Phosphoprotein Profile of Ameloblastoma
Issued Date
2025-08-01
Resource Type
eISSN
2476762X
Scopus ID
2-s2.0-105015275214
Pubmed ID
40849725
Journal Title
Asian Pacific Journal of Cancer Prevention APJCP
Volume
26
Issue
8
Start Page
3085
End Page
3091
Rights Holder(s)
SCOPUS
Bibliographic Citation
Asian Pacific Journal of Cancer Prevention APJCP Vol.26 No.8 (2025) , 3085-3091
Suggested Citation
Sanguansin S., Kengkarn S., Klongnoi B., Topanurak S., Roytrakul S., Chujan S., Kitkumthorn N. Phosphoprotein Profile of Ameloblastoma. Asian Pacific Journal of Cancer Prevention APJCP Vol.26 No.8 (2025) , 3085-3091. 3091. doi:10.31557/APJCP.2025.26.8.3085 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/112072
Title
Phosphoprotein Profile of Ameloblastoma
Corresponding Author(s)
Other Contributor(s)
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.