Induction of protein degradation in skeletal muscle by a phorbol ester involves upregulation of the ubiquitin–proteasome proteolytic pathway

Wyke, Stacey M.; Tisdale, Michael J.

doi:10.1016/j.lfs.2005.11.014

Cited by 27 publications

(25 citation statements)

References 25 publications

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“…Resveratrol has been investigated as a possible treatment to prevent muscle wasting. Resveratrol has been consistently shown to inhibit protein degradation and to attenuate atrophy of skeletal muscle fibers in vitro (Busquets et al 2007;Russell et al 2006;Wyke et al 2004;Wyke and Tisdale 2006). In C2C12 myotubes resveratrol treatment inhibited protein degradation induced by proteolysis inducing factor (PIF) (Wyke et al 2004), Angiotensin I and II (Russell et al 2006), and the phorbal ester 12-0-tetradecanoylphorbol-13-acetetate (TPA) .…”

Section: The Effects Of Resveratrol On Protein Catabolism and Muscle mentioning

confidence: 99%

Cellular effects of resveratrol in skeletal muscle

Naylor

2009

Life Sciences

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Section: The Effects Of Resveratrol On Protein Catabolism and Muscle mentioning

confidence: 99%

Cellular effects of resveratrol in skeletal muscle

Naylor

2009

Life Sciences

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“…Indeed, it has been shown that various signaling molecules in mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways were altered by accumulation of ␣-syn in a variety of cell cultures (35,50). In the present study the role of the PKC signaling pathway was addressed for the regulation of proteasome activity because it was recently shown that treatment of skeletal muscle with phorbol ester stimulated proteasome activity (39). Consistent with a previous study using neuroblastoma cells and human brains (40), ␣-syn was shown to bind with PKC, thereby down-regulating the activity of this molecule in ␣-syn-overexpressing MG63 cells (Fig.…”

Section: Discussionmentioning

confidence: 91%

“…In this regard we especially focused on the potential role of PKC since it was recently shown that treatment of skeletal muscle by phorbol ester resulted in stimulation of proteasome activity (39) and it was previously shown that ␣-syn bound with PKC and downregulated the activity of PKC in ␣-syn overexpressing neuroblastoma cells (40).…”

Section: Alteration Of G 1 Cell Cycle Regulators and Decreased Proteamentioning

confidence: 99%

α-Synuclein Stimulates Differentiation of Osteosarcoma Cells

Fujita

Sugama

Nakai

et al. 2007

Journal of Biological Chemistry

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Because a limited study previously showed that ␣-synuclein (␣-syn), the major pathogenic protein for Parkinson disease, was expressed in differentiating brain tumors as well as various peripheral cancers, the main objective of the present study was to determine whether ␣-syn might be involved in the regulation of tumor differentiation. For this purpose, ␣-syn and its non-amyloidogenic homologue ␤-syn were stably transfected to human osteosarcoma MG63 cell line. Compared with ␤-syn-overexpressing and vector-transfected cells, ␣-syn-overexpressing cells exhibited distinct features of differentiated osteoblastic phenotype, as shown by up-regulation of alkaline phosphatase and osteocalcin as well as inductive matrix mineralization. Further studies revealed that proteasome activity was significantly decreased in ␣-syn-overexpressing cells compared with other cell types, consistent with the fact that proteasome inhibitors stimulate differentiation of various osteoblastic cells. In ␣-syn-overexpressing cells, protein kinase C (PKC) activity was significantly decreased, and reactivation of PKC by phorbol ester significantly restored the proteasome activity and abrogated cellular differentiation. Moreover, activity of lysosome was up-regulated in ␣-syn-overexpressing cells, and treatment of these cells with autophagy-lysosomal inhibitors resulted in a decrease of proteasome activity associated with up-regulation of ␣-syn expression, leading to enhance cellular differentiation. Taken together, these results suggest that the stimulatory effect of ␣-syn on tumor differentiation may be attributed to down-regulation of proteasome, which is further modulated by alterations of various factors, such as protein kinase C signaling pathway and a autophagy-lysosomal degradation system. Thus, the mechanism of ␣-syn regulation of tumor differentiation and neuropathological effects of ␣-syn may considerably overlap with each other.

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“…Several PEs have been shown to have potent anti-inflammatory properties in experiments utilizing known pro-inflammatory factors [32,33]. Skeletal muscle exhibits enhanced proteolysis in response to the proinflammatory agent 12-O-tetradecanoylphorbol-13-acetate (TPA) [34]. TPA likely upregulates the ubiquitin proteasome pathwaythrough NFkB.…”

Section: Potential Aid For Post-damage Muscle Regenerationmentioning

confidence: 99%

Phytoecdysteroids: A Novel, Non-Androgenic Alternative for Muscle Health and Performance

McBride¹

2013

J Steroids Horm Sci

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Induction of protein degradation in skeletal muscle by a phorbol ester involves upregulation of the ubiquitin–proteasome proteolytic pathway

Cited by 27 publications

References 25 publications

Cellular effects of resveratrol in skeletal muscle

Cellular effects of resveratrol in skeletal muscle

α-Synuclein Stimulates Differentiation of Osteosarcoma Cells

Phytoecdysteroids: A Novel, Non-Androgenic Alternative for Muscle Health and Performance

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