Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma

• Published in: PloS one Vol. 12; no. 8; p. e0183692
• Main Authors: Wang, Shih-Ho, Wang, Kuan-Lin, Yang, Wen-Kai, Lee, Tsung-Han, Lo, Wan-Yu, Lee, Jane-Dar
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 23.08.2017; Public Library of Science (PLoS)
• Subjects: Adenocarcinoma; Adenocarcinoma - metabolism; Adenocarcinoma - pathology; Adherens junctions; Adhesive strength; ATPases; Biology and Life Sciences; Biomarkers; Biomarkers, Tumor - metabolism; Blotting, Western; Cadherins - metabolism; Cancer; Case-Control Studies; Cell adhesion & migration; Development and progression; E-cadherin; Enzymatic activity; Enzyme activity; Epithelium; Gastric cancer; Genetic aspects; Glands; Health aspects; Hospitals; Humans; Immunoblotting; Immunofluorescence; Immunoglobulins; Immunohistochemistry; Kinases; Lesions; Life sciences; Localization; Medicine and Health Sciences; Molecular biology; Motility; NADH; Nicotinamide adenine dinucleotide; Paraffin Embedding; Patients; Physiological aspects; Potassium; Prostate; Proteins; Research and Analysis Methods; Sodium; Sodium-Potassium-Exchanging ATPase - metabolism; Stomach cancer; Stomach Neoplasms - metabolism; Stomach Neoplasms - pathology; Surgery; Taiwan
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0183692

Gastric adenocarcinoma originates from an abnormal epithelium. The aim of this study was to investigate the expression of sodium-potassium ATPase (NKA), a transmembrane protein located in the epithelium for Na+ and K+ transportation, and E-cadherin, which are both crucial for the epithelium and adherens junction, as potential gastric cancer biomarkers. 45 patients diagnosed with gastric adenocarcinoma were recruited. Immunohistochemistry and immunofluorescence were conducted to for localization of NKA α1-, β1-isoform, and E-cadherin. NKA enzyme activity was determined by NADH-linked methods and immunoblotting of NKA α1-, β1-isoform, and E-cadherin were performed to evaluate protein expression. Immunostaining revealed that NKA was co-localized with E-cadherin in the glands of the gastric epithelium. Both NKA activity and α1-isoform protein expression were reduced in the study group (P < 0.05), indicating impaired NKA functions. In the adherens junctions, the NKA β1-isoform and E-cadherin were significantly reduced in the study groups (P < 0.05), indicating the adhesion force between cells may have been weakened. A significant decrease in NKA function (protein and activity) and E-cadherin in tumor lesions appear promising biomarker for gastric adenocarcinoma. Therefore, developing screening methods for detecting NKA function may be beneficial for the early diagnosis of gastric cancer. In our knowledge, this study was the first to investigate the NKA and E-cadherin expression in the relation of gastric adenocarcinoma in human patients.