Caspase Proteolysis of Desmin Produces a Dominant-negative Inhibitor of Intermediate Filaments and Promotes Apoptosis

Chen, Feng; Chang, Roger; Trivedi, Marcus; Capetanaki, Yassemi; Cryns, Vincent L.

doi:10.1074/jbc.m212021200

Cited by 101 publications

(97 citation statements)

References 47 publications

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“…HSP20s and HSP70s inhibit apoptosis by sequestering pro-apoptotic factors such as Bax (Beere & Green, 2001;Concannon, Gorman, & Samalli, 2003). Apoptosis have been identified as a tenderization enhancer just after slaughtering by Ouali et al (2006), notably by protein proteolysis done by caspases, enzymes able to degrade structural proteins (Chen, Chang, Trivedi, Capetanaki, & Cryns, 2003;Nakanishi, Maruyama, Shibata, & Morishima, 2001). So, this is in contradiction with the positive role of HSP20s with tenderness.…”

Section: Discrimination Of St Tenderness Classesmentioning

confidence: 99%

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

Guillemin¹,

Jurie²,

Renand³

et al. 2012

IJB

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This study analyzed the abundance of tenderness biomarkers: 24 proteins and 11 phenotypic carcass characteristics and muscle properties. This was done on 111 samples of two muscles, Longissimus thoracis (LT) and Semitendinosus (ST) from the Charolais cattle breed. The strategy was to constitute and explain three tenderness classes on the two muscles separately, on the shear-force data (Warner-Bratzler). Results showed that ST classes were explained by 12 proteins and 6 phenotypic characteristics. LT classes could only be explained by 7 phenotypic characteristics. This demonstrates that in ST and LT the tenderness variability is explained by different factors. In ST, the main results demonstrated the importance of Heat Shock Proteins such as Hsp27 (P = 0.002) and the oxidative stress protein: PRDX6 (P = 0.003). We also confirmed the role of the glycolytic enzyme Enolase 3 (P = 0.003), and contractile protein such as MyHC IIx (P = 0.028).

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Section: Discrimination Of St Tenderness Classesmentioning

confidence: 99%

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

Guillemin¹,

Jurie²,

Renand³

et al. 2012

IJB

View full text Add to dashboard Cite

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“…For example, it was reported that caspase-mediated cleavage of desmin is associated with apoptosis in muscle. 25 In addition, Limb Girdle muscular dystrophy type IIA is caused by mutation in protease calpain-3, a known activator of caspases, and apoptotic nuclei are observed in patients with this disorder. 26 Recently, several independent studies showed apoptotic myonuclei and caspase activation in myofibrillar myopathy.…”

Section: Homma Et Almentioning

confidence: 99%

BAG3 Deficiency Results in Fulminant Myopathy and Early Lethality

Homma

Iwasaki

Shelton

et al. 2006

The American Journal of Pathology

228

252

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Bcl-2-associated athanogene 3 (BAG3) is a member of a conserved family of cyto-protective proteins that bind to and regulate Hsp70 family molecular chaperones. Here, we show that BAG3 is prominently expressed in striated muscle and colocalizes with Zdisks. Mice with homozygous disruption of the bag3 gene developed normally but deteriorated postnatally with stunted growth evident by 1 to 2 weeks of age and death by 4 weeks. BAG3-deficient animals developed a fulminant myopathy characterized by noninflammatory myofibrillar degeneration with apoptotic features. Knockdown of bag3 expression in cultured C2C12 myoblasts increased apoptosis on induction of differentiation, suggesting a need for bag3 for maintenance of myotube survival and confirming a cell autonomous role for bag3 in muscle. We conclude that although BAG3 is not required for muscle development, this co-chaperone appears to be critically important for maintenance of mature skeletal muscle.

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“…Caspase 6 phosphorylates specific residues in desmin, induced by change in serum concentration that controls differentiation (50). Desmin has been described as a major substrate for proteolysis by a muscle-specific calpain (51).…”

Section: Molecular Interactionsmentioning

confidence: 99%

Desmin: molecular interactions and putative functions of the muscle intermediate filament protein

Costa

Escaleira

Cataldo

et al. 2004

Braz J Med Biol Res

121

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Desmin is the intermediate filament (IF) protein occurring exclusively in muscle and endothelial cells. There are other IF proteins in muscle such as nestin, peripherin, and vimentin, besides the ubiquitous lamins, but they are not unique to muscle. Desmin was purified in 1977, the desmin gene was characterized in 1989, and knock-out animals were generated in 1996. Several isoforms have been described. Desmin IFs are present throughout smooth, cardiac and skeletal muscle cells, but can be more concentrated in some particular structures, such as dense bodies, around the nuclei, around the Z-line or in costameres. Desmin is up-regulated in muscle-derived cellular adaptations, including conductive fibers in the heart, electric organs, some myopathies, and experimental treatments with drugs that induce muscle degeneration, like phorbol esters. Many molecules have been reported to associate with desmin, such as other IF proteins (including members of the membrane dystroglycan complex), nebulin, the actin and tubulin binding protein plectin, the molecular motor dynein, the gene regulatory protein MyoD, DNA, the chaperone αB-crystallin, and proteases such as calpain and caspase. Desmin has an important medical role, since it is used as a marker of tumors' origin. More recently, several myopathies have been described, with accumulation of desmin deposits. Yet, after almost 30 years since its identification, the function of desmin is still unclear. Suggested functions include myofibrillogenesis, mechanical support for the muscle, mitochondrial localization, gene expression regulation, and intracellular signaling. This review focuses on the biochemical interactions of desmin, with a discussion of its putative functions.

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Caspase Proteolysis of Desmin Produces a Dominant-negative Inhibitor of Intermediate Filaments and Promotes Apoptosis

Cited by 101 publications

References 47 publications

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

BAG3 Deficiency Results in Fulminant Myopathy and Early Lethality

Desmin: molecular interactions and putative functions of the muscle intermediate filament protein

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