Contractile activity-induced mitochondrial biogenesis and mTORC1

Carter, Heather N.; Hood, David A.

doi:10.1152/ajpcell.00156.2012

Cited by 35 publications

(30 citation statements)

References 49 publications

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“…In this study, we found that AMPK is involved in metformin-induced CEBPD expression. However, rapamycin had no effect on AMPK activation in myotubes [49], which is consistent with our findings. Therefore, combined metformin and rapamycin treatment can enhance autophagic cell death through AMPK-dependent and AMPK-independent pathways, respectively, and reduce the development of drug resistance in HCC (Figure 7).…”

Section: Discussionsupporting

confidence: 92%

Metformin promotes apoptosis in hepatocellular carcinoma through the CEBPD-induced autophagy pathway

et al. 2017

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Metformin, as an AMP-activated protein kinase (AMPK) activator, can activate autophagy. A study showed that metformin decreased the risk of hepatocellular carcinoma (HCC) in diabetic patients. However, the detailed mechanism in the metformin-mediated anticancer effect remains an open question. Transcription factor CCAAT/enhancer-binding protein delta (CEBPD) has been suggested to serve as a tumor suppressor and is responsive to multiple anticancer drugs in HCC. In this study, we found that CEBPD and autophagy are involved in metformin-induced cell apoptosis in Huh7 cells. The underlying mechanisms in this process included a reduction in Src-mediated CEBPD protein degradation and an increase in CEBPD-regulated LC3B and ATG3 gene transcription under metformin treatment. We also found that AMPK is involved in metformin-induced CEBPD expression. Combined treatment with metformin and rapamycin can enhance autophagic cell death through the AMPK-dependent and AMPK-independent pathway, respectively. Taken together, we provide a new insight and therapeutic approach by targeting autophagy in the treatment of HCC.

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Section: Discussionsupporting

confidence: 92%

Metformin promotes apoptosis in hepatocellular carcinoma through the CEBPD-induced autophagy pathway

et al. 2017

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“…Mitochondria-enriched fractions were obtained using an adapted protocol (6,17). Briefly, the medium was removed from myoblasts and washed with ice-cold PBS (Wisent).…”

Section: Methodsmentioning

confidence: 99%

Oxidative stress-induced mitochondrial fragmentation and movement in skeletal muscle myoblasts

Iqbal

Hood

2014

American Journal of Physiology-Cell Physiology

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Iqbal S, Hood DA. Oxidative stress-induced mitochondrial fragmentation and movement in skeletal muscle myoblasts. Am J Physiol Cell Physiol 306: C1176 -C1183, 2014. First published April 16, 2014; doi:10.1152/ajpcell.00017.2014.-Mitochondria are dynamic organelles, capable of altering their morphology and function. However, the mechanisms governing these changes have not been fully elucidated, particularly in muscle cells. We demonstrated that oxidative stress with H2O2 resulted in a 41% increase in fragmentation of the mitochondrial reticulum in myoblasts within 3 h of exposure, an effect that was preceded by a reduction in membrane potential. Using live cell imaging, we monitored mitochondrial motility and found that oxidative stress resulted in a 30% reduction in the average velocity of mitochondria. This was accompanied by parallel reductions in both organelle fission and fusion. The attenuation in mitochondrial movement was abolished by the addition of N-acetylcysteine. To investigate whether H2O2-induced fragmentation was mediated by dynaminrelated protein 1, we incubated cells with mDivi1, an inhibitor of dynamin-related protein 1 translocation to mitochondria. mDivi1 attenuated oxidative stress-induced mitochondrial fragmentation by 27%. Moreover, we demonstrated that exposure to H2O2 upregulated endoplasmic reticulum-unfolded protein response markers before the initiation of mitophagy signaling and the mitochondrial-unfolded protein response. These findings indicate that oxidative stress is a vital signaling mechanism in the regulation of mitochondrial morphology and motility. mitochondria; mitochondrial movement; oxidative stress; mitochondrial morphology MITOCHONDRIA ARE ESSENTIAL ORGANELLES for the life and death of eukaryotic cells. They play key roles in aerobic energy production, apoptosis, mitophagy, and cellular signaling. These versatile organelles were once thought to be static and rigid structures. More recently, mitochondria have been appreciated for their dynamic nature. They can change their distribution by moving along cytoskeletal tracks or change their overall morphology. The maintenance and appropriate networking of mitochondria within the cell is mediated by fusion and opposing fission processes. Fusion involves the mixing of mitochondrial material, whereas fission divides the organelle into smaller components. Disruptions in either of these opposing events can lead to developmental defects and disease (29), suggesting that the proper maintenance of mitochondrial morphology is critical for normal cell function.Mitochondrial fission is orchestrated, in part, by dynaminrelated protein 1 (Drp1) (4, 25), a protein that is a GTPase of the dynamin family. All dynamin members are structurally similar but functionally diverse GTP-binding proteins. Drp1 assists in mitochondrial fission by polymerizing into a ring-like structure around the organelle. The cross-bridging of the GTPase domains of adjacent Drp1 proteins results in GTP hydrolysis, constriction, and the ultimate severing of mitochon...

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“…Interestingly, it appears that the Tfam gene is responsive to exercise, as an elevation in the mRNA expression of Tfam has been observed following a single session of endurance exercise 11, 13, 36. Furthermore, increases in TFAM protein content with skeletal muscle have been documented in several in vitro 3, 37 and in vivo 38, 39, 40 animal endurance exercise training paradigms, as well as in human skeletal muscle 41 . In response to repeated bouts of exercise, a sequential series of events unfurls.…”

Section: Mitochondrial Transcription Factor Amentioning

confidence: 99%

Function of specialized regulatory proteins and signaling pathways in exercise-induced muscle mitochondrial biogenesis

Erlich

Tryon

Crilly

et al. 2016

Integrative Medicine Research

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Skeletal muscle mitochondrial content and function are regulated by a number of specialized molecular pathways that remain to be fully defined. Although a number of proteins have been identified to be important for the maintenance of mitochondria in quiescent muscle, the requirement for these appears to decrease with the activation of multiple overlapping signaling events that are triggered by exercise. This makes exercise a valuable therapeutic tool for the treatment of mitochondrially based metabolic disorders. In this review, we summarize some of the traditional and more recently appreciated pathways that are involved in mitochondrial biogenesis in muscle, particularly during exercise.

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Contractile activity-induced mitochondrial biogenesis and mTORC1

Abstract: Carter HN, Hood DA. Contractile activity-induced mitochondrial biogenesis and mTORC1.

Cited by 35 publications

References 49 publications

Metformin promotes apoptosis in hepatocellular carcinoma through the CEBPD-induced autophagy pathway

Metformin promotes apoptosis in hepatocellular carcinoma through the CEBPD-induced autophagy pathway

Oxidative stress-induced mitochondrial fragmentation and movement in skeletal muscle myoblasts

Function of specialized regulatory proteins and signaling pathways in exercise-induced muscle mitochondrial biogenesis

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