VDAC3 has differing mitochondrial functions in two types of striated muscles
| Autor: | Nha Lee, William J. Craigen, Dawna L. Armstrong, Keltoum Anflous-Pharayra |
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| Jazyk: | angličtina |
| Předmět: |
ADP
Voltage-dependent anion channel Biophysics Oxidative phosphorylation Mitochondrion Biochemistry Mitochondrial Membrane Transport Proteins Article Electron Transport Complex IV Mitochondrial Proteins Mitochondrial membrane transport protein Mice Oxygen Consumption Animals Voltage-Dependent Anion Channels Inner mitochondrial membrane Mice Knockout biology VDAC3 VDAC Myocardium Cell Biology Respiratory enzyme Muscle Striated Mitochondrial inner membrane Cell biology Mitochondria Adenosine Diphosphate Microscopy Electron Mitochondrial outer membrane biology.protein VDAC1 Bacterial Outer Membrane Proteins |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. (1):150-156 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/j.bbabio.2010.09.007 |
| Popis: | Voltage-dependent anion channel (VDAC) is an abundant mitochondrial outer membrane protein. In mammals, three VDAC isoforms have been characterized. We have previously reported alterations in the function of mitochondria when assessed in situ in different muscle types in VDAC1 deficient mice (Anflous, K., Armstrong, D., Craigen, W.J., 2001, J. Biol. Chem. 276, 1954-1960). In the present report we extend the study to VDAC3 deficient muscles and measure the respiratory enzyme activity in both VDAC1 and VDAC3 deficient muscles. While in the heart the absence of VDAC3 causes a decrease in the apparent affinity of in situ mitochondria for ADP, in the gastrocnemius, a mixed glycolytic/oxidative muscle, the affinity of in situ mitochondria for ADP remains unchanged. The absence of VDAC1 causes multiple defects in respiratory complex activities in both types of muscle. However, in VDAC3 deficient mice the defect is restricted to the heart and only to complex IV. These functional alterations correlate with structural aberrations of mitochondria. These results demonstrate that, unlike VDAC1, there is muscle-type specificity for VDAC3 function and therefore in vivo these two isoforms may fulfill different physiologic functions. |
| Databáze: | OpenAIRE |
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