Occludin expression decreases with the progression of human endometrial carcinoma

Hum Pathol. 2004 Feb;35(2):159-64. doi: 10.1016/j.humpath.2003.09.013.


The tight junctions of the glandular epithelium are crucial for the maintenance of cell polarity, separating the plasma membrane into apical and basolateral domains. Thus abnormalities of the tight junctions may result in the structural disturbances of glandular epithelial neoplasia. In this study we introduced an anti-occludin monoclonal antibody for semiquantitative assay of the occludin expression in tissue sections of human normal and neoplastic endometrial epithelia using the Adobe Photoshop and NIH Image programs. Normal endometrial glands and samples of endometrial hyperplasia and endometrioid carcinoma grade 1 fully expressed occludin at the apical cell border. In endometrioid carcinomas grades 2 and 3, however, occludin disappeared in solid areas of the carcinomatous tissues. Occludin was also found at the apical borders of the cancer cells that formed glandular structures. Occludin expression decreased progressively in parallel with the increase in carcinoma grade, and the decreased occludin expression correlated with myometrial invasion and lymph node metastasis. These results suggest that the loss of tight junctions has a close relationship with structural atypia in the progression of human endometrial carcinomas and their malignant potential.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / metabolism
  • Adenocarcinoma / pathology
  • Adult
  • Antibodies, Monoclonal
  • Biomarkers, Tumor / immunology
  • Biomarkers, Tumor / metabolism*
  • Disease Progression
  • Down-Regulation
  • Endometrial Hyperplasia / metabolism
  • Endometrial Hyperplasia / pathology
  • Endometrial Neoplasms / metabolism*
  • Endometrial Neoplasms / pathology*
  • Female
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Immunohistochemistry
  • Lymphatic Metastasis
  • Membrane Proteins / immunology
  • Membrane Proteins / metabolism*
  • Neoplasm Invasiveness
  • Occludin
  • Tight Junctions* / metabolism
  • Tight Junctions* / pathology


  • Antibodies, Monoclonal
  • Biomarkers, Tumor
  • Membrane Proteins
  • OCLN protein, human
  • Occludin