title: Beta-catenin activation and epithelial-mesenchymal transition in the pathogenesis of pterygium.
abstract: OBJECTIVE
  To investigate whether beta-catenin activation and epithelial-mesenchymal transition (EMT) is involved in the pathogenesis of pterygium.
  
  
  METHODS
  beta-Catenin and E-cadherin expression were examined in surgically excised tissue and eye bank corneas with intact pterygium. Snail and Slug, the transcriptional repressors of E-cadherin, and matrix metalloproteinase (MMP)-7, a down-stream gene regulated by beta-catenin were also investigated. Epithelial cells undergoing EMT-like changes were identified by double immunostaining for alpha-smooth muscle actin (SMA)/vimentin and cytokeratin 14. Transmission electron microscopy was used to examine the ultrastructure of the pterygial head.
  
  
  RESULTS
  Histopathology showed aberrant fibrotic proliferation beneath the pterygium epithelium, with epithelial processes extending into the stroma. Transmission electron microscopy revealed the dissociation of epithelial cells, which were surrounded by activated fibroblast-like cells. Characteristic downregulation of E-cadherin and intranuclear accumulation of beta-catenin and lymphoid-enhancer-factor-1 in pterygial epithelium were also observed by immunohistochemistry. Of note, epithelial cells extending into the stroma were positive for both alpha-SMA/vimentin and cytokeratin 14. Snail and Slug were immunopositive in the nuclei of pterygial epithelial cells, but not in normal corneal epithelial cells.
  
  
  CONCLUSIONS
  EMT of basal epithelial cells may play a key role in the pathogenesis of pterygium.
authors: Department of Ophthalmology; Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan.
authors: Naoko
authors: N
authors: Kato
authors: Shigeto
authors: S
authors: Shimmura
authors: Tetsuya
authors: T
authors: Kawakita
authors: Hideyuki
authors: H
authors: Miyashita
authors: Yoko
authors: Y
authors: Ogawa
authors: Satoru
authors: S
authors: Yoshida
authors: Kazunari
authors: K
authors: Higa
authors: Hideyuki
authors: H
authors: Okano
authors: Kazuo
authors: K
authors: Tsubota
mesh_terms: D000199:Actins / Q000378:metabolism; D015820:Cadherins / Q000378:metabolism; D004847:Epithelial Cells / Q000378:metabolism / Q000473:pathology*; D005347:Fibroblasts / Q000378:metabolism / Q000473:pathology*; D005355:Fibrosis; D019084:Fluorescent Antibody Technique, Indirect; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000235:genetics; D006801:Humans; D007124:Immunoenzyme Techniques; D053547:Keratin-14 / Q000378:metabolism; D016850:Limbus Corneae / Q000473:pathology; D051821:Lymphoid Enhancer-Binding Factor 1 / Q000378:metabolism; D020783:Matrix Metalloproteinase 7 / Q000235:genetics; D011625:Pterygium / Q000209:etiology* / Q000378:metabolism / Q000473:pathology; D012333:RNA, Messenger / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D000071250:Snail Family Transcription Factors; D014157:Transcription Factors / Q000378:metabolism; D014746:Vimentin / Q000378:metabolism; D051176:beta Catenin / Q000378:metabolism*
chemical_list: D000199:Actins; D015820:Cadherins; D053547:Keratin-14; C497573:LEF1 protein, human; D051821:Lymphoid Enhancer-Binding Factor 1; D012333:RNA, Messenger; C000604407:SNAI1 protein, human; D000071250:Snail Family Transcription Factors; D014157:Transcription Factors; D014746:Vimentin; D051176:beta Catenin; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); C060932:MMP7 protein, human; D020783:Matrix Metalloproteinase 7