December 2002
Volume 43, Issue 13
ARVO Annual Meeting Abstract  |   December 2002
A role for ZO-1 in Corneal Fibroblasts
Author Affiliations & Notes
  • LD Taliana
    Ophthalmology/Cell Biology & Anatomy Mount Sinai School of Medicine New York NY
  • AM Bernstein
    Ophthalmology/Cell Biology & Anatomy Mount Sinai School of Medicine New York NY
  • RS Greenberg
    Ophthalmology/Cell Biology & Anatomy Mount Sinai School of Medicine New York NY
  • SK Masur
    Ophthalmology/Cell Biology & Anatomy Mount Sinai School of Medicine New York NY
  • Footnotes
    Commercial Relationships   L.D. Taliana, None; A.M. Bernstein, None; R.S. Greenberg, None; S.K. Masur, None. Grant Identification: NIH R01 EY09414, Fight For Sight, Research to Prevent Blindness
Investigative Ophthalmology & Visual Science December 2002, Vol.43, 2934. doi:
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    • Get Citation

      LD Taliana, AM Bernstein, RS Greenberg, SK Masur; A role for ZO-1 in Corneal Fibroblasts . Invest. Ophthalmol. Vis. Sci. 2002;43(13):2934.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract: : Purpose: ZO-1 is a member of a cytoplasmic protein family with multiple interaction domains that bind transmembrane proteins as well as the actin cytoskeleton. Previously we reported that ZO-1 co-localizes with Cx43 and cadherins at cell-cell contacts (IOVS 42:1509, 2001). We also demonstrated that ZO-1 localizes with α5ß1 and αvß3 at leading edges of lamellipodia. Since ZO-1 is expressed where reorganization of cell-cell and cell-matrix adhesion sites is occurring, we investigated whether ZO-1 associates with FAK (focal adhesion kinase), a cytosolic molecule that mediates integrin/actin cytoskeleton interactions. Methods:Immunocytochemistry, western blot analysis and immunoprecipitation were performed on cells and lysates of cultured primary rabbit corneal fibroblasts and mouse embryo fibroblasts (MEFs). Results:In scrape-wounded confluent cultures of rabbit corneal fibroblasts, we found both FAK and ZO-1 expressed in the lamellipodia. (In contrast, ZO-1 but not FAK was present in cell-cell contacts.) Furthermore, a functional relationship between the lamellipodial FAK and ZO-1 was suggested by our finding that immunoprecipitation by anti-FAK, co-immunprecipitates ZO-1 and FAK. To better understand the connection between ZO-1 and FAK, we evaluated the localization of ZO-1 in cells in the absence of FAK: we compared the distribution of ZO-1 in two types of MEFs: wildtype (WT) and those without FAK (FAK-/-) (Ilic D et al. Nature, 377: 539, 1995). In the scrape wound model, WT MEFs had ZO-1 at both cell-cell contacts and lamellipodia as in rabbit corneal fibroblasts. In contrast, in scrape-wounded FAK-/- MEFs, ZO-1 was strongly expressed in cell-cell contacts but absent from lamellipodia, suggesting the FAK was required to target ZO-1 at the leading edge. Integrin-dependent localization of ZO-1 to lamellipodia was confirmed by plating corneal fibroblasts on fibronectin for 15 minutes. Conclusion:We hypothesize that a FAK/ZO-1 scaffold superstructure promotes reorganization of cytoskeletal adhesion complexes in lamellipodia in response to wounding and that ZO-1 localization at the leading edge is integrin dependent.

Keywords: 339 cell adhesions/cell junctions • 374 cornea: stroma and keratocytes • 631 wound healing 

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