Nuclear translocation of β-catenin induced by E-cadherin endocytosis causes recurrent erosion of diabetic cornea

2021 ◽  
pp. 153537022098324
Author(s):  
Wenbei Ma ◽  
Zhengyuan Xie ◽  
Hui Chen ◽  
Lina Zeng ◽  
Xiaohong Chen ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
High Glucose ◽  
Nuclear Translocation ◽  
Visual Disturbance ◽  
Cell Junctions ◽  
Cell Junction ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Ulcers ◽  
E Cadherin

Recurrent epithelial erosion and refractory corneal ulcer are the clinical features of diabetic keratopathy (DK), which eventually lead to corneal scar and visual disturbance. In this study, we sought to determine the abnormalities of cell junction in diabetic corneal epithelial cells and the effect of high glucose on the β-catenin/E-cadherin complex. Corneal histology showed that corneal epithelial cells of high glucose mice were loosely arranged, and the immunohistochemistry showed that the expression of E-cadherin decreased, the levels of β-catenin increased in nuclear. High glucose-induced degradation and endocytosis of E-cadherin of corneal epithelial cells reduce the formation of β-catenin/E-cadherin complex and promote the nuclear translocation of β-catenin. Moreover, high glucose also activated the transcription and expression of matrix metallopeptidase and snail, which interfered with the adhesion of corneal epithelial cells to the basement membrane. These findings reveal that DK is associated with the dissociation of cell junctions. The maintenance of the stability of the β-catenin/E-cadherin complex may be a potential therapeutic target of refractory corneal ulcers in patients with diabetes.

Prolonged exposure to high glucose impaired cellular behavior of normal human corneal epithelial cells

2003 ◽  
Vol 27 (4) ◽  
pp. 197-203 ◽  
Author(s):  
Hiroki Fujita ◽  
Ikuo Morita ◽  
Hiroshi Takase ◽  
Kyoko Ohno-Matsui ◽  
Manabu Mochizuki
Keyword(s):  
Epithelial Cells ◽  
High Glucose ◽  
Prolonged Exposure ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Cellular Behavior ◽  
Normal Human ◽  
Human Corneal Epithelial Cells

Pathogenesis of Corneal Lesions Caused by Moraxella bovis in Gnotobiotic Calves

1987 ◽  
Vol 24 (4) ◽  
pp. 287-295 ◽  
Author(s):  
D. G. Rogers ◽  
N. F. Cheville ◽  
G. W. Pugh
Keyword(s):  
Epithelial Cells ◽  
Virulent Strain ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Ulcers ◽  
Control Calf ◽  
Moraxella Bovis ◽  
Cellular Debris ◽  
Cell Processes ◽  
Scanning Electron

Moraxella bovis was instilled into the conjunctival sac of gnotobiotic calves and corneas were sampled serially after infection. Lesions developed in seven of eight infected calves, but were absent in a noninfected control calf. Histologically, M. bovis was first seen in foci of swollen epithelium and within basal epithelial cells adjacent to ulcers. Corneal ulcers were severe in later stages of infection; fibrin deposits, neutrophils, and bacteria were present in the stromas. Examination of early lesions by scanning electron microscopy showed M. bovis in pits on the surfaces of dark epithelial cells, enmeshed in degenerate epithelial cells and within erosions and an ulcer; in later samples, bacteria were rare. Ultrastructurally, M. bovis was seen in surface pits in superficial epithelial cell processes and within swollen epithelial cells. In stroma, M. bovis was frequently seen among collagen fibrils, within neutrophil phagosomes, and associated with cellular debris. This study demonstrates that a virulent strain of M. bovis can invade bovine corneal epithelial cells and can cause keratitis in the absence of injurious ultraviolet irradiation or other known predisposing environmental factors.

Reduced Expression of Laminin-5 in Corneal Epithelial Cells Under High Glucose Condition

Cornea ◽  
2006 ◽  
Vol 25 (1) ◽  
pp. 61-67 ◽  
Author(s):  
WenNan Lu ◽  
Nobuyuki Ebihara ◽  
Kaoru Miyazaki ◽  
Akira Murakami
Keyword(s):  
Epithelial Cells ◽  
High Glucose ◽  
Corneal Epithelial Cells ◽  
Laminin 5 ◽  
Corneal Epithelial ◽  
High Glucose Condition ◽  
Glucose Condition

scholarly journals Benzalkonium chloride-induced myofibroblastic transdifferentiation of Tenon’s capsule fibroblasts is inhibited by coculture with corneal epithelial cells or by interleukin-10

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Chiemi Yamashiro ◽  
Kazuhiro Tokuda ◽  
Yuka Kobayashi ◽  
Fumiaki Higashijima ◽  
Takuya Yoshimoto ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Benzalkonium Chloride ◽  
Nuclear Translocation ◽  
Smooth Muscle Actin ◽  
Interleukin 10 ◽  
Corneal Epithelial Cells ◽  
Induced Expression ◽  
Corneal Epithelial ◽  
Tenon’S Capsule ◽  
Tenon's Capsule

AbstractBenzalkonium chloride (BAC) is used as a preservative in eyedrops but induces subconjunctival fibrosis that can result in failure of glaucoma surgery. Tenon’s capsule fibroblasts in subconjunctival tissue interact with the corneal epithelium through tear fluid. With the use of a coculture system, we have now investigated the effect of human corneal epithelial (HCE) cells on myofibroblastic transdifferentiation of human Tenon fibroblasts (HTFs) induced by BAC (5 × 10−6%). Immunofluorescence and immunoblot analyses revealed that the BAC-induced expression of α smooth muscle actin (αSMA) in HTFs was suppressed by coculture of these cells with HCE cells (p < 0.01). The concentration of interleukin-10 (IL-10) in culture supernatants of BAC-treated HTFs was increased by coculture with HCE cells (17.26-fold, vs. coculure, p < 0.001). Immunofluorescence and immunoblot analyses also showed that exogenous IL-10 (300 pg/ml) suppressed the BAC-induced expression of αSMA by 43.65% (p < 0.05) as well as the nuclear translocation of myocardin-related transcription factor-A (MRTF-A) by 39.32% (p < 0.01) in HTFs cultured alone. Our findings suggest that corneal epithelial cells may protect against subconjunctival fibrosis by maintaining IL-10 levels and preventing the MRTF-A-dependent transdifferentiation of HTFs into myofibroblasts.

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.

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