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. 2012 Aug 27;122(9):3330–3342. doi: 10.1172/JCI63004

Figure 2. Biochemical analyses of dystroglycan in skeletal muscle from Fktn-KO mice and littermates.

Figure 2

(A) Western blot analyses of WGA-purified skeletal muscle from myf5-Cre/Fktn (E8) KO mice and littermates (LC, Het). All KOs have reduced αDG mass, as measured by detection of core protein (αDG core). This corresponds to a complete loss of αDG binding activity in laminin overlay (Lam O/L) and loss or reduction of αDG glyco-epitopes (αDG glyco). βDG protein is detected in all cases. (B) Western blot analyses of MCK-Cre/Fktn (E17) KO and littermates, as in A. (C) Detection of αDG free phosphate. WGA-enriched skeletal muscle was applied to PHOS-beads to capture proteins with exposed phosphates. αDG from control mice has no free phosphate, but E8 and E17 muscle KOs (myf5-Cre/Fktn KO, MCK-Cre/Fktn KO) contain a substantial proportion with exposed phosphate. βDG is normally phosphorylated and serves as an experimental control.