Fig. 3

Comparative proteomic analysis of QF and FDB muscle fibers from WT and ASM^−/− mice. a Protein abundance values for three biological replicates of WT or ASM^−/− QF and FDB muscles isolated from WT and ASM^−/− mice. b Volcano plots indicating statistically significant (P < 0.05) differences between WT and ASM^−/− samples in the expression of all master proteins identified for QF and FDB muscles. Green box, proteins downregulated more than twofold in ASM^−/− relative to WT; pink box, proteins upregulated more than twofold in ASM^−/− relative to WT. c Volcano plots indicating statistically significant (P < 0.05) differences between WT and ASM^−/− samples in the expression of master proteins within a subset of functionally important skeletal muscle proteins, in QF and FDB muscles. Green box, proteins downregulated more than twofold in ASM^−/− relative to WT; pink box, proteins upregulated more than twofold in ASM^−/− relative to WT. d FDB fibers isolated from four WT mice and four ASM^−/− mice were solubilized and analyzed by Western blot with anti-SERCA1 antibodies (each lane corresponds to fibers isolated from one animal). Antibodies against α-tubulin were used as a loading control. e Densitometry values of the data in d expressed as SERCA1/α-tubulin ratio, showing no significant differences between the amount of SERCA1 in WT and ASM^−/− FDB fibers.