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Difference between revisions of "Astin 2013 Sci Rep"

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{{Publication
{{Publication
|title=Astin R, Bentham R, Djafarzadeh S, Horscroft JA, Kuc RE, Leung PS, Skipworth JR, Vicencio JM, Davenport AP, Murray AJ, Takala J, Jakob SM, Montgomery H, Szabadkai G (2013) No evidence for a local renin-angiotensin system in liver mitochondria. Sci Rep 3:2467.
|title=Astin R, Bentham R, Djafarzadeh S, Horscroft JA, Kuc RE, Leung PS, Skipworth JR, Vicencio JM, Davenport AP, Murray AJ, Takala J, Jakob SM, Montgomery H, Szabadkai G (2013) No evidence for a local renin-angiotensin system in liver mitochondria. Sci Rep 3:2467.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/23959064 PMID:23959064]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/23959064 PMID:23959064 Open Access]
|authors=Astin R, Bentham R, Djafarzadeh S, Horscroft JA, Kuc RE, Leung PS, Skipworth JR, Vicencio JM, Davenport AP, Murray AJ, Takala J, Jakob SM, Montgomery H, Szabadkai G
|authors=Astin R, Bentham R, Djafarzadeh S, Horscroft JA, Kuc RE, Leung PS, Skipworth JR, Vicencio JM, Davenport AP, Murray AJ, Takala J, Jakob SM, Montgomery H, Szabadkai G
|year=2013
|year=2013
|journal=Sci Rep
|journal=Sci Rep
|abstract=The circulating, endocrine renin-angiotensin system (RAS) is important to circulatory homeostasis, while ubiquitous tissue and cellular RAS play diverse roles, including metabolic regulation. Indeed, inhibition of RAS is associated with improved cellular oxidative capacity. Recently it has been suggested that an intra-mitochondrial RAS directly impacts on metabolism. Here we sought to rigorously explore this hypothesis. Radiolabelled ligand-binding and unbiased proteomic approaches were applied to purified mitochondrial sub-fractions from rat liver, and the impact of AngII on mitochondrial function assessed. Whilst high-affinity AngII binding sites were found in the mitochondria-associated membrane (MAM) fraction, no RAS components could be detected in purified mitochondria. Moreover, AngII had no effect on the function of isolated mitochondria at physiologically relevant concentrations. We thus found no evidence of endogenous mitochondrial AngII production, and conclude that the effects of AngII on cellular energy metabolism are not mediated through its direct binding to mitochondrial targets.
|abstract=The circulating, endocrine renin-angiotensin system (RAS) is important to circulatory homeostasis, while ubiquitous tissue and cellular RAS play diverse roles, including metabolic regulation. Indeed, inhibition of RAS is associated with improved cellular oxidative capacity. Recently it has been suggested that an intra-mitochondrial RAS directly impacts on metabolism. Here we sought to rigorously explore this hypothesis. Radiolabelled ligand-binding and unbiased proteomic approaches were applied to purified mitochondrial sub-fractions from rat liver, and the impact of AngII on mitochondrial function assessed. Whilst high-affinity AngII binding sites were found in the mitochondria-associated membrane (MAM) fraction, no RAS components could be detected in purified mitochondria. Moreover, AngII had no effect on the function of isolated mitochondria at physiologically relevant concentrations. We thus found no evidence of endogenous mitochondrial AngII production, and conclude that the effects of AngII on cellular energy metabolism are not mediated through its direct binding to mitochondrial targets.
|mipnetlab=UK Cambridge Murray AJ, UK Cambridge University of Cambridge
|mipnetlab=UK Cambridge Murray AJ, CH Bern Djafarzadeh S
}}
}}
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{{Labeling
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== Correction ==
== Correction ==
An OROBOROS Oxygraph-2k, Innsbruck, Austria was used in this publication, whereas the "Graz, Austria" reference usually credits the Anton Paar/OROBOROS Oxygraph, the first-generation instrument for high-resolution respirometry, which was replaced by the Oxygraph-2k in 2002.
An Oroboros Oxygraph-2k, Innsbruck, Austria was used in this publication, whereas the "Graz, Austria" reference usually credits the Anton Paar/Oroboros Oxygraph, the first-generation instrument for high-resolution respirometry, which was replaced by the Oxygraph-2k in 2002.
* ''Further details'': [[Gnaiger 2012 Abstract Bioblast-Gentle Science]]
* ''Further details'': [[Gnaiger 2012 Abstract Bioblast-Gentle Science]]

Latest revision as of 13:22, 23 January 2019

Publications in the MiPMap
Astin R, Bentham R, Djafarzadeh S, Horscroft JA, Kuc RE, Leung PS, Skipworth JR, Vicencio JM, Davenport AP, Murray AJ, Takala J, Jakob SM, Montgomery H, Szabadkai G (2013) No evidence for a local renin-angiotensin system in liver mitochondria. Sci Rep 3:2467.

Β» PMID:23959064 Open Access

Astin R, Bentham R, Djafarzadeh S, Horscroft JA, Kuc RE, Leung PS, Skipworth JR, Vicencio JM, Davenport AP, Murray AJ, Takala J, Jakob SM, Montgomery H, Szabadkai G (2013) Sci Rep

Abstract: The circulating, endocrine renin-angiotensin system (RAS) is important to circulatory homeostasis, while ubiquitous tissue and cellular RAS play diverse roles, including metabolic regulation. Indeed, inhibition of RAS is associated with improved cellular oxidative capacity. Recently it has been suggested that an intra-mitochondrial RAS directly impacts on metabolism. Here we sought to rigorously explore this hypothesis. Radiolabelled ligand-binding and unbiased proteomic approaches were applied to purified mitochondrial sub-fractions from rat liver, and the impact of AngII on mitochondrial function assessed. Whilst high-affinity AngII binding sites were found in the mitochondria-associated membrane (MAM) fraction, no RAS components could be detected in purified mitochondria. Moreover, AngII had no effect on the function of isolated mitochondria at physiologically relevant concentrations. We thus found no evidence of endogenous mitochondrial AngII production, and conclude that the effects of AngII on cellular energy metabolism are not mediated through its direct binding to mitochondrial targets.


β€’ O2k-Network Lab: UK Cambridge Murray AJ, CH Bern Djafarzadeh S


Labels: MiParea: Respiration 


Organism: Rat  Tissue;cell: Liver  Preparation: Isolated mitochondria 


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


Correction

An Oroboros Oxygraph-2k, Innsbruck, Austria was used in this publication, whereas the "Graz, Austria" reference usually credits the Anton Paar/Oroboros Oxygraph, the first-generation instrument for high-resolution respirometry, which was replaced by the Oxygraph-2k in 2002.