Difference between revisions of "Iyer 2009 Mitochondrion"
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{{Publication | {{Publication | ||
|title=Iyer S, Thomas R, Portell F, Dunham L, Quigley C, Bennett JP (2009) Recombinant mitochondrial transcription factor A with N-terminal mitochondrial transduction domain increases respiration and mitochondrial gene expression. Mitochondrion 9: 196-203. | |title=Iyer S, Thomas R, Portell F, Dunham L, Quigley C, Bennett JP (2009) Recombinant mitochondrial transcription factor A with N-terminal mitochondrial transduction domain increases respiration and mitochondrial gene expression. Mitochondrion 9:196-203. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19460293 PMID: 19460293] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/19460293 PMID: 19460293 Open Access] | ||
|authors=Iyer S, Thomas R, Portell F, Dunham L, Quigley C, Bennett JP | |authors=Iyer S, Thomas R, Portell F, Dunham L, Quigley C, Bennett JP | ||
|year=2009 | |year=2009 | ||
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|abstract=We developed a scalable procedure to produce human mitochondrial transcription factor A (TFAM) modified with an N-terminal protein transduction domain (PTD) and mitochondrial localization signal (MLS) that allow it to cross membranes and enter mitochondria through its āmitochondrial transduction domainā (MTD = PTD + MLS). Alexa488-labeled MTDāTFAM rapidly entered the mitochondrial compartment of cybrid cells carrying the G11778A LHON mutation. ''MTDāTFAM'' reversibly increased respiration and levels of respiratory proteins. ''In vivo'' treatment of mice with MTDāTFAM increased motor endurance and complex I-driven respiration in mitochondria from brain and skeletal muscle. MTDāTFAM increases mitochondrial bioenergetics and holds promise for treatment of mitochondrial diseases involving deficiencies of energy production. | |abstract=We developed a scalable procedure to produce human mitochondrial transcription factor A (TFAM) modified with an N-terminal protein transduction domain (PTD) and mitochondrial localization signal (MLS) that allow it to cross membranes and enter mitochondria through its āmitochondrial transduction domainā (MTD = PTD + MLS). Alexa488-labeled MTDāTFAM rapidly entered the mitochondrial compartment of cybrid cells carrying the G11778A LHON mutation. ''MTDāTFAM'' reversibly increased respiration and levels of respiratory proteins. ''In vivo'' treatment of mice with MTDāTFAM increased motor endurance and complex I-driven respiration in mitochondria from brain and skeletal muscle. MTDāTFAM increases mitochondrial bioenergetics and holds promise for treatment of mitochondrial diseases involving deficiencies of energy production. | ||
|keywords=TFAM, Respiration, Mitochondrial gene expression, Respiratory proteins | |keywords=TFAM, Respiration, Mitochondrial gene expression, Respiratory proteins | ||
|mipnetlab=US VA Richmond Bennett JP | |mipnetlab=US VA Richmond Bennett JP, US VA Richmond Iyer S | ||
|discipline=Biomedicine | |discipline=Biomedicine | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
| | |area=Respiration, Genetic knockout;overexpression | ||
|organism=Human | |organism=Human | ||
|tissues=Skeletal | |tissues=Skeletal muscle, Nervous system | ||
|enzymes=Complex I | |enzymes=Complex I | ||
| | |diseases=Inherited | ||
| | |couplingstates=ROUTINE | ||
|instruments=Oxygraph-2k | |||
|discipline=Biomedicine | |discipline=Biomedicine | ||
}} | }} |
Latest revision as of 14:42, 20 March 2015
Iyer S, Thomas R, Portell F, Dunham L, Quigley C, Bennett JP (2009) Recombinant mitochondrial transcription factor A with N-terminal mitochondrial transduction domain increases respiration and mitochondrial gene expression. Mitochondrion 9:196-203. |
Iyer S, Thomas R, Portell F, Dunham L, Quigley C, Bennett JP (2009) Mitochondrion
Abstract: We developed a scalable procedure to produce human mitochondrial transcription factor A (TFAM) modified with an N-terminal protein transduction domain (PTD) and mitochondrial localization signal (MLS) that allow it to cross membranes and enter mitochondria through its āmitochondrial transduction domainā (MTD = PTD + MLS). Alexa488-labeled MTDāTFAM rapidly entered the mitochondrial compartment of cybrid cells carrying the G11778A LHON mutation. MTDāTFAM reversibly increased respiration and levels of respiratory proteins. In vivo treatment of mice with MTDāTFAM increased motor endurance and complex I-driven respiration in mitochondria from brain and skeletal muscle. MTDāTFAM increases mitochondrial bioenergetics and holds promise for treatment of mitochondrial diseases involving deficiencies of energy production. ā¢ Keywords: TFAM, Respiration, Mitochondrial gene expression, Respiratory proteins
ā¢ O2k-Network Lab: US VA Richmond Bennett JP, US VA Richmond Iyer S
Labels: MiParea: Respiration, Genetic knockout;overexpression
Pathology: Inherited
Organism: Human Tissue;cell: Skeletal muscle, Nervous system
Enzyme: Complex I
Coupling state: ROUTINE
HRR: Oxygraph-2k