Difference between revisions of "Bayot 2014 Biochimie"
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{{Publication | {{Publication | ||
|title=Bayot A, Gareil M, Chavatte L, Hamon MP, L'hermitte-Stead C, Beaumatin F, Priault M, Rustin P, Lombès A, Friguet B, Bulteau AL ( | |title=Bayot A, Gareil M, Chavatte L, Hamon MP, L'hermitte-Stead C, Beaumatin F, Priault M, Rustin P, Lombès A, Friguet B, Bulteau AL (2014) Effect of Lon protease knockdown on mitochondrial function in HeLa cells. Biochimie 100:38-47. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/24355201 PMID: 24355201] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/24355201 PMID: 24355201] | ||
|authors=Bayot A, Gareil M, Chavatte L, Hamon MP, L'hermitte-Stead C, Beaumatin F, Priault M, Rustin P, Lombes A, Friguet B, Bulteau AL | |authors=Bayot A, Gareil M, Chavatte L, Hamon MP, L'hermitte-Stead C, Beaumatin F, Priault M, Rustin P, Lombes A, Friguet B, Bulteau AL | ||
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|journal=Biochimie | |journal=Biochimie | ||
|abstract=ATP-dependent proteases are currently emerging as key regulators of mitochondrial functions. Among these proteolytic systems, Lon protease is involved in the control of selective protein turnover in the mitochondrial matrix. In the absence of Lon, yeast cells have been shown to accumulate electron-dense inclusion bodies in the matrix space, to loose integrity of mitochondrial genome and to be respiratory deficient. In order to address the role of Lon in mitochondrial functionality in human cells, we have set up a HeLa cell line stably transfected with a vector expressing a shRNA under the control of a promoter which is inducible with doxycycline. We have demonstrated that reduction of Lon protease results in a mild phenotype in this cell line in contrast with what have been observed in other cell types such as WI-38 fibroblasts. Nevertheless, deficiency in Lon protease led to an increase in ROS production and to an accumulation of carbonylated protein in the mitochondria. Our study suggests that Lon protease has a wide variety of targets and is likely to play different roles depending of the cell type. | |abstract=ATP-dependent proteases are currently emerging as key regulators of mitochondrial functions. Among these proteolytic systems, Lon protease is involved in the control of selective protein turnover in the mitochondrial matrix. In the absence of Lon, yeast cells have been shown to accumulate electron-dense inclusion bodies in the matrix space, to loose integrity of mitochondrial genome and to be respiratory deficient. In order to address the role of Lon in mitochondrial functionality in human cells, we have set up a HeLa cell line stably transfected with a vector expressing a shRNA under the control of a promoter which is inducible with doxycycline. We have demonstrated that reduction of Lon protease results in a mild phenotype in this cell line in contrast with what have been observed in other cell types such as WI-38 fibroblasts. Nevertheless, deficiency in Lon protease led to an increase in ROS production and to an accumulation of carbonylated protein in the mitochondria. Our study suggests that Lon protease has a wide variety of targets and is likely to play different roles depending of the cell type. | ||
|keywords= | |keywords=Lon protease, Mitochondria, HeLa cells, Protein oxidation, Cellular redox status, FCCP, HBSS, Hank's buffered salt solution, HeLa cells, Lon protease, MTT, Mitochondria, Protein oxidation, ROS, VO(2), Carbonyl cyanide-chloro phenylhydrazine, carbonyl cyanide-trifluoromethoxy phenylhydrazine, Cytochrome c oxidase, Oxygen consumption rate, Reactive oxygen species | ||
|mipnetlab=FR Paris Bouillaud F | |mipnetlab=FR Paris Bouillaud F | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration | |area=Respiration, Genetic knockout;overexpression | ||
|organism=Human | |||
|tissues=Endothelial;epithelial;mesothelial cell, HeLa | |||
|couplingstates=LEAK, ROUTINE, ET | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} | ||
Latest revision as of 16:55, 9 November 2017
| Bayot A, Gareil M, Chavatte L, Hamon MP, L'hermitte-Stead C, Beaumatin F, Priault M, Rustin P, Lombès A, Friguet B, Bulteau AL (2014) Effect of Lon protease knockdown on mitochondrial function in HeLa cells. Biochimie 100:38-47. |
Bayot A, Gareil M, Chavatte L, Hamon MP, L'hermitte-Stead C, Beaumatin F, Priault M, Rustin P, Lombes A, Friguet B, Bulteau AL (2014) Biochimie
Abstract: ATP-dependent proteases are currently emerging as key regulators of mitochondrial functions. Among these proteolytic systems, Lon protease is involved in the control of selective protein turnover in the mitochondrial matrix. In the absence of Lon, yeast cells have been shown to accumulate electron-dense inclusion bodies in the matrix space, to loose integrity of mitochondrial genome and to be respiratory deficient. In order to address the role of Lon in mitochondrial functionality in human cells, we have set up a HeLa cell line stably transfected with a vector expressing a shRNA under the control of a promoter which is inducible with doxycycline. We have demonstrated that reduction of Lon protease results in a mild phenotype in this cell line in contrast with what have been observed in other cell types such as WI-38 fibroblasts. Nevertheless, deficiency in Lon protease led to an increase in ROS production and to an accumulation of carbonylated protein in the mitochondria. Our study suggests that Lon protease has a wide variety of targets and is likely to play different roles depending of the cell type. • Keywords: Lon protease, Mitochondria, HeLa cells, Protein oxidation, Cellular redox status, FCCP, HBSS, Hank's buffered salt solution, HeLa cells, Lon protease, MTT, Mitochondria, Protein oxidation, ROS, VO(2), Carbonyl cyanide-chloro phenylhydrazine, carbonyl cyanide-trifluoromethoxy phenylhydrazine, Cytochrome c oxidase, Oxygen consumption rate, Reactive oxygen species
• O2k-Network Lab: FR Paris Bouillaud F
Labels: MiParea: Respiration, Genetic knockout;overexpression
Organism: Human
Tissue;cell: Endothelial;epithelial;mesothelial cell, HeLa
Coupling state: LEAK, ROUTINE, ET
HRR: Oxygraph-2k
