Fig. 4
From: Biochemical and pathological changes result from mutated Caveolin-3 in muscle
Study of ER-Golgi relevant proteins. (a) Immunohistochemical studies focusing on ER-Golgi stress confirm UPR activation (increased abundance of the phosphorylated (activated) form of eIF2α, of HSP70 and RCN2) in p.P104L muscle fibres. Interestingly, the cytosolic chaperone HSP70 shows enrichment at the sub-sarcolemmal sarcoplasm of muscle fibres expressing the mutant protein. RCN2 is accumulating in damaged muscle fibres. (b) Pathomorphological findings highlighted in Figure 3 are accompanied by reduced expression of ATL1, a protein important for the structural maintenance of the ER-Golgi system as well as altered abundance of proteins controlled by ER-stress and UPR (SIL1 and BiP, HSP70, RCN2 and SEC61). Coomassie brilliant blue staining: loading control