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. 2011 Jan;178(1):261–272. doi: 10.1016/j.ajpath.2010.11.020

Figure 5.

Figure 5

Abnormal glycosylation of α-dystroglycan in shFKRP-treated muscles after 10 months. A: Immunofluorescent staining of the AAV-shFKRP-treated GAS muscles with α-dystroglycan–specific antibody IIH6 at 10 months postinjection. Note the reduction of staining in the shFKRP2 + 5–treated muscles. B: Western blot of proteins extracted from GAS muscles of each treated group were done using anti-α-dystroglycan (IIH6) and β-dystroglycan (DAG-1) antibodies to evaluate the glycosylation of α-dystroglycan and the expression of β-dystroglycan, respectively. The GAS muscles from mdx mice and PBS-treated mice were used as the negative and positive controls, respectively. C: A ligand overlay assay using laminin on a blot of WGA-enriched shFKPR knockdown muscles was performed. Note that the affinity of the α-dystroglycan to laminin in shFKRP2 + 5–treated muscles (lanes 6 and 7) was weaker than in the control group (lane 2). D: Solid-phase assays were performed to quantitate the maximum laminin binding ability to α-DG in the shFKRP-treated muscles. Note that the binding ability of α-DG in shFKRP2 (53.7% ± 5.0%); -5(40.6% ± 4.4%); and -2 + 5 (31.0% ± 3.0%) treated groups was decreased and weaker than in the control group (n = 5, mean ± SD, *P < 0.001.)