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Difference between revisions of "Neufer 2014 Abstract MiP2014"

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{{Abstract
{{Abstract
|title=Assessing ATP production and oxygen consumption simultaneously in permeabilized fibers: ATP/O.
|title=Assessing ATP production and oxygen consumption simultaneously in permeabilized fibers: ATP/O.
|info=[[File:Neufer_DP.jpg|240px|right|Neufer DP]] [http://www.mitophysiology.org/index.php?mip2014 MiP2014], [[Laner 2014 Mitochondr Physiol Network MiP2014|Book of Abstracts Open Access]]
|info=[[File:Neufer_PD.jpg|240px|right|Neufer DP]] [http://www.mitophysiology.org/index.php?mip2014 MiP2014], [[Laner 2014 Mitochondr Physiol Network MiP2014|Book of Abstracts Open Access]]
|authors=Lark DS, Ryan T, Anderson EJ, Neufer DP
|authors=Lark DS, Ryan T, Anderson EJ, Neufer DP
|year=2014
|year=2014

Revision as of 17:25, 11 August 2014

Assessing ATP production and oxygen consumption simultaneously in permeabilized fibers: ATP/O.

Link:

Neufer DP

MiP2014, Book of Abstracts Open Access

Lark DS, Ryan T, Anderson EJ, Neufer DP (2014)

Event: MiP2014

The biochemical efficiency of oxidative phosphorylation (OXPHOS), quantified as the amount of ATP produced per oxygen atom consumed (ATP/O), is vital to maintaining proper myocyte energetics. However, despite its central importance, it is difficult to experimentally determine the ATP/O ratio as a function of metabolic demand, and therefore, the relationship between OXPHOS efficiency and metabolic demand is poorly understood. O2 consumption (high-resolution respirometry) and ATP production (determined fluorometrically using a 2-deoxyglucose – hexokinase – glucose-6-phosphate dehydrogenase – NADP+ respiratory clamp system [1]), rates were measured simultaneously in permeabilized mouse oxidative and glycolytic skeletal muscle fiber bundles using a customized OROBOROS Oxygraph-2k.

At low [ADP] (5-20 Β΅M), the ATP/O ratio increased as a function of [ADP], independent of an increase in O2 consumption. Maximal ATP/O peaked at ~2.0 and was not different between oxidative and glycolytic muscle. Pharmacological inhibition of adenylate kinase decreased ATP production rate but did not alter ADP-dependent increases in OXPHOS efficiency.

These findings suggest that mitochondria respond to low levels of metabolic demand by initially increasing OXPHOS efficiency.


β€’ O2k-Network Lab: US NC Greenville Neufer PD, US NC Greenville East Carolina Univ


Labels: MiParea: Respiration 


Organism: Mouse  Tissue;cell: Skeletal muscle  Preparation: Permeabilized tissue 

Regulation: ADP, ATP production, Coupling efficiency;uncoupling  Coupling state: OXPHOS 

HRR: Oxygraph-2k 

MiP2014 

Affiliation

1-East Carolina Diabetes Obesity Inst; 2-Dep Kinesiolog; 3-Dep Physiol; 4-Dep Pharmacolog Toxicolog; East Carolina Univ, Greenville, NC, USA. – [email protected]

References and acknowledgements

Supported by: National Institute of Health R01 DK096907 (USA).

  1. Gouspillou G, Rouland R, Calmettes G, Deschodt-Arsac V, Franconi J-M, Bourdel-Marchasson I, Diolez P (2011) Accurate determination of the oxidative phosphorylation affinity for ADP in isolated mitochondria. PloS One 6:e20709.