scholarly journals Cellular FLICE-like inhibitory protein (cFLIP) critically maintains apoptotic resistance in human lens epithelial cells

2021 ◽  
Vol 12 (4) ◽  
Author(s):  
Jingru Huangfu ◽  
Caili Hao ◽  
Zongbo Wei ◽  
I. Michael Wormstone ◽  
Hong Yan ◽  
...  
Keyword(s):  
Cell Death ◽  
Epithelial Cell ◽  
Cell Survival ◽  
Hela Cells ◽  
Ex Vivo ◽  
Cell Types ◽  
Lens Epithelial Cell ◽  
Human Lens ◽  
Inhibitory Protein ◽  
Almost All

AbstractThe present study aims to understand the mechanism of the lens epithelial cell’s strong anti-apoptotic capacity and survival in the mature human lens that, on the one hand, maintains lens transparency over several decades, while on the other hand, increases the risk of posterior capsule opacification (PCO). Here we compared FHL124 cells and HeLa cells, spontaneously immortalized epithelial cell lines derived from the human lens and cervical cancer cells, respectively, of their resistance to TNFα-mediated cell death. TNFα plus cycloheximide (CHX) triggered almost all of HeLa cell death. FHL124 cells, however, were unaffected and able to block caspase-8 activation as well as prevent caspase-3 and PARP-1 cleavage. Interestingly, despite spontaneous NFκB and AP-1 activation and upregulation of multiple cell survival/anti-apoptotic genes in both cell types, only FHL124 cells were able to survive the TNFα challenge. After screening and comparing the cell survival genes, cFLIP was found to be highly expressed in FHL124 cells and substantially upregulated by TNFα stimulation. FHL124 cells with a mild cFLIP knockdown manifested a profound apoptotic response to TNFα stimulus similar to HeLa cells. Most importantly, we confirmed these findings in an ex vivo lens capsular bag culture system. In conclusion, our results show that cFLIP is a critical gene that is regulating lens epithelial cell survival.

EAAT and Xc−Exchanger Inhibition Depletes Glutathione in the Transformed Human Lens Epithelial Cell Line SRA 01/04

2015 ◽  
pp. 1-10 ◽  
Author(s):  
Marlyn P. Langford ◽  
Thomas B. Redens ◽  
Chanping Liang ◽  
A. Scott Kavanaugh ◽  
Donald E. Texada
Keyword(s):  
Epithelial Cell ◽  
Cell Line ◽  
Lens Epithelial Cell ◽  
Human Lens ◽  
Epithelial Cell Line ◽  
Human Lens Epithelial Cell

scholarly journals Evidence for two physiologically distinct gap junctions expressed by the chick lens epithelial cell.

1986 ◽  
Vol 102 (1) ◽  
pp. 194-199 ◽  
Author(s):  
T M Miller ◽  
D A Goodenough
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Gap Junctions ◽  
Cell Communication ◽  
Cell Types ◽  
Lens Epithelial Cell ◽  
Dye Transfer ◽  
Fiber Cells ◽  
Junctional Permeability ◽  
Different Cell Types

Lens epithelial cells communicate with two different cell types. They communicate with other epithelial cells via gap junctions on their lateral membranes, and with fiber cells via junctions on their apices. We tested independently these two routes of cell-cell communication to determine if treatment with a 90% CO2-equilibrated medium caused a decrease in junctional permeability; the transfer of fluorescent dye was used as the assay. We found that the high-CO2 treatment blocked intraepithelial dye transfer but not fiber-to-epithelium dye transfer. The lens epithelial cell thus forms at least two physiologically distinct classes of gap junctions.

Effect of growth factors on proliferation and expression of growth factor receptors in a human lens epithelial cell line

2006 ◽  
Vol 32 (3) ◽  
pp. 510-514 ◽  
Author(s):  
Juergen Kampmeier ◽  
Alicja Baldysiak-Figiel ◽  
Yvonne de Jong-Hesse ◽  
Gerhard K. Lang ◽  
Gabriele E. Lang
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Epithelial Cell ◽  
Cell Line ◽  
Growth Factor Receptors ◽  
Lens Epithelial Cell ◽  
Human Lens ◽  
Epithelial Cell Line ◽  
Human Lens Epithelial Cell

Dual Role of Pim-2 Depends on the Associated Proteome.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 4334-4334
Author(s):  
Daphna Levy ◽  
Amos M. Cohen ◽  
Jeremy Don
Keyword(s):  
Cell Survival ◽  
Hela Cells ◽  
Cell Types ◽  
Dual Role ◽  
Lymphocytic Leukemia ◽  
Dominant Negative ◽  
G1 Arrest ◽  
Apoptotic Pathway ◽  
Hodgkin's Lymphomas ◽  
Apoptotic Effects

Abstract Pim-2, a Ser/Thr kinase, is a proto-oncogene originally identified as common proviral insertion sites in T and B cell lymphomas in mice. Deregulation of Pim-2 expression has been documented in several human malignancies, including leukemia, lymphoma, multiple myeloma and prostate cancer. In human non-Hodgkin’s lymphomas and in chronic lymphocytic leukemia Pim-2 is up-regulated and its expression correlates with disease activity. Pim-2 promotes cell survival in response to a wide variety of proliferative signals. Pim-2 promotes cell survival by phosphorylation of Bad and Cot. The goal of this study was to clarify the significance of our new unanticipated aspect of Pim-2′s function, namely, that over-expression of Pim-2 in HeLa cells led to cell cycle arrest at G1 and to increased apoptosis. We found that the G1 arrest was associated with increased (T14/Y15) phosphorylation of CDK2, increased proteosomic degradation of CDC25A, and increased levels of the CDK inhibitor p57. In addition, we found increased E2F-1 levels, which suggested the usage of the E2F-1 dependent apoptotic pathway. Using dominant negative forms of either E2F-1 or p73, which were co-expressed with Pim-2 in HeLa cells, revealed significant rescue of the G1 arrest and apoptotic phenomena. Silencing of Pim-2 in these cells, via siRNA, reversed the G1 arrest and pro-apoptotic effects, and verified the Pim-2 dependent specificity. We conclude that Pim-2 might play a dual role. Our data suggest that under certain environmental circumstances and in various cell types, Pim-2 appears to increase cell survival by abrogating some pro-apoptotic substrates, but under different proteomic associations Pim-2 might favor G1 arrest and apoptosis.

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