Degradation of sarcomeric and cytoskeletal proteins in cultured skeletal muscle cells

Purintrapiban, Juntipa; Wang, Mei-chuan; Forsberg, Neil E.

doi:10.1016/s1096-4959(03)00201-x

Cited by 63 publications

(22 citation statements)

References 27 publications

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“…Although numerous members of the calpain family of proteases exist, the two best characterized calpains found in skeletal muscle are calpain 1 and calpain 2 (21). Active calpains have been shown to release sarcomeric proteins by cleaving cytoskeletal proteins (e.g., titin, nebulin) that anchor contractile elements (30,54). Moreover, calpain is known to degrade several cellular kinases and phosphatases and can also degrade oxidized contractile proteins such as actin and myosin (21,24,66).…”

Section: Powers Et Almentioning

confidence: 99%

Mechanistic Links Between Oxidative Stress and Disuse Muscle Atrophy

Powers

Smuder

Criswell

2011

Antioxidants & Redox Signaling

160

137

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Long periods of skeletal muscle inactivity promote a loss of muscle protein resulting in fiber atrophy. This disuseinduced muscle atrophy results from decreased protein synthesis and increased protein degradation. Recent studies have increased our insight into this complicated process, and evidence indicates that disturbed redox signaling is an important regulator of cell signaling pathways that control both protein synthesis and proteolysis in skeletal muscle. The objective of this review is to outline the role that reactive oxygen species play in the regulation of inactivity-induced skeletal muscle atrophy. Specifically, this report will provide an overview of experimental models used to investigate disuse muscle atrophy and will also highlight the intracellular sources of reactive oxygen species and reactive nitrogen species in inactive skeletal muscle. We then will provide a detailed discussion of the evidence that links oxidants to the cell signaling pathways that control both protein synthesis and degradation. Finally, by presenting unresolved issues related to oxidative stress and muscle atrophy, we hope that this review will serve as a stimulus for new research in this exciting field. Antioxid. Redox Signal. 15, 2519-2528.

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Section: Powers Et Almentioning

confidence: 99%

Mechanistic Links Between Oxidative Stress and Disuse Muscle Atrophy

Powers

Smuder

Criswell

2011

Antioxidants & Redox Signaling

160

137

View full text Add to dashboard Cite

show abstract

“…Although numerous members of the calpain family of proteases exist, the two best-characterized calpains found in skeletal muscle are termed -calpain and m-calpain and refer to micromolar and millimolar amounts of calcium required to activate each respective calpain isoform (28). Although calpains are not at present known to directly degrade the contractile proteins actin and myosin, they participate in sarcomeric protein release by cleaving cytoskeletal proteins (e.g., titin, nebulin) that anchor contractile elements (43,67). Moreover, calpain is known to degrade several kinases and phosphatases, including calcium/calmodulin-dependent kinase (CaM kinase II), protein kinase C (PKC-␣, PKC-␤I, PKC-␤II, and PKC-␥), and calcineurin (28, 32, 81).…”

Section: Proteolytic Pathways In Skeletal Musclementioning

confidence: 99%

Oxidative stress and disuse muscle atrophy

Powers

Kavazis²,

McClung³

2007

Journal of Applied Physiology

410

282

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“…One consequence of changes in intracellular Ca 2+ concentration is the activation of Ca 2+ -activated enzymes, such as calpains, which are major proteolytic systems in skeletal muscle (16). Calpains are proteases that can selectively cleave cytoskeletal proteins, and desmin has been shown to be one of their major and first substrates both in vivo and in vitro; and calpains are found in association with the sarcolemma (17). We speculate that in the present study Ca 2+ depletion might have induced a calpain-dependent cytoskeletal remodeling including desmin cleavage, resulting in the presence of desmin dots and aggregates in the cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

Changes in cell shape and desmin intermediate filament distribution are associated with down-regulation of desmin expression in C2C12 myoblasts grown in the absence of extracellular Ca2+

Mermelstein

Amaral

Rebello

et al. 2005

Braz J Med Biol Res

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Desmin is the main intermediate filament (IF) protein of muscle cells. In skeletal muscle, desmin IFs form a scaffold that interconnects the entire contractile apparatus with the subsarcolemmal cytoskeleton and cytoplasmic organelles. The interaction between desmin and the sarcolemma is mediated by a number of membrane proteins, many of which are Ca 2+ -sensitive. In the present study, we analyzed the effects of the Ca 2+ chelator EGTA (1.75 mM) on the expression and distribution of desmin in C2C12 myoblasts grown in culture. We used indirect immunofluorescence microscopy and reverse transcription polymerase chain reaction (RT-PCR) to analyze desmin distribution and expression in C2C12 cells grown in the presence or absence of EGTA. Control C2C12 myoblasts showed a well-spread morphology after a few hours in culture and became bipolar when grown for 24 h in the presence of EGTA. Control C2C12 cells showed a dense network of desmin from the perinuclear region to the cell periphery, whereas EGTA-treated cells showed desmin aggregates in the cytoplasm. RT-PCR analysis revealed a down-regulation of desmin expression in EGTA-treated C2C12 cells compared to untreated cells. The present results suggest that extracellular Ca 2+ availability plays a role in the regulation of desmin expression and in the spatial distribution of desmin IFs in myoblasts, and is involved in the generation and maintenance of myoblast cell shape.

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Degradation of sarcomeric and cytoskeletal proteins in cultured skeletal muscle cells

Cited by 63 publications

References 27 publications

Mechanistic Links Between Oxidative Stress and Disuse Muscle Atrophy

Mechanistic Links Between Oxidative Stress and Disuse Muscle Atrophy

Oxidative stress and disuse muscle atrophy

Changes in cell shape and desmin intermediate filament distribution are associated with down-regulation of desmin expression in C2C12 myoblasts grown in the absence of extracellular Ca2+

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