Characterization of control and immobilized skeletal muscle: an overview from genetic engineering

St‐Amand, Jonny; Okamura, Koji; Matsumoto, Keitaro; Shimizu, Seiichi; Sogawa, Yoshiro

doi:10.1096/fj.00-0150com

Cited by 86 publications

(125 citation statements)

References 61 publications

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“…For example, skeletal muscle PK-catalyzed phosphotransfer activity can be increased upon binding with MM-CK resulting in an increased flux through PK, independently of its substrate concentrations (45). Interestingly, an up-regulation of GAPDH and/or PK mRNA, as we found here, has also been reported for heart and skeletal muscle in response to muscle disuse and ischemic stress (46,47).…”

Section: Discussionsupporting

confidence: 87%

Adenylate Kinase 1 Deficiency Induces Molecular and Structural Adaptations to Support Muscle Energy Metabolism

Janssen¹,

Groof²,

Wijers³

et al. 2003

Journal of Biological Chemistry

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Genetic ablation of adenylate kinase 1 (AK1), a member of the AK family of phosphotransfer enzymes, disturbs muscle energetic economy and decreases tolerance to metabolic stress, despite rearrangements in alternative high energy phosphoryl transfer pathways. To define the mechanisms of this adaptive response, soleus and gastrocnemius muscles from AK1 ؊/؊ mice were characterized by cDNA array profiling, Western blot and ultrastructural analysis. We demonstrate that AK1 deficiency induces fiber-type specific variation in groups of transcripts involved in glycolysis and mitochondrial metabolism and in gene products defining structural and myogenic events. This was associated with increased phosphotransfer capacities of the glycolytic enzymes pyruvate kinase and 3-phosphoglycerate kinase. Moreover, in AK1 ؊/؊ mice, fast-twitch gastrocnemius, but not slow-twitch soleus, had an increase in adenine nucleotide translocator (ANT) and mitochondrial creatine kinase protein, along with a doubling of the intermyofibrillar mitochondrial volume. These results provide molecular evidence for wide-scale remodeling in AK1-deficient muscles aimed at preservation of efficient energetic communication between ATP producing and utilizing cellular sites.

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Section: Discussionsupporting

confidence: 87%

Adenylate Kinase 1 Deficiency Induces Molecular and Structural Adaptations to Support Muscle Energy Metabolism

Janssen¹,

Groof²,

Wijers³

et al. 2003

Journal of Biological Chemistry

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“…We also observed isoform switching of myosin-binding protein C (MyBP-C), from the slow type (Cs) to the fast type (Cf) as well as to the intermediate type (Ci) (Fig. 3 C; see McCormick et al, 1994;St-Amand et al, 2001). However, the total MyBP-C level was not signifi cantly reduced in disuse (Fig.…”

Section: R E S U Lt S a N D Discussionmentioning

confidence: 90%

Disuse-induced Preferential Loss of the Giant Protein Titin Depresses Muscle Performance via Abnormal Sarcomeric Organization

Udaka¹,

Ohmori²,

Terui³

et al. 2008

J Cell Biol

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Persistent muscle weakness due to disuse-associated skeletal muscle atrophy limits the quality of life for patients with various diseases and individuals who are confi ned to bed. Fibers from disused muscle exhibit a marked reduction in active force production, which can exacerbate motor function, coupled with the well-known loss of muscle quantity. Despite recent understanding of the signaling pathways leading to the quantity loss, the molecular mechanisms of the depressed qualitative performance still remain elusive. Here we show that long-term disuse causes preferential loss of the giant sarcomere protein titin, associated with changes in physiologic muscle function. Ca 2+ sensitivity of active force decreased following 6 wk of hindlimb immobilization in the soleus muscle of the rat, accompanied by a shift in the length-active force relationship to the shorter length side. Our analyses revealed marked changes in the disused sarcomere, with shortening of thick and thin fi laments responsible for altered length dependence and expansion of interfi lament lattice spacing leading to a reduction in Ca 2+ sensitivity. These results provide a novel view that disuse-induced preferential titin loss results in altered muscle function via abnormal sarcomeric organization.

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“…The serial analysis of gene expression (SAGE) method was performed as previously described (Velculescu et al 1995, St-Amand et al 2001. Total RNA was isolated by Trizol (Invitrogen Canada Inc).…”

Section: Transcriptome Analysismentioning

confidence: 99%

Gender difference of androgen actions on skeletal muscle transcriptome

Yoshioka¹,

Boivin²,

Bolduc³

et al. 2007

Journal of Molecular Endocrinology

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Sarcopenia is related to metabolic syndrome in postmenopausal women. Hormone replacement therapies with androgens improve muscle functions by molecular mechanisms that are still unknown, at least partly because the skeletal muscle transcriptome has been less characterized in females. We performed the serial analysis of gene expression method in six experimental groups, intact (male and female), ovariectomy (OVX), OVXCdihydrotestosterone (DHT) injection 1, 3, or 24 h before kill in mice. The 438 transcript species differentially expressed between gender showed that females had higher expression levels of mRNA related to cytoskeleton/contractile apparatus and mitochondrial processes as well as protein, lipid, and amino acid metabolisms. In females, OVX and DHT modulated 109 and 128 transcript species respectively. OVX repressed transcripts of fast/glycolytic fiber, glycolysis, and glucose transport, whereas all these effects were reversed 3 h after the DHT injection. Moreover, DHT treatment induced transcripts which reduce intracellular Ca 2C level at early time points. These results may suggest that DHT treatment in OVX mice increases muscle contractility by affecting fiber distribution and intracellular Ca 2C concentration as well as improving glucose metabolism. On the other hand, transcripts of fast/oxidative fiber, oxidative phosphorylation, and ATP production were repressed 24 h after DHT administration. In our previous study using male mice, transcripts in oxidative phosphorylation and ATP production were induced 24 h after DHT injection (Yoshioka M, Boivin A, Ye P, Labrie F & St-Amand J 2006 Effects of dihydrotestosterone on skeletal muscle transcriptome in mice measured by serial analysis of gene expression. Journal of Molecular Endocrinology 36 247-259). These results demonstrate gender differences in DHT actions on skeletal muscle, and contribute to a precise understanding of the molecular mechanisms of androgen actions in the female skeletal muscle.

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Characterization of control and immobilized skeletal muscle: an overview from genetic engineering

Cited by 86 publications

References 61 publications

Adenylate Kinase 1 Deficiency Induces Molecular and Structural Adaptations to Support Muscle Energy Metabolism

Adenylate Kinase 1 Deficiency Induces Molecular and Structural Adaptations to Support Muscle Energy Metabolism

Disuse-induced Preferential Loss of the Giant Protein Titin Depresses Muscle Performance via Abnormal Sarcomeric Organization

Gender difference of androgen actions on skeletal muscle transcriptome

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