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Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma
BACKGROUND: 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 epi...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568324/ https://www.ncbi.nlm.nih.gov/pubmed/28832634 http://dx.doi.org/10.1371/journal.pone.0183692 |
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author | Wang, Shih-Ho Wang, Kuan-Lin Yang, Wen-Kai Lee, Tsung-Han Lo, Wan-Yu Lee, Jane-Dar |
author_facet | Wang, Shih-Ho Wang, Kuan-Lin Yang, Wen-Kai Lee, Tsung-Han Lo, Wan-Yu Lee, Jane-Dar |
author_sort | Wang, Shih-Ho |
collection | PubMed |
description | BACKGROUND: 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. METHODS: 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. RESULTS: 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. CONCLUSIONS: 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. |
format | Online Article Text |
id | pubmed-5568324 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-55683242017-09-09 Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma Wang, Shih-Ho Wang, Kuan-Lin Yang, Wen-Kai Lee, Tsung-Han Lo, Wan-Yu Lee, Jane-Dar PLoS One Research Article BACKGROUND: 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. METHODS: 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. RESULTS: 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. CONCLUSIONS: 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. Public Library of Science 2017-08-23 /pmc/articles/PMC5568324/ /pubmed/28832634 http://dx.doi.org/10.1371/journal.pone.0183692 Text en © 2017 Wang et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Wang, Shih-Ho Wang, Kuan-Lin Yang, Wen-Kai Lee, Tsung-Han Lo, Wan-Yu Lee, Jane-Dar Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma |
title | Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma |
title_full | Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma |
title_fullStr | Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma |
title_full_unstemmed | Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma |
title_short | Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma |
title_sort | expression and potential roles of sodium-potassium atpase and e-cadherin in human gastric adenocarcinoma |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568324/ https://www.ncbi.nlm.nih.gov/pubmed/28832634 http://dx.doi.org/10.1371/journal.pone.0183692 |
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