First Author | Guzun R | Year | 2011 |
Journal | Biochim Biophys Acta | Volume | 1807 |
Issue | 4 | Pages | 458-69 |
PubMed ID | 21296049 | Mgi Jnum | J:175014 |
Mgi Id | MGI:5142169 | Doi | 10.1016/j.bbabio.2011.01.010 |
Citation | Guzun R, et al. (2011) Mitochondria-cytoskeleton interaction: Distribution of beta-tubulins in cardiomyocytes and HL-1 cells. Biochim Biophys Acta 1807(4):458-69 |
abstractText | 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 betaII-tubulin is associated with mitochondrial outer membrane (MOM). betaI-tubulin demonstrates diffused intracellular distribution, betaIII-tubulin is colocalized with Z-lines and betaIV-tubulin forms microtubular network. HL-1 cells are characterized by the absence of betaII-tubulin, by the presence of bundles of filamentous betaIV-tubulin and diffusely distributed betaI- and betaIII-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 betaII-tubulin. The absence of betaII-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 betaII-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 betaII-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). |