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The association of mitochondrial morphology and supercomplex redistribution with skeletal muscle oxidative capacity in older adults

  • University of Lausanne
Research Output: Contribution to journal Article Peer-review

Open access

Publication Information

Output type

Research Output: Contribution to journal Article Peer-review

Original language

English

Article number

e70359

Journal (Volume, Issue Number)

Physiological Reports (Volume 13, Issue 9)

Publication milestones

  • Published - 01/05/2025

Publication status

Published - 01/05/2025

Publication IDs

  • Scopus: 105004704000

Abstract

Skeletal muscle maximal oxidative capacity (ATPmax) is a key component of age-related sarcopenia and muscle health. The contribution of mitochondrial morphology and electron transport chain supercomplex (SC) assemblies to ATPmax has yet to be determined in human muscle. ATPmax measured in vivo by 31phosphorus magnetic resonance spectroscopy in the quadriceps femoris of nine volunteers (65.5 ± 3.3 years old) was correlated with muscle biopsy outcomes before and after 4 months of supervised exercise. Mitochondrial morphology was assessed in electron micrographs, and SCs were measured by blue native gel electrophoresis. In the sedentary conditions, ATPmax was positively associated with complex (C) I and CIII in SC I+III2+IVn and negatively associated with CI and CIII in SC I+III2. Regarding mitochondrial morphology, ATPmax was positively associated with markers of mitochondrial elongation. Exercise training-induced increases in ATPmax were accompanied by mitochondrial elongation and by the redistribution of free complex III. Indicators of mitochondrial elongation were associated with the redistribution of specific complexes to SC I+III2+IVn. Higher skeletal muscle oxidative capacity in older adults is associated with mitochondrial elongation and the redistribution of electron transport chain complexes into higher rank SCs in the same muscle. Further, we provide evidence that mitochondrial elongation favors mitochondrial SC assembly.