, of AMELX cause hypoplastic-hypomaturation enamel with snow-capped teeth (AI types IIB and IIC) due to a complete loss of gene function, neomorphic variants, including signal peptide defects and 3′ truncations, lead to severe hypoplastic/aplastic enamel (AI type IE) probably caused by “toxic” cellular effects of the mutant proteins. Full article
(This article belongs to the Special Issue Molecular Metabolism of Ameloblasts in Tooth Development)
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