Figures
The α-tubulin displayed in the bottom panel of Fig 4C is incorrect. Please see the complete correct Fig 4 here.
A, WI-38 cells were transfected with 0.5 μg of CTGF-Luc and 0.1 μg of pBK-CMV-Lac Z for 24 h. The cells were treated with U0126 before they were subjected to hypoxia (1% O2) for an additional 24 h. The luciferase activity assay is described in the “Material and Methods” section. The results are expressed as the mean ± SEM of three independent experiments performed in duplicate. * p < 0.05, compared with the hypoxia group without U0126 treatment. B, WI-38 cells were transfected with control siRNA (con siRNA), MEK1 siRNA, and ERK1 siRNA. After 24 h, the cells were subjected to hypoxia for an additional 24 h. CTGF and α-tubulin levels were detected using western blotting, as described previously. The results are expressed as the mean ± SEM of three independent experiments. * p < 0.05, compared with hypoxia plus the control siRNA group. C, WI-38 cells were transfected with control siRNA (con siRNA), MEK1 siRNA, and ERK1 siRNA. After 24 h of transfection, MEK1, ERK1, and α-tubulin levels were detected using western blotting. Typical traces represent three independent experiments that yield similar results. D, WI-38 cells were pretreated with SB203580 for 20 min before they were subjected to hypoxia (1% O2) for an additional 24 h. CTGF and α-tubulin levels in the cell lysates were detected using western blotting. The results are expressed as the mean ± SEM of five independent experiments. * p < 0.05, compared with the hypoxia group without SB203580 treatment. E, WI-38 cells were subjected to hypoxia (1% O2) for the indicated time intervals, after which the levels of p38 phosphorylation and p38α were detected using western blotting. The results are expressed as the mean ± SEM of three independent experiments. * p < 0.05, compared with the control group without hypoxia treatment.
In Fig 5D, the row containing Lamin A/C incorrectly appears twice. Please see the complete correct Fig 5 here.
WI-38 Cells were subjected to hypoxia (1% O2) for a time interval of 0–60 min (A) or 2–24 h (B), after which the levels of ERK phosphorylation and ERK in cell lysates were detected using western blotting. The results are expressed as the mean ± SEM of three and four independent experiments. * p < 0.05, compared with the control group without hypoxia treatment. C, WI-38 cells were subjected to hypoxia (1% O2) for 10 min, before they were immunoprecipitated with a specific ERK antibody and mag sepharose magnetic beads, as described in the “Materials and methods” section. After elusion from the beads, the levels of GLI-1, GLI-2, and ERK in the lysates were detected using western blotting. Typical traces represent three independent experiments that yield similar results. D, WI-38 cells were pretreated with U0126 for 20 min before they were subjected to hypoxia (1% O2) for an additional 2 h, after which nuclear protein was collected. The levels of GLI-1, GLI-2, and lamin A/C in the nuclear extract were detected using western blotting. Typical traces represent three independent experiments that yield similar results.
Reference
- 1. Cheng Y, Lin C-h, Chen J-Y, Li C-H, Liu Y-T, Chen B-C (2016) Induction of Connective Tissue Growth Factor Expression by Hypoxia in Human Lung Fibroblasts via the MEKK1/MEK1/ERK1/GLI-1/GLI-2 and AP-1 Pathways. PLoS ONE11(8): e0160593. https://doi.org/10.1371/journal.pone.0160593 pmid:27486656
Citation: Cheng Y, Lin C-h, Chen J-Y, Li C-H, Liu Y-T, Chen B-C (2017) Correction: Induction of Connective Tissue Growth Factor Expression by Hypoxia in Human Lung Fibroblasts via the MEKK1/MEK1/ERK1/GLI-1/GLI-2 and AP-1 Pathways. PLoS ONE 12(11): e0188608. https://doi.org/10.1371/journal.pone.0188608
Published: November 21, 2017
Copyright: © 2017 Cheng et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.