Results: 5

1.
FIGURE 5.

FIGURE 5. From: Basal Bioenergetic Abnormalities in Skeletal Muscle from Ryanodine Receptor Malignant Hyperthermia-susceptible R163C Knock-in Mice.

Scheme of the metabolism and signal transduction pathways in R163C skeletal muscle. See explanation in the text. Bold letters indicate the parameters evaluated in this study. The scheme was based on the data obtained in this study and classified according to the DAVID functional classification tool (, ).

Cecilia Giulivi, et al. J Biol Chem. 2011 January 7;286(1):99-113.
2.
FIGURE 3.

FIGURE 3. From: Basal Bioenergetic Abnormalities in Skeletal Muscle from Ryanodine Receptor Malignant Hyperthermia-susceptible R163C Knock-in Mice.

Densitometry of protein bands detected by Western blotting in R163C skeletal muscle. Western blots for myoglobin, calcineurin, and RCAN3 were obtained for WT and R163C skeletal muscle. The intensities of the bands were normalized to actin (used as a loading control). Western blots of pAMPK (Thr-172) and pACC (Ser-79) were normalized to each respective total and unphosphorylated protein (i.e. AMPK and acetyl-CoA carboxylase). Western blots for pPKCϵ (Ser-660) and pPKCα (Thr-638/641) were normalized to a pan-PKC and PKCα, respectively. All results shown in the figure were expressed as percentage of WT values. No statistical differences were observed for total PKC, AMPK, or ACC2 when normalized to actin between WT and R163C.

Cecilia Giulivi, et al. J Biol Chem. 2011 January 7;286(1):99-113.
3.
FIGURE 1.

FIGURE 1. From: Basal Bioenergetic Abnormalities in Skeletal Muscle from Ryanodine Receptor Malignant Hyperthermia-susceptible R163C Knock-in Mice.

A, representative Western blot of RyR1 protein in the whole membrane fraction of skeletal muscle isolated from WT and R163C mice. RyR1 expression was detected by separating the proteins by SDS-PAGE, followed by Western blotting as described under “Experimental Procedures.” Total protein applied was 10 μg/lane. B, summary densitometry data of RyR1 protein in WT and R163C mice expressed in fluorescence units per μg of protein. Densitometry was performed on at least four separate blots. a.u., arbitrary units. C, representative Western blot of myoglobin, ATPase β-subunit, and complex II 70-kDa subunit in the mitochondrial (M) and post-mitochondrial (PM) fractions from skeletal muscle obtained from WT mice. Experimental details were given under “Experimental Procedures.”

Cecilia Giulivi, et al. J Biol Chem. 2011 January 7;286(1):99-113.
4.
FIGURE 4.

FIGURE 4. From: Basal Bioenergetic Abnormalities in Skeletal Muscle from Ryanodine Receptor Malignant Hyperthermia-susceptible R163C Knock-in Mice.

A, transcript levels of Myh isoforms in WT and R163C skeletal muscle. All R163C values were significantly different from WT with p < 0.03. B, direct association between oxidative capacity (evaluated as citrate synthase or succinate dehydrogenase activities as markers for mitochondria) and glycogen content has been observed (); thus glycogen content in mouse muscles with various proportions of type IIB fibers was evaluated. Glycogen content was assayed on lower hind leg muscles tibialis anterior (TA), extensor digitorum longus (EDL), soleus, gastrocnemius (GST), the upper hind leg muscle, quadriceps (QUAD), the back muscle spinalis thoracis (SPN), and brachii muscles (BRC) from female WT and R163C (brachii muscles only). The percentage of Myh4 was evaluated as described under “Experimental Procedures” or as calculated from Ref. using the percentage of type IIB in the population of fibers for that particular muscle(s). The data points were fitted to a linear regression (r2 = 0.81 with a p < 0.05 using χ2 goodness of fit). Glycogen content decreased from muscles constituted mainly of type I (or slow-twitch) fibers to those that have a higher proportion of fast-twitch fibers.

Cecilia Giulivi, et al. J Biol Chem. 2011 January 7;286(1):99-113.
5.
FIGURE 2.

FIGURE 2. From: Basal Bioenergetic Abnormalities in Skeletal Muscle from Ryanodine Receptor Malignant Hyperthermia-susceptible R163C Knock-in Mice.

Protein and transcript levels of mitochondrial proteins in skeletal muscle from R163C relative to WT. A, mitochondrial protein expression expressed as percentage of WT values. Western blots of the indicated mitochondrial proteins were performed on mitochondrial fractions from WT and R163C skeletal muscle. Dashed lines indicate the average of protein expression for nDNA- or mtDNA-encoded proteins. Abbreviations used are as follows: SDHA, complex II 70-kDa subunit; CCO I, cytochrome c oxidase subunit I; ATPB, ATPase β-subunit; VDAC-1, voltage-dependent anion channel 1; MnSOD, manganese-dependent superoxide dismutase; CCO II, cytochrome c oxidase subunit II; ND1 and ND6 subunits 1 and 6 of NADH dehydrogenase. B, transcript level of each gene was normalized to actin and then expressed as the fold difference to the WT values. All experimental details for RNA extraction, cDNA preparation, and PCR conditions were explained in detail under “Experimental Procedures.” Dashed line indicates the WT values. Abbreviations used are as follows: CYTB, cytochrome b; MRPL10, mitochondrial ribosomal protein L10. Asterisks indicate statistically significant differences when compared with their respective WT values (p = 0.007 and 0.01, for CYTB and ND1, respectively).

Cecilia Giulivi, et al. J Biol Chem. 2011 January 7;286(1):99-113.

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