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. 2010 Nov 16;6(8):1078–1089. doi: 10.4161/auto.6.8.13378

Figure 4.

Figure 4

Decrease in the amount of potentially toxic Ub-proteins in muscle from autophagy-deficient GAA−/− strains upon therapy. (A) Western blot of protein lysates from gastrocnemius (fast) muscle with anti-ubiquitin (FK2) antibody. No difference in the levels of Ub-proteins is observed between untreated (lane 1) and ERT-treated (lane 2) GAA−/− mice. (B) Western blot of lysates from gastrocnemius muscle, prepared as detergent (Triton X-100)-soluble (s) and -nonsoluble fractions (ns), with FK2. Lane 1-WT; Lane 2-HS Acre:Atg5F/F:WT; Lane 3-HS Acre:Atg5F/F:GAA−/− untreated; Lane 4-HS Acre:Atg5F/F:GAA−/− treated. Note that there is a modest increase in the amount of Ub-proteins in muscle-specific autophagy-deficient WT mice (lane 2). (C) Single fibers stained for Ub (red) and LAMP-1 (green) show a dramatic decrease in the amount of Ub-proteins upon therapy. Muscle samples were taken from 4-month-old mice. Bars: 20 microns (top two parts); 10 microns (two lower parts). Occasional fibers from autophagy-deficient GAA−/− strains still contain enlarged lysosomes. The distribution of Ub-proteins in untreated fast muscle of MLCcre:Atg7F/F:GAA−/− mice (shown in Suppl. Fig. 2) is similar to that in the HS Acre:Atg5F/F:GAA−/− mice.