Protein Phosphorylation in Serine Residues Correlates with Progression from Precancerous Lesions to Cervical Cancer in Mexican Patients

• Published in: BioMed research international Vol. 2020; no. 2020; pp. 1 - 11
• Main Authors: Padilla-Mendoza, Juan Ramon, de Oca, Arturo Contis-Montes, Rodriguez, Mario Alberto, Lopez-Casamichana, Mavil, Bolanos, Jeni, Quintas-Granados, Laura Itzel, Reyes-Hernandez, Octavio Daniel, Fragozo-Sandoval, Fabiola, Resendiz-Albor, Aldo Arturo, Arellano-Gutierrez, Claudia Vanessa, Lopez-Reyes, Israel
• Format: Journal Article
• Language: English
• Published: Cairo, Egypt Hindawi Publishing Corporation 2020; Hindawi; John Wiley & Sons, Inc; Hindawi Limited
• Subjects: Adult; Apoptosis; Biological activity; Biomedical research; Cancer; Cancer patients; Cell division; Cervical cancer; Cervix Uteri - physiopathology; Cervix Uteri - virology; Clusterin - metabolism; Deregulation; Development and progression; Disease Progression; Ethanol; Female; Heat-Shock Proteins - metabolism; Human papillomavirus; Humans; Infections; Keratin-19 - metabolism; Keratin-8 - metabolism; Kinases; Lesions; Mass spectrometry; Membranes; Mexico; Middle Aged; Molecular Chaperones - metabolism; Papillomaviridae; Papillomavirus infections; Papillomavirus Infections - complications; Papillomavirus Infections - physiopathology; Papillomavirus Infections - virology; Phosphatase; Phosphorylation; Post-translational modification; Precancerous Conditions - virology; Proteins; Proteomics; Regulatory proteins; Residues; Scientific imaging; Serine; Serine - metabolism; Signaling; Squamous Intraepithelial Lesions of the Cervix - complications; Squamous Intraepithelial Lesions of the Cervix - physiopathology; Squamous Intraepithelial Lesions of the Cervix - virology; Structure-function relationships; Threonine; Threonine - metabolism; Tumorigenesis; Tyrosine; Uterine Cervical Neoplasms - complications; Uterine Cervical Neoplasms - physiopathology; Uterine Cervical Neoplasms - virology; Young Adult; Mexico; United States > US
• ISSN: 2314-6133; 2314-6141
• DOI: 10.1155/2020/5058928

Protein phosphorylation is a posttranslational modification that is essential for normal cellular processes; however, abnormal phosphorylation is one of the prime causes for alteration of many structural, functional, and regulatory proteins in disease conditions. In cancer, changes in the states of protein phosphorylation in tyrosine residues have been more studied than phosphorylation in threonine or serine residues, which also undergo alterations with greater predominance. In general, serine phosphorylation leads to the formation of multimolecular signaling complexes that regulate diverse biological processes, but in pathological conditions such as tumorigenesis, anomalous phosphorylation may result in the deregulation of some signaling pathways. Cervical cancer (CC), the main neoplasm associated with human papillomavirus (HPV) infection, is the fourth most frequent cancer worldwide. Persistent infection of the cervix with high-risk human papillomaviruses produces precancerous lesions starting with low-grade squamous intraepithelial lesions (LSIL), progressing to high-grade squamous intraepithelial lesions (HSIL) until CC is generated. Here, we compared the proteomic profile of phosphorylated proteins in serine residues from healthy, LSIL, HSIL, and CC samples. Our data show an increase in the number of phosphorylated proteins in serine residues as the grade of injury rises. These results provide a support for future studies focused on phosphorylated proteins and their possible correlation with the progression of cervical lesions.