BMAL1 and CLOCK proteins exhibit differential association with mitochondrial dynamics, protein synthesis pathways and muscle strength in human muscle

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dc.contributor.authorFigueroa-Toledo, A. M.
dc.contributor.authorGutiérrez-Pino, J.
dc.contributor.authorCarriel-Nesvara, A.
dc.contributor.authorMarchese-Bittencourt, M.
dc.contributor.authorZbinden-Foncea, Hermann
dc.contributor.authorCastro-Sepulveda, Mauricio
dc.date.accessioned2024-11-28T18:05:26Z
dc.date.available2024-11-28T18:05:26Z
dc.date.issued2024-06-26
dc.description.abstractMurine models lacking CLOCK/BMAL1 proteins in skeletal muscle (SkM) present muscle deterioration and mitochondria abnormalities. It is unclear whether humans with lower levels of these proteins in the SkM have similar alterations. Here we evaluated the association between BMAL1 and CLOCK protein mass with mitochondrial dynamics parameters and molecular and functional SkM quality markers in males. SkM biopsies were taken from the vastus lateralis of 16 male (non-athletes, non-obese and non-diabetic) subjects (8–9 a.m.). The morphology of mitochondria and their interaction with the sarcoplasmic reticulum (mitochondria-SR) were determined using transmission electron microscopy images. Additionally, protein abundance of the OXPHOS complex, mitochondria fusion/fission regulators, mitophagy and signalling proteins related to muscle protein synthesis were measured. To evaluate the quality of SkM, the cross-sectional area and maximal SkM strength were also measured. The results showed that BMAL1 protein mass was positively associated with mitochondria-SR distance, mitochondria size, mitochondria cristae density and mTOR protein mass. On the other hand, CLOCK protein mass was negatively associated with mitochondria-SR interaction, but positively associated with mitochondria complex III, OPA1 and DRP1 protein mass. Furthermore, CLOCK protein mass was positively associated with the protein synthesis signalling pathway (total mTOR, AKT and P70S6K protein mass) and SkM strength. These findings suggest that the BMAL1 and CLOCK proteins play different roles in regulating mitochondrial dynamics and SkM function in males, and that modulation of these proteins could be a potential therapeutic target for treating muscle diseases.
dc.identifier.citationThe Journal of Physiology, (2024) p. 1-13.
dc.identifier.doihttps://doi.org/10.1113/JP285955#support-information-section
dc.identifier.issn0022-3751
dc.identifier.issne1469-7793
dc.identifier.orcidhttps://orcid.org/0000-0002-9643-1037
dc.identifier.orcidhttp://orcid.org/0000-0002-2270-299X
dc.identifier.urihttp://hdl.handle.net/20.500.12254/3942
dc.language.isoen
dc.publisherThe Physiological Society
dc.rightsAtribución-NoComercial-CompartirIgual 3.0 Chile (CC BY-NC-SA 3.0 CL)
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/cl/
dc.subjectMitophagy
dc.subjectCircadian clock
dc.subjectMitochondria cristae density
dc.subjectMitochondria fusion and fission
dc.subjectMuscle strength
dc.titleBMAL1 and CLOCK proteins exhibit differential association with mitochondrial dynamics, protein synthesis pathways and muscle strength in human muscle
dc.typeArticle
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