The AMP-activated protein kinase α2 catalytic subunit controls whole-body insulin sensitivity
J. Clin. Invest. Benoit Viollet, et al. 111:91 doi:10.1172/JCI16567 [Go to this article.]

Figure 1
Generation of mice lacking AMPKα2. (a) Schematic representation (not to scale) of genomic structure of AMPKα2 wild-type allele, AMPKα2 gene-targeting construct, AMPKα2 targeted allele, and AMPKα2 null allele. Squares indicate loxP sites and H’s indicate HindIII restriction sites. C corresponds to the exon encoding the AMPKα2 catalytic domain (amino acids 189–260) (b) Southern blot analysis after HindIII digestion of tail DNA from offspring derived from heterozygous intercrosses. Expected fragment sizes of the AMPKα2 wild-type (+/+; 5.3 kb) and null (–/–; 3.8 kb) alleles after HindIII digestion and hybridization with the indicated probe (solid bar in a) are shown. (c) Western blot analysis of AMPKα1 and AMPKα2 proteins in liver and gastrocnemius muscle from control (+/+) and AMPKα2–/– mice. (d) Phosphorylation level of ACC in liver and gastrocnemius muscle from control and AMPKα2–/– mice.