Staples 2010 Abstract IOC60: Difference between revisions

From Bioblast
No edit summary
No edit summary
Β 
(13 intermediate revisions by 5 users not shown)
Line 1: Line 1:
{{Abstract
{{Abstract
|title=Staples J, Chung D, Armstrong C (2010) Fast in, slow out: Kinetics of mitochondrial metabolic suppression during hibernation entrance and arousal. MiPNet15.10.
|title=Staples JF, Chung DJ, Armstrong C (2010) Fast in, slow out: Kinetics of mitochondrial metabolic suppression during hibernation entrance and arousal. MiPNet15.10.
|info=http://www.uwo.ca/biology/Faculty/staples/index.htm
|authors=Staples JF, James F, Chung DJ, Armstrong C
|authors=Staples J, James F, Chung D, Armstrong C
|year=2010
|year=2010
|event=IOC60
|event=MiPNet15.10_IOC60
|abstract=During entrance into a [[torpor]] bout the whole-animal metabolic rate of mammalian hibernators can decrease by up to 100-fold within a matter of hours. This metabolic suppression corresponds with a rapid decrease in succinate-fuelled State 3 respiration rates of liver mitochondria, measured at 37 Β°C. When isolated from 13-lined ground squirrel (''Ictodomys tridecemlineatus'') in early entrance (''T''b=30 Β°C), respiration decreased by 61% compared with interbout euthermia. Respiration did not decline further in late entrance (''T''b=15 Β°C) or steady-state torpor (''T''b=5 Β°C). In contrast, during early arousal (''T''b=15 Β°C), despite rapid increases in metabolic rate, State 3 respiration did not increase significantly from torpor levels. By the time ''T''b reached 30 Β°C in late arousal, however, respiration was 3-fold higher than torpor and continued to increase gradually, so that in interbout euthermia it was 6-fold higher than torpor and not significantly different from the summer active state. Preincubation with 2 mM isocitrate (removing oxaloacetate inhibition of succinate dehydrogenase) increased respiration only in torpor and early arousal. The β€œfast” initiation of mitochondrial metabolic suppression during entrance and its β€œslow” reversal during arousal suggests a mechanism that requires fairly high body temperatures.
|abstract=During entrance into a [[torpor]] bout the whole-animal metabolic rate of mammalian hibernators can decrease by up to 100-fold within a matter of hours. This metabolic suppression corresponds with a rapid decrease in succinate-fuelled State 3 respiration rates of liver mitochondria, measured at 37 Β°C. When isolated from 13-lined ground squirrel (''Ictodomys tridecemlineatus'') in early entrance (''T''b=30 Β°C), respiration decreased by 61% compared with interbout euthermia. Respiration did not decline further in late entrance (''T''b=15 Β°C) or steady-state torpor (''T''b=5 Β°C). In contrast, during early arousal (''T''b=15 Β°C), despite rapid increases in metabolic rate, State 3 respiration did not increase significantly from torpor levels. By the time ''T''b reached 30 Β°C in late arousal, however, respiration was 3-fold higher than torpor and continued to increase gradually, so that in interbout euthermia it was 6-fold higher than torpor and not significantly different from the summer active state. Preincubation with 2 mM isocitrate (removing oxaloacetate inhibition of succinate dehydrogenase) increased respiration only in torpor and early arousal. The β€œfast” initiation of mitochondrial metabolic suppression during entrance and its β€œslow” reversal during arousal suggests a mechanism that requires fairly high body temperatures.
|keywords=hibernation, mitochondria, Ictidomys, ground squirrel
|keywords=Hibernation, Mitochondria, Ictidomys, Ground squirrel
|mipnetlab=CA London Staples JF
|discipline=Mitochondrial Physiology
|discipline=Mitochondrial Physiology
|articletype=Workshop, MiPNet-online Publication
|articletype=Workshop, MiPNet-online Publication
|event=IOC60
}}
}}
{{Labeling
{{Labeling
|organism=Other Mammal
|organism=Other mammals
|tissues=Hepatocyte; Liver
|tissues=Liver
|preparations=Isolated Mitochondria
|preparations=Isolated mitochondria
|enzymes=Complex II; Succinate Dehydrogenase
|enzymes=Complex II;succinate dehydrogenase
|kinetics=Temperature
|topics=Temperature
|topics=Respiration; OXPHOS; ETS Capacity
|discipline=Mitochondrial Physiology
|discipline=Mitochondrial Physiology
|articletype=Workshop, MiPNet-online Publication
|articletype=Workshop, MiPNet-online Publication
|event=IOC60
}}
}}
[[Category:IOC60]]

Latest revision as of 16:52, 27 March 2018

Staples JF, Chung DJ, Armstrong C (2010) Fast in, slow out: Kinetics of mitochondrial metabolic suppression during hibernation entrance and arousal. MiPNet15.10.

Link:

Staples JF, James F, Chung DJ, Armstrong C (2010)

Event: MiPNet15.10_IOC60

During entrance into a torpor bout the whole-animal metabolic rate of mammalian hibernators can decrease by up to 100-fold within a matter of hours. This metabolic suppression corresponds with a rapid decrease in succinate-fuelled State 3 respiration rates of liver mitochondria, measured at 37 Β°C. When isolated from 13-lined ground squirrel (Ictodomys tridecemlineatus) in early entrance (Tb=30 Β°C), respiration decreased by 61% compared with interbout euthermia. Respiration did not decline further in late entrance (Tb=15 Β°C) or steady-state torpor (Tb=5 Β°C). In contrast, during early arousal (Tb=15 Β°C), despite rapid increases in metabolic rate, State 3 respiration did not increase significantly from torpor levels. By the time Tb reached 30 Β°C in late arousal, however, respiration was 3-fold higher than torpor and continued to increase gradually, so that in interbout euthermia it was 6-fold higher than torpor and not significantly different from the summer active state. Preincubation with 2 mM isocitrate (removing oxaloacetate inhibition of succinate dehydrogenase) increased respiration only in torpor and early arousal. The β€œfast” initiation of mitochondrial metabolic suppression during entrance and its β€œslow” reversal during arousal suggests a mechanism that requires fairly high body temperatures.

β€’ Keywords: Hibernation, Mitochondria, Ictidomys, Ground squirrel

β€’ O2k-Network Lab: CA London Staples JF


Labels:


Organism: Other mammals  Tissue;cell: Liver  Preparation: Isolated mitochondria  Enzyme: Complex II;succinate dehydrogenase  Regulation: Temperature 




Cookies help us deliver our services. By using our services, you agree to our use of cookies.