Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction
J. Clin. Invest. Jan Lammerding, et al. 113:370 doi:10.1172/JCI19670 [
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Figure 5Defective NF-κB signaling in lamin A/C–deficient cells. (
a) Western blot analysis of nuclear and cytoplasmic protein fractions. Cytokine-induced nuclear translocation of p65/RelA and degradation of cytoplasmic IκBα was indistinguishable between WT and
Lmna–/– fibroblasts. Cytoplasmic proteins were loaded at a lower concentration. Con, control. (
b) Electrophoretic mobility shift assay for NF-κB target sequence using protein from the same nuclear fractions as in
a. Probe specificity was confirmed using unlabeled competitive and noncompetitive probes. Identity of NF-κB subunits p50 and p65 was confirmed by supershift assay. (
c) Cytokine-induced NF-κB–regulated luciferase activity was significantly impaired in
Lmna–/– cells (percent of baseline: 282% ± 18.5% vs. 185% ± 22.2%;
P < 0.001,
n = 9). Baseline activity was not significantly different between WT and
Lmna–/– cells.
