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The article focuses on analyzing exclusive proteins associated with malignant phenotype acquisition in pleomorphic adenoma (PA), highlighting their structural and functional roles. Topics include the identification of exclusive proteins in PA, residual PA, and carcinoma ex pleomorphic adenoma (CXPA), their biological processes, and their potential implications in the pathogenesis of PA and CXPA.

Objective: To analyze the proteomic profile of salivary pleomorphic adenoma (PA) and carcinoma ex pleomorphic adenoma (CXPA) samples and correlate them with the malignant transformation of the PA. Materials and methods: Thirty samples (10 PA, 16 CXPA, and 4 residual PA) were microdissected and submitted to liquid chromatography‐tandem mass spectrometry (LC‐MS/MS). The proteomic data and protein identification were analyzed through LC‐MS/MS spectra using the MaxQuant software. Results: The proteomic analysis identified and quantified a total of 240 proteins in which 135 were found in PA, residual PA, and CXPA. The shared proteins were divided into six subgroups, and the proteins that showed statistically significant differences (p > 0.05) and fold‐change > or <2.5 in one subgroup to another subgroup were included. Seven proteins (Apolipoprotein A‐I—APOA1, haptoglobin—HP, protein of the synaptonemal complex 1—SYCP1, anion transport protein of band 3—SLC4A1, subunit μ1 of AP‐1 complex—AP1M1, beta subunit of hemoglobin—HBB, and dermcidin—DCD) were classified as potential protein signatures, being HP, AP1M1, and HBB with higher abundance for PA to residual PA, APOA1 with higher abundance for PA to CXPA, SLC4A1 with lower abundance in the PA to CXPA, SYCP1with lower abundance for residual PA to CXPA, and DCD with higher abundance in the CXPA with epithelial differentiation to myoepithelial differentiation. Conclusions: In this work, we demonstrated the comparative proteomic profiling of PA, residual PA, and CXPA, and seven were proposed as protein signatures, some of which may be associated with the malignant phenotype acquisition. [ABSTRACT FROM AUTHOR]

Osteopontin (OPN) is a calcium‐binding glycol‐phosphoprotein present in many physiologic and pathological processes. This protein can control bone cell adhesion, osteoclastic activity, and bone matrix mineralization. However, its participation in pathological processes such as atherosclerosis, sarcoidosis, tuberculosis, and cancer have been described. Some studies have shown that OPN may participate in the development and progression of oral cancer. Although the role of OPN in oral cancer is not fully understood, some studies have suggested that this protein may induce malignant phenotype of cells by activation of PI3K/AKT/mTOR pathway, which favors cell proliferation, invasion, metastasis, angiogenesis, and failure of treatment. This review discusses the possible mechanism of involvement of OPN in oral cancer and its potential clinical application in diagnosis and prognosis. [ABSTRACT FROM AUTHOR]