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Difference between revisions of "Guzun 2011 Biochim Biophys Acta"

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(Created page with "{{Publication |title=Guzun R, Karu-Varikmaa M, Gonzalez-Granillo M, Kuznetsov AV, Michel L, Cottet-Rousselle C, Saaremäe M, Kaambre T, Metsis M, Grimm M, Auffray C, Saks V (2011...")
 
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{{Publication
{{Publication
|title=Guzun R, Karu-Varikmaa M, Gonzalez-Granillo M, Kuznetsov AV, Michel L, Cottet-Rousselle C, Saaremäe M, Kaambre T, Metsis M, Grimm M, Auffray C, Saks V (2011) Mitochondria–cytoskeleton interaction: Distribution of β-tubulins in cardiomyocytes and HL-1 cells. Biochim Biophys Acta 1807: 458-469.  
|title=Guzun R, Karu-Varikmaa M, Gonzalez-Granillo M, Kuznetsov AV, Michel L, Cottet-Rousselle C, Saaremäe M, Kaambre T, Metsis M, Grimm M, Auffray C, Saks V (2011) Mitochondria–cytoskeleton interaction: Distribution of β-tubulins in cardiomyocytes and HL-1 cells. Biochim Biophys Acta 1807: 458-469.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/21296049 PMID: 21296049]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/21296049 PMID: 21296049]
|authors=Guzun R, Karu-Varikmaa M, Gonzalez-Granillo M, Kuznetsov AV, Michel L, Cottet-Rousselle C, Saaremäe M, Kaambre T, Metsis M, Grimm M, Auffray C, Saks V
|authors=Guzun R, Karu-Varikmaa M, Gonzalez-Granillo M, Kuznetsov AV, Michel L, Cottet-Rousselle C, Saaremäe M, Kaambre T, Metsis M, Grimm M, Auffray C, Saks V
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|journal=Biochim Biophys Acta
|journal=Biochim Biophys Acta
|abstract=Mitochondria-cytoskeleton interactions were analyzed in adult rat cardiomyocytes and in cancerous non-beating HL-1 cells of cardiac phenotype. We show that in adult cardiomyocytes βII-tubulin is associated with mitochondrial outer membrane (MOM). βI-tubulin demonstrates diffused intracellular distribution, βIII-tubulin is colocalized with Z-lines and βIV-tubulin forms microtubular network. HL-1 cells are characterized by the absence of βII-tubulin, by the presence of bundles of filamentous βIV-tubulin and diffusely distributed βI- and βIII-tubulins. Mitochondrial isoform of creatine kinase (MtCK), highly expressed in cardiomyocytes, is absent in HL-1 cells. Our results show that high apparent K(m) for exogenous ADP in regulation of respiration and high expression of MtCK both correlate with the expression of βII-tubulin. The absence of βII-tubulin isotype in isolated mitochondria and in HL-1 cells results in increased apparent affinity of oxidative phosphorylation for exogenous ADP. This observation is consistent with the assumption that the binding of βII-tubulin to mitochondria limits ADP/ATP diffusion through voltage-dependent anion channel of MOM and thus shifts energy transfer via the phosphocreatine pathway. On the other hand, absence of both βII-tubulin and MtCK in HL-1 cells can be associated with their more glycolysis-dependent energy metabolism which is typical for cancer cells (Warburg effect).
|abstract=Mitochondria-cytoskeleton interactions were analyzed in adult rat cardiomyocytes and in cancerous non-beating HL-1 cells of cardiac phenotype. We show that in adult cardiomyocytes βII-tubulin is associated with mitochondrial outer membrane (MOM). βI-tubulin demonstrates diffused intracellular distribution, βIII-tubulin is colocalized with Z-lines and βIV-tubulin forms microtubular network. HL-1 cells are characterized by the absence of βII-tubulin, by the presence of bundles of filamentous βIV-tubulin and diffusely distributed βI- and βIII-tubulins. Mitochondrial isoform of creatine kinase (MtCK), highly expressed in cardiomyocytes, is absent in HL-1 cells. Our results show that high apparent K(m) for exogenous ADP in regulation of respiration and high expression of MtCK both correlate with the expression of βII-tubulin. The absence of βII-tubulin isotype in isolated mitochondria and in HL-1 cells results in increased apparent affinity of oxidative phosphorylation for exogenous ADP. This observation is consistent with the assumption that the binding of βII-tubulin to mitochondria limits ADP/ATP diffusion through voltage-dependent anion channel of MOM and thus shifts energy transfer via the phosphocreatine pathway. On the other hand, absence of both βII-tubulin and MtCK in HL-1 cells can be associated with their more glycolysis-dependent energy metabolism which is typical for cancer cells (Warburg effect).
|mipnetlab= EE Tallinn Kaambre T, EE Tallinn Saks VA, FR Grenoble Saks VA, FR Grenoble Schlattner U
|mipnetlab=EE Tallinn Kaambre T, EE Tallinn Saks VA, FR Grenoble Saks VA, FR Grenoble Schlattner U
}}
}}
{{Labeling
{{Labeling
|area=Respiration, mt-Structure;fission;fusion
|organism=Rat
|tissues=Heart
|model cell lines=Other cell lines
|preparations=Isolated Mitochondria
|couplingstates=OXPHOS
|substratestates=CI
|instruments=Oxygraph-2k
|instruments=Oxygraph-2k
|additional=Labels
}}
}}

Revision as of 11:22, 3 February 2014

Publications in the MiPMap
Guzun R, Karu-Varikmaa M, Gonzalez-Granillo M, Kuznetsov AV, Michel L, Cottet-Rousselle C, Saaremäe M, Kaambre T, Metsis M, Grimm M, Auffray C, Saks V (2011) Mitochondria–cytoskeleton interaction: Distribution of β-tubulins in cardiomyocytes and HL-1 cells. Biochim Biophys Acta 1807: 458-469.

» PMID: 21296049

Guzun R, Karu-Varikmaa M, Gonzalez-Granillo M, Kuznetsov AV, Michel L, Cottet-Rousselle C, Saaremäe M, Kaambre T, Metsis M, Grimm M, Auffray C, Saks V (2011) Biochim Biophys Acta

Abstract: Mitochondria-cytoskeleton interactions were analyzed in adult rat cardiomyocytes and in cancerous non-beating HL-1 cells of cardiac phenotype. We show that in adult cardiomyocytes βII-tubulin is associated with mitochondrial outer membrane (MOM). βI-tubulin demonstrates diffused intracellular distribution, βIII-tubulin is colocalized with Z-lines and βIV-tubulin forms microtubular network. HL-1 cells are characterized by the absence of βII-tubulin, by the presence of bundles of filamentous βIV-tubulin and diffusely distributed βI- and βIII-tubulins. Mitochondrial isoform of creatine kinase (MtCK), highly expressed in cardiomyocytes, is absent in HL-1 cells. Our results show that high apparent K(m) for exogenous ADP in regulation of respiration and high expression of MtCK both correlate with the expression of βII-tubulin. The absence of βII-tubulin isotype in isolated mitochondria and in HL-1 cells results in increased apparent affinity of oxidative phosphorylation for exogenous ADP. This observation is consistent with the assumption that the binding of βII-tubulin to mitochondria limits ADP/ATP diffusion through voltage-dependent anion channel of MOM and thus shifts energy transfer via the phosphocreatine pathway. On the other hand, absence of both βII-tubulin and MtCK in HL-1 cells can be associated with their more glycolysis-dependent energy metabolism which is typical for cancer cells (Warburg effect).


O2k-Network Lab: EE Tallinn Kaambre T, EE Tallinn Saks VA, FR Grenoble Saks VA, FR Grenoble Schlattner U


Labels: MiParea: Respiration, mt-Structure;fission;fusion 


Organism: Rat  Tissue;cell: Heart  Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property. 


Coupling state: OXPHOS 

HRR: Oxygraph-2k