Literature DB >> 12742348

Tight junction-related protein expression and distribution in human corneal epithelium.

Yuriko Ban1, Atsuyoshi Dota, Leanne J Cooper, Nigel J Fullwood, Takahiro Nakamura, Masakatsu Tsuzuki, Chikako Mochida, Shigeru Kinoshita.   

Abstract

PURPOSE: To investigate the expression and cellular distribution of the tight junction-related proteins occludin, claudin and ZO-1 in human corneal epithelium.
METHODS: Light and electron immunohistochemistry was used to determine tissue distribution of occludin, claudin-1 and ZO-1 in the human corneal epithelium. Reverse transcription-polymerase chain reaction was used to reveal claudin mRNA expression in human corneal epithelium.
RESULTS: In transverse sections, occludin and ZO-1 were localized at the apical cell-cell junctions between superficial cells in stratified corneal epithelium. Both basal and basolateral membranes of superficial cells were stained by the claudin-1 antibody, but no apical membrane staining was observed. In en face sections, claudin-1 and ZO-1 antibodies showed as bands that corresponded to the junctional complex. Claudin-1 staining of superficial cell cytoplasm was also observed. Occludin staining was seen at the junctional complex, where it was not continuous, but dotted along the cell junctions. The transcripts for claudin-1 and several other claudin isotypes, such as -2, -3, -4, -7, -9 and -14 were identified.
CONCLUSION: Not only occludin, but also some claudins act as integral transmembrane proteins in the corneal epithelium. ZO-1 is a component of the corneal epithelial tight junction, as it is in most epithelial cells.

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Year:  2003        PMID: 12742348     DOI: 10.1016/s0014-4835(03)00054-x

Source DB:  PubMed          Journal:  Exp Eye Res        ISSN: 0014-4835            Impact factor:   3.467


  47 in total

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9.  Expression and distribution of junctional adhesion molecule-1 in the human cornea.

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10.  Melatonin receptor expression in Xenopus laevis surface corneal epithelium: diurnal rhythm of lateral membrane localization.

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