期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1807, 期 1, 页码 150-156出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2010.09.007
关键词
Mitochondrial outer membrane; VDAC; ADP; Mitochondrial inner membrane
资金
- Muscular Dystrophy Association [R01 GM55713, R01 NS42319]
- Baylor College of Medicine Child Health Research Center
- Intellectual and Developmental Disabilities Research Center
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM055713] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS042319] Funding Source: NIH RePORTER
Voltage-dependent anion channel (VDAC) is an abundant mitochondrial outer membrane protein. In mammals, three VDAC isoforrns 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 et al., 2001). 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 VDAO 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. (C) 2010 Elsevier B.V. All rights reserved.
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