Phosphoprotein Profile of Ameloblastoma.

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.