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Difference between revisions of "Larsen 2012 CryoLetters"

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{{Publication
{{Publication
|title=Larsen S, Wright-Paradis C, Gnaiger E, Helge JW, Boushel RC (2012) Cryopreservation of human skeletal muscle impairs mitochondrial function. CryoLetters in press.
|title=Larsen S, Wright-Paradis C, Gnaiger E, Helge JW, Boushel RC (2012) Cryopreservation of human skeletal muscle impairs mitochondrial function. Cryo Letters 33:170-6.
|authors=Larsen S, Wright-Paradis C, Gnaiger E, Helge JW, Boushel RC
|info=[http://www.ncbi.nlm.nih.gov/pubmed/22825783 PMID: 22825783]
|authors=Larsen S, Wright-Paradis C, Gnaiger Erich, Helge JW, Boushel RC
|year=2012
|year=2012
|journal=CryoLetters
|journal=CryoLetters
|abstract=Previous studies have investigated if cryopreservation is a viable approach for functional mitochondrial analysis. Different tissues have been studied, and conflicting results have been published. The aim of the present study was to investigate if mitochondria in human skeletal muscle maintain functionality after long term cryopreservation (1 year). Skeletal muscle samples were preserved in dimethyl sulfoxide (Me2SO) for later analysis. Human skeletal muscle fibres were thawed and permeabilised with saponin, and mitochondrial respiration was measured by high-resolution respirometry. The capacity of oxidative phosphorylation (OXPHOS) was significantly (P<0.05) reduced in cryopreserved human skeletal muscle samples. Cryopreservation impaired respiration with substrates linked to Complex I more than for Complex II (P<0.05). Addition of cytochrome c revealed an increase in respiration indicating cytochrome c loos from the mitochondria. The results from this study demonstrate that normal mitochondrial functionality is not maintained in cryopreserved human skeletal muscle samples.
|abstract=Previous studies have investigated if cryopreservation is a viable approach for functional mitochondrial analysis. Different tissues have been studied, and conflicting results have been published. The aim of the present study was to investigate if mitochondria in human skeletal muscle maintain functionality after long term cryopreservation (1 year). Skeletal muscle samples were preserved in dimethyl sulfoxide (Me2SO) for later analysis. Human skeletal muscle fibres were thawed and permeabilised with saponin, and mitochondrial respiration was measured by high-resolution respirometry. The capacity of oxidative phosphorylation (OXPHOS) was significantly (''P''<0.05) reduced in cryopreserved human skeletal muscle samples. Cryopreservation impaired respiration with substrates linked to Complex I more than for Complex II (''P''<0.05). Addition of cytochrome ''c'' revealed an increase in respiration indicating cytochrome ''c'' loos from the mitochondria. The results from this study demonstrate that normal mitochondrial functionality is not maintained in cryopreserved human skeletal muscle samples.
|keywords=Cryopreservation, high-resolution respirometry, human skeletal muscle, mitochondrial function, permeabilised fibres
|keywords=Cryopreservation, High-resolution respirometry, Human skeletal muscle, Mitochondrial function, Permeabilised fibres
|mipnetlab=DK Copenhagen Boushel RC, AT Innsbruck Gnaiger E
|mipnetlab=SE Stockholm Boushel RC, AT Innsbruck Gnaiger E, CA Vancouver Boushel RC, DK Copenhagen Dela F, DK Copenhagen Larsen S
}}
}}
{{Labeling
{{Labeling
|instruments=Oxygraph-2k
|area=Respiration, Instruments;methods
|injuries=Ischemia-Reperfusion; Preservation
|injuries=Cryopreservation, Ischemia-reperfusion
|organism=Human
|organism=Human
|tissues=Skeletal muscle
|tissues=Skeletal muscle
|preparations=Permeabilized tissue
|preparations=Permeabilized tissue
|topics=Respiration; OXPHOS; ETS Capacity
|couplingstates=LEAK, OXPHOS
|pathways=N, S, NS
|instruments=Oxygraph-2k
}}
}}
== O2k-Publications ==
* [[O2k-Publications: Instruments;methods]]

Latest revision as of 02:47, 23 November 2021

Publications in the MiPMap
Larsen S, Wright-Paradis C, Gnaiger E, Helge JW, Boushel RC (2012) Cryopreservation of human skeletal muscle impairs mitochondrial function. Cryo Letters 33:170-6.

Β» PMID: 22825783

Larsen S, Wright-Paradis C, Gnaiger Erich, Helge JW, Boushel RC (2012) CryoLetters

Abstract: Previous studies have investigated if cryopreservation is a viable approach for functional mitochondrial analysis. Different tissues have been studied, and conflicting results have been published. The aim of the present study was to investigate if mitochondria in human skeletal muscle maintain functionality after long term cryopreservation (1 year). Skeletal muscle samples were preserved in dimethyl sulfoxide (Me2SO) for later analysis. Human skeletal muscle fibres were thawed and permeabilised with saponin, and mitochondrial respiration was measured by high-resolution respirometry. The capacity of oxidative phosphorylation (OXPHOS) was significantly (P<0.05) reduced in cryopreserved human skeletal muscle samples. Cryopreservation impaired respiration with substrates linked to Complex I more than for Complex II (P<0.05). Addition of cytochrome c revealed an increase in respiration indicating cytochrome c loos from the mitochondria. The results from this study demonstrate that normal mitochondrial functionality is not maintained in cryopreserved human skeletal muscle samples. β€’ Keywords: Cryopreservation, High-resolution respirometry, Human skeletal muscle, Mitochondrial function, Permeabilised fibres

β€’ O2k-Network Lab: SE Stockholm Boushel RC, AT Innsbruck Gnaiger E, CA Vancouver Boushel RC, DK Copenhagen Dela F, DK Copenhagen Larsen S


Labels: MiParea: Respiration, Instruments;methods 

Stress:Cryopreservation, Ischemia-reperfusion  Organism: Human  Tissue;cell: Skeletal muscle  Preparation: Permeabilized tissue 


Coupling state: LEAK, OXPHOS  Pathway: N, S, NS  HRR: Oxygraph-2k 


O2k-Publications