Document Type : Research Articles
Authors
1
Department of Oral Biology, Faculty of Dentistry, Mahidol University, Bangkok, Yothi Road, Rajthewi District, Bangkok 10400, Thailand.
2
Department of Hematology, Faculty of Medical Technology, Rangsit University, 52/347 Muang-Ake, Phaholyothin Road, Lak-Hok, Muang Pathumthani, Pathumthani, 12000, Thailand.
3
Department of Oral and Maxillofacial Surgery, Faculty of Dentistry, Mahidol University, Bangkok, Yothi Road, Rajthewi District, Bangkok 10400, Thailand.
4
Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, Bangkok, 10400, Thailand.
5
Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Thailand Science Park, Phahonyotin Road, Klong 1, Khlong Luang, 12120, Pathum Thani, Thailand.
6
Laboratory of Pharmacology, Chulabhorn Research Institute, Bangkok, 10210, Thailand.
7
Center of Excellence on Environmental Health and Toxicology (EHT), Office of the Permanent Secretary (OPS), Ministry of Higher Education, Science, Research and Innovation (MHESI), Bangkok, 10400, Thailand.
Abstract
Objective: Ameloblastoma (AM) is a well-known benign odontogenic tumor recognized for its aggressive nature, believed to originate from tooth-forming tissue or the dental follicle (DF). Phosphoproteins are crucial for cellular signaling, enabling intracellular communication and regulating various physiological processes. In cancer, phosphoproteins are fundamental to both pathogenesis and pathophysiology. However, studies on phosphoproteins in AM are still limited. This study aimed to compare phosphoprotein profile and identify the crucial phosphoproteins between AM and DF. Methods: The phosphoprotein profiles of seven AM and five DF were discovered using mass spectrometry, and their associated phosphosites were examined by Netphos 3.1. Biological functions were analyzed by Metascape database. Results: Thirteen significant phosphoproteins were found in AM, and six in DF, all of which have phosphorylation sites. For example, among the proteins uniquely identified in AM were SENP1 (Sentrin-specific protease 1), DDX42 (ATP-dependent RNA helicase DDX42), LMBR1L (Protein LMBR1L), Cathepsin H (CATH), and Retinoblastoma-binding protein 5 (RBBP5), whereas those unique to DF included GC-rich sequence DNA-binding factor (GCF), Plexin-C1 (PLXC1), and proline/serine-rich coiled-coil protein 1 (PSRC1), PTHD3 (Patched domain-containing protein 3), and TPC6B (Trafficking protein particle complex subunit 6B). For biological analysis, the enriched terms included processing of capped intron-containing pre-mRNA, signaling by rho GTPases, establishment of organelle localization, signaling by receptor tyrosine kinases and cell morphogenesis. Conclusion: These phosphoproteomic findings provide essential insights into the pathogenesis of AM and warrant further investigation. This is crucial for advancing our understanding of AM biology and identifying potential therapeutic targets.
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