Abstract
E-cadherin, a transmembrane adhesion molecule, and phosphatase of regenerating liver 3 (PRL-3) protein, a member of the family of tyrosine phosphatases, seem to be responsible for cancer cell migration. Therefore, the study objective was to determine a correlation between PRL-3 and E-cadherin, to assess their expression in neoplastic tissue and normal mucosa of the stomach, to analyze their effect on cancer advancement, and to evaluate their potential as prognostic markers in gastric cancer. The expressions of PRL-3 and E-cadherin were assessed immunohistochemically in 71 patients with gastric cancer. Positive expression of PRL-3 was observed in 42.2 % of gastric cancer cases, whereas E-cadherin expression was abnormal in 38 % of cases. The study revealed that the positive PRL-3 expression and abnormal E-cadherin expression were associated with mucinous gastric carcinoma and lymph node involvement. The former was also related to the infiltrating type of tumor and abnormal E-cadherin expression. The expression of PRL-3, but not of E-cadherin, was associated with shorter survival of patients. PRL-3 and E-cadherin exhibit interactions in gastric cancer and are involved in the formation of lymph node metastases. The PRL-3 protein can be an independent predictive factor of overall survival in gastric cancer patients.
Highlights
The phosphatase of regenerating liver 3 (PRL-3) protein belongs to the family of tyrosine phosphatases, with a unique
Its physiological role is poorly investigated, literature data suggest that PRL-3 takes part in neoformation, i.e., in migration, metastasizing, and angiogenesis [1, 2]
Considering the similar role of both proteins in the migration of cancer cells and epithelial-mesenchymal transformation (EMT), the objective of the current study was to determine the correlation between the PRL-3 protein and E-cadherin, to assess their expression in cancer tissue and in normal gastric mucosa, as well as to investigate their effect on tumor stage
Summary
The phosphatase of regenerating liver 3 (PRL-3) protein belongs to the family of tyrosine phosphatases, with a unique. COOH-terminal prenylation motif, and it is involved in a major reaction for the cell, i.e., dephosphorylation of tyrosine residues deactivating enzymes. Factors that regulate PRL-3 expression as well as its enzymes are not well known, and researchers are still searching for pathways and processes associated with the protein involvement. Regulation of cell adhesion is another mechanism of the protein in the promotion of cancer cell invasion and metastasizing [8, 9]. The PRL-3 is involved in tumor growth through the mechanism of epithelial-mesenchymal transformation (EMT). PRL-3 activates the Akt pathway, which results in glycogen synthase kinase 3β (GSK-3β) inactivation and in overexpression of mesenchymal markers—vimentin, fibronectin, and Snail—
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