Abstract
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.
Highlights
Protein phosphorylation is a posttranslational modification (PTM) carried out on tyrosine, threonine, and serine residues [1, 2], which regulates protein functions and signaling pathways that orchestrate a variety of cellular processes, such as cell growth, differentiation, and apoptosis [3,4,5,6]
The protein phosphorylation in serine residues leads to the formation of multimolecular signaling complexes that regulate diverse biological processes, for example, DNA processing and repair, apoptosis, cell division, proliferation, and differentiation; in pathological conditions such as tumorigenesis, abnormal serine phosphorylation may result in the deregulation of signaling pathways responsible of proliferation and apoptosis inhibition [9,10,11]
We focused in HSP27, Clusterin, Keratin 8 (KRT8), and Keratin 19 (KRT19) proteins, and we proposed that their phosphorylation in serine residues could be related in the progression to CC
Summary
Protein phosphorylation is a posttranslational modification (PTM) carried out on tyrosine, threonine, and serine residues [1, 2], which regulates protein functions and signaling pathways that orchestrate a variety of cellular processes, such as cell growth, differentiation, and apoptosis [3,4,5,6]. The use of western blot assays with antibodies against serine phosphorylation may allow the detection of phosphorylated proteins [12, 13], which can be identified by mass spectrometry (MS) Afterwards, antibodies against these phosphorylated proteins could be used to evaluate the changes in concentration and in phosphorylation states of them during cancer development [14,15,16]. The detection of these changes could be useful for therapeutic, diagnostic, and/or prognostic applications [17, 18]
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