Apoptosis repressor with caspase recruitment domain (ARC) inhibits myogenic differentiation

Hunter, Arwen L.; Zhang, Jingchun; Chen, Shirley C.; Si, Xiaoning; Wong, Brian W.; Ekhterae, Daryoush; Luo, Honglin; Granville, David J.

doi:10.1016/j.febslet.2007.01.050

Cited by 18 publications

(16 citation statements)

References 24 publications

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“…However, new research shows that ARC participates in preconditioning-triggered cardioprotection by blocking cytochrome C release and caspase-3 activation, and activation of caspase-3 caused by Dox is blocked by ARC (An et al, 2009). Furthermore, ARC inhibits myoblast differentiation associated with caspase-3 activation (Hunter et al, 2007). Coincident with these findings, our results showed that mouse-derived ARC can significantly reduce caspase-3 mRNA and protein levels.…”

Section: Discussionsupporting

confidence: 81%

Exogenous ARC down-regulates caspase-3 expression and inhibits apoptosis of broiler chicken cardiomyocytes exposed to hydrogen peroxide

Guo

et al. 2012

Avian Pathology

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Apoptosis repressor with caspase recruitment domain (ARC) is highly involved in apoptosis induced by oxidative stress or ischaemia/reperfusion injury. Furthermore, even though the exact mechanism is still unknown, some studies suggest that exogenous ARC also possesses anti-apoptotic ability. The study investigated whether mouse-derived ARC acquires anti-apoptotic ability and the pathway of regulation in chick embryo cardiomyocytes. To evaluate whether mouse-derived ARC can inhibit chick embryo cardiomyocyte apoptosis induced by hydrogen peroxide, recombinant pcDNA3.1/ARC plasmid was acquired and transfected into chick embryo cardiomyocytes. ARC-related gene (caspase-2, caspase-8, caspase-3, and caspase-9, cytochrome C, bcl-2, and XIAP) mRNA and protein expression levels were detected by real-time polymerase chain reaction and western blotting, respectively. Here we demonstrate that hydrogen peroxide induced apoptosis in chick embryo cardiomyocytes in a time-dependent manner and that this effect could be suppressed by mouse-derived ARC expression. Moreover, unlike endogenous ARC, exogenous ARC was exclusively expressed in the cytoplasm and down-regulated caspase-2, caspase-8, and caspase-3, bcl-2, and XIAP gene expression levels. However, only caspase-3 protein levels were decreased. In addition, threonine 149 phosphorylation by CK2 was required for exogenous ARC to exert an antiapoptotic effect in chicken embryo cardiomyocytes and suggested exogenous ARC may in part share the same pathway of regulation with endogenous ARC. These results indicate that mouse-derived ARC plays an important role in protection of chick embryo cardiomyocytes against oxidative stress apoptosis by inhibiting caspase-3 mRNA and protein expression levels.

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Section: Discussionsupporting

confidence: 81%

Exogenous ARC down-regulates caspase-3 expression and inhibits apoptosis of broiler chicken cardiomyocytes exposed to hydrogen peroxide

Guo

et al. 2012

Avian Pathology

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“…Fernando et al (Fernando et al, 2002) provided evidence that an apoptotic caspase, caspase-3, was required for skeletal myoblast differentiation, and research on the effects of apoptosis repressor with caspase recruitment domain (ARC) on cardiac-muscle fusion has suggested a role for caspase-3 in cardiomyocyte differentiation (Hunter et al, 2007). Although these results clearly implicate the effector caspase in differentiation, neither report identified components of the pathway that are responsible for caspase-3 activation.…”

Section: Discussionmentioning

confidence: 99%

A non-apoptotic role for caspase-9 in muscle differentiation

Murray

McMahon

Howley

et al. 2008

Journal of Cell Science

154

117

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Caspases, a family of cysteine proteases most often investigated for their roles in apoptosis, have also been demonstrated to have functions that are vital for the efficient execution of cell differentiation. One such role that has been described is the requirement of caspase-3 for the differentiation of skeletal myoblasts into myotubes but, as yet, the mechanism leading to caspase-3 activation in this case remains elusive. Here, we demonstrate that caspase-9, an initiator caspase in the mitochondrial death pathway, is responsible for the activation of caspase-3 in differentiating C2C12 cells. Reduction of caspase-9 levels, using an shRNA construct, prevented caspase-3 activation and inhibited myoblast fusion. Myosin-heavychain expression, which accompanies myoblastic differentiation, was not caspase-dependent. Overexpression of Bcl-xL, a protein that inhibits caspase-9 activation, had the same effect on muscle differentiation as knockdown of caspase-9. These data suggest that the mitochondrial pathway is required for differentiation; however, the release of cytochrome c or Smac (Diablo) could not be detected, raising the possibility of a novel mechanism of caspase-9 activation during muscle differentiation.

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“…Several studies have examined the signal cascades that activate and modulate caspase 3 during non-death responses, yet a definitive control mechanism has not been elucidated. [37][38][39] Such inactivation could indirectly end CAD activity by discontinuing proteolysis of ICAD. Intact ICAD (both long and short isoforms) can disassemble the CAD dimer, moreover our observation that ICAD-L is only partial cleaved (with a large pool of intact ICAD-L remaining) suggests that this mechanism maybe operative to prevent extensive DNA fragmentation.…”

Section: Curbing the Caspase3/cad Signalmentioning

confidence: 99%