Alarmins From Corneal Epithelial Cells Upregulate CCL11 and VCAM-1 in Corneal Fibroblasts

2013 ◽  
Vol 54 (8) ◽  
pp. 5817 ◽  
Author(s):  
Ken Fukuda ◽  
Waka Ishida ◽  
Hiroshi Tanaka ◽  
Yosuke Harada ◽  
Akira Matsuda ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Fibroblasts

scholarly journals Transient Mitomycin C-treatment of human corneal epithelial cells and fibroblasts alters cell migration, cytokine secretion, and matrix accumulation

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Sonali Pal-Ghosh ◽  
Gauri Tadvalkar ◽  
Verna Rose Lieberman ◽  
Xiaoqing Guo ◽  
James D. Zieske ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mitomycin C ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1 ◽  
Cytokine Secretion ◽  
Collagen Deposition ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Fibroblasts

Abstract A single application of Mitomycin C (MMC) is used clinically in ophthalmology to reduce scarring and enhance wound resolution after surgery. Here we show in vitro that a 3-hour MMC treatment of primary and telomerase immortalized human corneal limbal epithelial (HCLE) cells impacts their migration and adhesion. Transient MMC treatment induces HCLE expression of senescence associated secretory factors, cytokine secretion, and deposition of laminin 332 for several days. Transient MMC treatment also reduces migration and deposition of transforming growth factor-β1 (TGFβ1)-stimulated collagen by corneal fibroblasts. Using conditioned media from control and MMC treated cells, we demonstrate that factors secreted by MMC-treated corneal epithelial cells attenuate collagen deposition by HCFs whereas those secreted by MMC-treated HCFs do not. These studies are the first to probe the roles played by corneal epithelial cells in reducing collagen deposition by corneal fibroblasts in response to MMC.

Nuclear translocation of ferritin in corneal epithelial cells

2001 ◽  
Vol 114 (12) ◽  
pp. 2327-2334 ◽  
Author(s):  
Cindy X. Cai ◽  
Thomas F. Linsenmayer
Keyword(s):  
Epithelial Cells ◽  
Nuclear Localization ◽  
Nuclear Translocation ◽  
Supramolecular Assembly ◽  
The Body ◽  
Corneal Epithelial Cells ◽  
Tissue Specific ◽  
Corneal Epithelial ◽  
Corneal Fibroblasts ◽  
Ferritin H

Our previous studies have shown that ferritin within developing avian corneal epithelial cells is predominantly a nuclear protein and that one function of the molecule in this location is to protect DNA from UV damage. To elucidate the mechanism for this tissue-specific nuclear translocation, cultured corneal epithelial cells and corneal fibroblasts were transfected with a series of deletion constructs for the heavy chain of ferritin, ferritin-H, tagged with a human c-myc epitope. The subcellular localization of the ferritin was determined by immunofluorescence for the myc-tag. For the corneal epithelial cells, the first 10 or the last 30 amino acids of ferritin-H could be deleted without affecting the nuclear localization. However, larger deletions of these areas, or deletions along the length of the body of the molecule, resulted largely in retention of the truncated proteins within the cytoplasm. Thus, it seems that no specific region functions as an NLS. Immunoblotting analysis of SDS-PAGE-separated extracts suggests that assembly of the supramolecular form of ferritin is not necessary for successful nuclear translocation, because one deletion construct that failed to undergo supramolecular assembly showed nuclear localization. In transfected fibroblasts, the endogenous ferritin remained predominantly in the cytoplasm, as did that synthesized from transfected full-length ferritin constructs and from two deletion constructs encoding truncated chains that could still assemble into the supramolecular form of ferritin. However, those truncated chains that were unable to participate in supramolecular assembly generally showed both nuclear and cytoplasmic localization, indicating that, in this cell type, supramolecular assembly is involved in restricting ferritin to the cytoplasm. These data suggest that for corneal epithelial cells, the nuclear localization of ferritin most likely involves a tissue-specific mechanism that facilitates transport into the nucleus, whereas, in fibroblasts, the cytoplasmic retention involves supramolecular assembly that prevents passive diffusion into the nucleus.

Upregulation of Connexin43 Expression in Corneal Fibroblasts by Corneal Epithelial Cells

2009 ◽  
Vol 50 (5) ◽  
pp. 2054 ◽  
Author(s):  
Ji-Ae Ko ◽  
Ryoji Yanai ◽  
Naoyuki Morishige ◽  
Toshiaki Takezawa ◽  
Teruo Nishida
Keyword(s):  
Epithelial Cells ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Fibroblasts
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