Conditional disruption of IκB kinase 2 fails to prevent obesity-induced insulin resistance
J. Clin. Invest. Mathias Röhl, et al. 113:474 doi:10.1172/JCI18712 [Go to this article.]

Figure 3
GTG treatment results in increased TNF-α expression in WAT, activation of TNF-α signaling in skeletal muscle, and decreased plasma adiponectin concentrations. (a) The upper panel shows a Northern blot analysis of RNA extracted from WAT of control and IKK2^Het mice injected either with PBS or GTG. “TNF-α” marks the position of the murine TNF-α mRNA. The lower panel shows a photograph of the ethidium bromide–stained RNA gel prior to transfer onto a nylon membrane as a loading control. “18S” marks the position of the 18S RNA. (b) Protein extracts were prepared from skeletal muscle of lean and obese IKK2^WT and IKK2^Het/Mus mice and subjected to SDS-PAGE followed by Western transfer. After transfer onto nitrocellulose filters, blots were cut and the upper part was subjected to Western blot analysis with an antiserum against RasGap as a loading control, while the lower part was subjected to Western blot analysis with an antiserum that detects IκBα when phosphorylated at serine 32. The lower panel shows the densitometric quantification of IκBα phosphorylation as mean ± SEM of four to six animals in each group. (c) Plasma adiponectin concentrations in lean and obese mice, given as mean ± SEM of at least 16 animals in each group (*P < 0.01). (d) Plasma adiponectin concentrations in GTG-treated male mice of the indicated genotype, given as mean ± SEM of at least six animals in each group, revealed no significant differences depending on IKK2 expression.