Guillet 2010 neurogenetics: Difference between revisions

Latest revision as of 12:38, 16 February 2018

Guillet V, Gueguen N, Verny C, Ferre M, Homedan C, Loiseau D, Procaccio V, Amati-Bonneau P, Bonneau D, Reynier P, Chevrollier A (2010) Adenine nucleotide translocase is involved in a mitochondrial coupling defect in MFN2-related Charcot-Marie-Tooth type 2A disease. Neurogenetics 11:127-33.

» PMID: 19618221

Guillet V, Gueguen N, Verny C, Ferre M, Homedan C, Loiseau D, Procaccio V, Amati-Bonneau P, Bonneau D, Reynier P, Chevrollier A (2010) Neurogenetics

Abstract: Charcot–Marie–Tooth type 2A disease (CMT2A), a dominantly inherited peripheral neuropathy, is caused by mutations in MFN2, a mitochondrial fusion protein. Having previously demonstrated a mitochondrial coupling defect in CMT2A patients’ fibroblasts, we here investigate mitochondrial oxygen consumption and the expression of adenine nucleotide translocase (ANT) and uncoupling proteins from eight other patients with the disease. The mitochondrial uncoupling was associated with a higher respiratory rate, essentially involving complex II proteins. Furthermore, a twofold increase in the expression of ANT led to the reduced efficiency of oxidative phosphorylation in CMT2A cells, suggesting that MFN2 plays a role in controlling ATP/ADP exchanges. • Keywords: Charcot–Marie–Tooth-CMT2A, MFN2, Mitochondria, Adenine nucleotide translocase

• O2k-Network Lab: FR Angers Gueguen N

Labels: MiParea: Respiration, nDNA;cell genetics Pathology: Other

Organism: Human Tissue;cell: Fibroblast Preparation: Enzyme Enzyme: Adenine nucleotide translocase, Complex II;succinate dehydrogenase Regulation: Coupling efficiency;uncoupling Coupling state: OXPHOS

HRR: Oxygraph-2k

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 {{Publication
-|title=Guillet V, Gueguen N, Verny C, Ferre M, Homedan C, Loiseau D, Procaccio V, Amati-Bonneau P, Bonneau D, Reynier P, Chevrollier A (2009) Adenine nucleotide translocase is involved in a mitochondrial coupling defect in MFN2-related Charcot-Marie-Tooth type 2A disease. Neurogenetics 11: 127-133.
+|title=Guillet V, Gueguen N, Verny C, Ferre M, Homedan C, Loiseau D, Procaccio V, Amati-Bonneau P, Bonneau D, Reynier P, Chevrollier A (2010) Adenine nucleotide translocase is involved in a mitochondrial coupling defect in ''MFN2''-related Charcot-Marie-Tooth type 2A disease. Neurogenetics 11:127-33.
+|info=[http://www.ncbi.nlm.nih.gov/pubmed/19618221 PMID: 19618221]
 |authors=Guillet V, Gueguen N, Verny C, Ferre M, Homedan C, Loiseau D, Procaccio V, Amati-Bonneau P, Bonneau D, Reynier P, Chevrollier A
-|year=2009
+|year=2010
 |journal=Neurogenetics
-|abstract='''Charcot–Marie–Tooth type 2A disease''' (CMT2A), a dominantly inherited peripheral neuropathy, is caused by mutations in ''MFN2'', a mitochondrial fusion protein. Having previously demonstrated a mitochondrial coupling defect in CMT2A patients’ fibroblasts, we here investigate mitochondrial oxygen consumption and the expression of adenine nucleotide translocase (ANT) and uncoupling proteins from eight other patients with the disease. The mitochondrial uncoupling was associated with a higher respiratory rate, essentially involving complex II proteins. Furthermore, a twofold increase in the expression of ANT led to the reduced efficiency of oxidative phosphorylation in CMT2A cells, suggesting that ''MFN2'' plays a role in controlling ATP/ADP exchanges.
+|abstract=Charcot–Marie–Tooth type 2A disease (CMT2A), a dominantly inherited peripheral neuropathy, is caused by mutations in ''MFN2'', a mitochondrial fusion protein. Having previously demonstrated a mitochondrial coupling defect in CMT2A patients’ fibroblasts, we here investigate mitochondrial oxygen consumption and the expression of adenine nucleotide translocase (ANT) and uncoupling proteins from eight other patients with the disease. The mitochondrial uncoupling was associated with a higher respiratory rate, essentially involving complex II proteins. Furthermore, a twofold increase in the expression of ANT led to the reduced efficiency of oxidative phosphorylation in CMT2A cells, suggesting that ''MFN2'' plays a role in controlling ATP/ADP exchanges.
 |keywords=Charcot–Marie–Tooth-CMT2A, MFN2, Mitochondria, Adenine nucleotide translocase
-|info=[http://www.ncbi.nlm.nih.gov/pubmed/19618221 PMID: 19618221]
+|mipnetlab=FR Angers Gueguen N
+|discipline=Biomedicine
 }}
 {{Labeling
-|discipline=Biomedicine
+|area=Respiration, nDNA;cell genetics
-|injuries=Genetic Defect; Knockdown; Overexpression
+|diseases=Other
 |organism=Human
 |tissues=Fibroblast
 |preparations=Enzyme
-|enzymes=Complex II; Succinate Dehydrogenase, Adenine Nucleotide Translocase
+|enzymes=Adenine nucleotide translocase, Complex II;succinate dehydrogenase
-|kinetics=ADP; Pi, Oxygen
+|topics=Coupling efficiency;uncoupling
-|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential
+|couplingstates=OXPHOS
 |instruments=Oxygraph-2k
+|discipline=Biomedicine
 }}