ArticleVirchows Archiv : an international journal of pathology2004
Expression of occludin, a tight-junction-associated protein, in human lung carcinomas.
Article in Virchows Archiv : an international journal of pathology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
- Drug monomers from Salvia miltiorrhiza Bge. promoting tight junction protein expression for therapeutic effects on lung cancer.Scientific reports · 2023Article
- Tight Junctions, the Epithelial Barrier, and Toll-like Receptor-4 During Lung Injury.Inflammation · 2022Review
- Effects of the Glutamine Administration on T Helper Cell Regulation and Inflammatory Response in Obese Mice Complicated with Polymicrobial Sepsis.Mediators of inflammation · 2020Article
- Construction of prognostic risk prediction model of oral squamous cell carcinoma based on co-methylated genes.International journal of molecular medicine · 2019Article
- Increase in resistance to anticancer drugs involves occludin in spheroid culture model of lung adenocarcinoma A549 cells.Scientific reports · 2018Article
- Expression of claudin-5, claudin-7 and occludin in oral squamous cell carcinoma and their clinico-pathological significance.Journal of clinical and experimental dentistry · 2016Article
- Epidermal tight junctions in health and disease.Tissue barriers · 2015Article
- Metadherin regulates proliferation and metastasis via actin cytoskeletal remodelling in non-small cell lung cancer.British journal of cancer · 2014Article
- Melatonin inhibits the migration of human lung adenocarcinoma A549 cell lines involving JNK/MAPK pathway.PloS one · 2014Article
- Article
- Tight junctions in lung cancer and lung metastasis: a review.International journal of clinical and experimental pathology · 2012Review
- Tight junctions: a barrier to the initiation and progression of breast cancer?Journal of biomedicine & biotechnology · 2010Review
- Raf 1 represses expression of the tight junction protein occludin via activation of the zinc-finger transcription factor slug.Oncogene · 2007Article
- Changes of cell adhesion and extracellular matrix (ECM) components in cervical intraepithelial neoplasia.Pathology oncology research : POR · 2005Article
- Tight Junctions and the Tumor Microenvironment.Current pathobiology reportsReview
- Hippo pathway elements Co-localize with Occludin: A possible sensor system in pancreatic epithelial cells.Tissue barriersArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Occludin is a tight-junction-associated transmembrane protein, and previous observations suggested that occludin might play a crucial role in the formation and maintenance of organized tubular structures. Based on these observations, we explored the possible role of occludin immunostaining in the diagnosis of lung carcinomas. A total of 68 lung carcinomas and surrounding normal lung tissues were studied. A formalin-fixed, paraffin-embedded section from each tumor was stained with a new anti-occludin monoclonal antibody raised in our laboratory. In normal lung tissues, the anti-occludin antibody strongly stained the apicoluminal borders of the bronchial/bronchiolar epithelia and bronchial glands as a dot or short line. The antibody also stained the intercellular borders of alveolar epithelia. In cancer cells that faced lumina of all adenocarcinomas, regardless of grade, including bronchioloalveolar carcinomas, occludin showed an expression pattern identical to that of the normal bronchial and alveolar epithelia. Occludin reactivity was not noted in any cases of squamous cell carcinoma, large cell carcinoma, small cell carcinoma, or large cell neuroendocrine carcinoma. The results of the present study suggest that occludin can serve as an immunohistochemical indicator of the "true" glandular differentiation that forms tubulo-papillary structures in human lung carcinoma tissues.
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