Erratum: Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkBa/NF-kB pathway in limb-girdle muscular dystrophy type 2A

Baghdiguian, Stephen; Martin, Marianne; Richard, Isabelle; Pons, Françoise; Astier, Catherine; Bourg, Nathalie; Hay, Ronald T.; Chemaly, R.; Halaby, G.; Loiselet, Jacques; Anderson, Louise V.B.; Munáin, Adolfo López de; Fardeau, Michel; Mangeat, Paul; Beckmann, Jacques S.; Lefranc, Gérard

doi:10.1038/10579

Cited by 128 publications

(72 citation statements)

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“…34,35 Calpain 3 deficiency is associated with myonuclear apoptosis possibly due to inability to degrade IkBa. 36 Furthermore, calpain-independent cell death was also observed in thymocyte triggered by heat shock and by valinomycin and in cultured rat cardiomyocytes during metabolic inhibition. 21,37 Thus, the role of calpain in apoptosis is controversial and depends on cell types and treatment.…”

Section: Introductionmentioning

confidence: 92%

Increase in ultraviolet sensitivity by overexpression of calpastatin in ultraviolet-resistant UVr-1 cells derived from ultraviolet-sensitive human RSa cells

et al. 2000

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Human RSa cells are highly sensitive to apoptotic-like cell death by ultraviolet irradiation (UV) while UV r -1 cells are their variant with an increased resistance to UV. Three days after UV at 10 J/m 2 , the viability of RSa cells was approximately 17% while that of UV r -1 cells was 65%. This different survival might reflect apoptotic cell death since apoptosis-specific DNA ladder was more clearly observed in RSa cells than in UV r -1 cells after UV. Addition of ALLN/calpain inhibitor I to the culture medium after UV resulted in similar survival (14 ± 18%) between RSa and UV r -1 cells. Immunoblot analysis showed down-regulation of protein kinase Cy, Src, Bax and m-calpain after UV was more prominent in UV r -1 than in RSa cells. Activated m-calpain appeared within 1 h post-UV only in UV r -1 cells. The expression of calpastatin, a specific endogenous inhibitor of calpain, was higher in RSa than in UV r -1 cells. To further examine the role of calpain in UV-induced cell death, cDNA of human calpastatin was transfected into UV r -1 cells. The results showed that overexpression of calpastatin suppressed down-regulation of Src, m-calpain and Bax. Concomitantly, colony survival after UV was reduced in calpastatin-transfected cells as compared to vector control cells. Our results suggest that activation of calpain might account for, at least in part, the lower susceptibility to UVinduced cell death in UV r -1 cells. Cell Death and Differentiation (2000) 7, 531 ± 537.

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Section: Introductionmentioning

confidence: 92%

Increase in ultraviolet sensitivity by overexpression of calpastatin in ultraviolet-resistant UVr-1 cells derived from ultraviolet-sensitive human RSa cells

et al. 2000

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“…The mechanisms by which reovirus triggers increased cellular calpain activity are not known but may include initiation of calcium fluxes following viral attachment, as demonstrated with rotavirus, a closely related virus (15); upregulation of growth factors which facilitate calpain activation (37,66); or upregulation of endogenous calpain activator proteins which have been characterized for several cell types (49). Calpain may play a physiologic role in the regulation of a variety of cellular transcription factors and cell cycle-regulating factors implicated in apoptosis, including Jun, Fos, p53, cyclin D, and NF-B (3,7,73). We have recently shown that activation of NF-B is required for reovirus-induced apoptosis (J. L. Connolly, S. E. Rodgers, B. Pike, P. Clarke, K. L. Tyler, and T. S. Dermody, Abstr.…”

Section: Discussionmentioning

confidence: 99%

Calpain Inhibition Protects against Virus-Induced Apoptotic Myocardial Injury

DeBiasi

Edelstein²,

Sherry

et al. 2001

J Virol

101

111

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Viral myocarditis is an important cause of human morbidity and mortality for which reliable and effective therapy is lacking. Using reovirus strain 8B infection of neonatal mice, a well-characterized experimental model of direct virus-induced myocarditis, we now demonstrate that myocardial injury results from apoptosis. Proteases play a critical role as effectors of apoptosis. The activity of the cysteine protease calpain increases in reovirus-infected myocardiocytes and can be inhibited by the dipeptide alpha-ketoamide calpain inhibitor Z-Leu-aminobutyric acid-CONH(CH 2 )3-morpholine (CX295). Treatment of reovirus-infected neonatal mice with CX295 protects them against reovirus myocarditis as documented by (i) a dramatic reduction in histopathologic evidence of myocardial injury, (ii) complete inhibition of apoptotic myocardial cell death as identified by terminal deoxynucleotidyltransferase-mediated dUTP-biotin nick end labeling, (iii) a reduction in serum creatine phosphokinase, and (iv) improved weight gain. These findings are the first evidence for the importance of a calpain-associated pathway of apoptotic cell death in viral disease. Inhibition of apoptotic signaling pathways may be an effective strategy for the treatment of viral disease in general and viral myocarditis in particular.

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“…Due to its nuclear localization signal sequence, calpain-3 might act in the nucleus in particular conditions and might be involved in the regulation of transcription factors controlling survival genes and apoptosis. 15,16 Several molecules with regulatory functions have been reported to be substrates for calpains in cell culture, but various lines of research have suggested that calpains may be involved in cytoskeletal or myofibrillar protein degradation. 5,17,18 While it is unlikely that calpain-3 is implicated in myoblast fusion, being fusion-effective in muscle of LGMD2A patients, it might act in the disassembly of myofibrils during early stages of turnover 17 or cause a postfusion defect in muscle maturation.…”

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confidence: 99%

Loss of Calpain-3 Autocatalytic Activity in LGMD2A Patients with Normal Protein Expression

Fanin

Nascimbeni

Fulizio

et al. 2003

The American Journal of Pathology

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The diagnosis of limb girdle muscular dystrophy (LGMD) type 2A (due to mutations in the gene encoding for calpain-3) is currently based on protein analysis, but mutant patients with normal protein expression have also been identified. In this study we investigated 150 LGMD patients with normal calpain-3 protein expression, identified gene mutations by an allele-specific polymerase chain reaction test, and analyzed the mutant calpain-3 catalytic activity. Four different mutations were found in eight patients (5.5%): a frame-shifting deletion (550 A del) and three missense (R490Q, R489Q, R490W). Patients with normal calpain-3 protein expression on Western blot are a considerable proportion (20%) of our total LGMD2A population. While in control muscle the calpain-3 Ca ؉؉ -dependent autocatalytic activity was evident within 5 minutes and was prevented by ethylene diaminetetraacetic acid, in all mutant patient samples the protein was not degraded, indicating that the normal autocatalytic function had been lost. By this new functional test, we show that conventional protein diagnosis fails to detect some mutant proteins, and prove the pathogenetic role of R490Q, R489Q, R490W missense mutations. We suggest that these mutations impair protein activity by affecting interdomain protein interaction, or reduce autocatalytic activity by lowering the Ca

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Erratum: Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkBa/NF-kB pathway in limb-girdle muscular dystrophy type 2A

Abstract: Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkBa/NF-kB pathway in limb-girdle muscular dystrophy type 2A

Cited by 128 publications

References 1 publication

Increase in ultraviolet sensitivity by overexpression of calpastatin in ultraviolet-resistant UVr-1 cells derived from ultraviolet-sensitive human RSa cells

Increase in ultraviolet sensitivity by overexpression of calpastatin in ultraviolet-resistant UVr-1 cells derived from ultraviolet-sensitive human RSa cells

Calpain Inhibition Protects against Virus-Induced Apoptotic Myocardial Injury

Loss of Calpain-3 Autocatalytic Activity in LGMD2A Patients with Normal Protein Expression

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