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  • Lewis, Christopher T. A.Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark (author)

Remodelling of skeletal muscle myosin metabolic states in hibernating mammals

  • BookEnglish2023

Publisher, publication year, extent ...

  • 2023
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:oru-110365
  • https://urn.kb.se/resolve?urn=urn:nbn:se:oru:diva-110365URI
  • https://doi.org/10.1101/2023.11.14.566992DOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:vet swepub-contenttype
  • Subject category:ovr swepub-publicationtype

Notes

  • bioRxiv
  • Hibernation is a period of metabolic suppression utilized by many small and large mammal species to survive during winter periods. As the underlying cellular and molecular mechanisms remain incompletely understood, our study aimed to determine whether skeletal muscle myosin and its metabolic efficiency undergo alterations during hibernation to optimize energy utilization. We isolated muscle fibers from small hibernators, Ictidomys tridecemlineatus and Eliomys quercinus and larger hibernators, Ursus arctos and Ursus americanus. We then conducted loaded Mant-ATP chase experiments alongside X-ray diffraction to measure resting myosin dynamics and its ATP demand. In parallel, we performed multiple proteomics analyses. Our results showed a preservation of myosin structure in U. arctos and U. americanus during hibernation, whilst in I. tridecemlineatus and E. quercinus, changes in myosin metabolic states during torpor unexpectedly led to higher levels in energy expenditure of type II, fast-twitch muscle fibers at ambient lab temperatures (20°C). Upon repeating loaded Mant-ATP chase experiments at 8°C (near the body temperature of torpid animals), we found that myosin ATP consumption in type II muscle fibers was reduced by 77-107% during torpor compared to active periods. Additionally, we observed Myh2 hyper-phosphorylation during torpor in I. tridecemilineatus, which was predicted to stabilize the myosin molecule. This may act as a potential molecular mechanism mitigating myosin-associated increases in skeletal muscle energy expenditure during periods of torpor in response to cold exposure. Altogether, we demonstrate that resting myosin is altered in hibernating mammals, contributing to significant changes to the ATP consumption of skeletal muscle. Additionally, we observe that it is further altered in response to cold exposure and highlight myosin as a potentially contributor to skeletal muscle non-shivering thermogenesis.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Melhedegaard, Elise G.Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark (author)
  • Ognjanovic, Marija M.Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark (author)
  • Olsen, Mathilde S.Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark (author)
  • Laitila, JenniDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark (author)
  • Seaborne, Robert A. E.Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark; Centre for Human and Applied Physiological Sciences, Faculty of Life Sciences & Medicine, King's College London, London, UK (author)
  • Grønset, Magnus NørregaardDepartment of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen, Denmark (author)
  • Zhang, ChengxinDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI, USA (author)
  • Iwamoto, HiroyukiSpring-8, Japan Synchrotron Radiation Research Institute, Hyogo, Japan (author)
  • Hessel, Anthony L.Institute of Physiology II, University of Muenster, Muenster, Germany; Accelerated Muscle Biotechnologies Consultants, Boston, Massachusetts, USA (author)
  • Kuehn, Michel N.Institute of Physiology II, University of Muenster, Muenster, Germany; Accelerated Muscle Biotechnologies Consultants, Boston, Massachusetts, USA (author)
  • Merino, CarlaBiosfer Teslab, Reus, Spain (author)
  • Amigó, NuriaBiosfer Teslab, Reus, Spain (author)
  • Fröbert, Ole,1964-Örebro universitet,Institutionen för medicinska vetenskaper,Department of Clinical Medicine, Faculty of Health, Aarhus University, Aarhus, Denmark; Faculty of Health, Department of Cardiology, Örebro University, Örebro, Sweden(Swepub:oru)oft (author)
  • Giroud, SylvainEnergetics Lab, Department of Biology, Northern Michigan University, Marquette, MI, USA; Research Institute of Wildlife Ecology, Department of Interdisciplinary Life Sciences, University of Veterinary Medicine Vienna, Vienna, Austria (author)
  • Staples, James F.Department of Biology, University of Western Ontario, London, Ontario, Canada (author)
  • Goropashnaya, Anna V.Center for Transformative Research in Metabolism, Institute of Arctic Biology, University of Alaska Fairbanks, Fairbanks, AK, USA (author)
  • Fedorov, Vadim B.Center for Transformative Research in Metabolism, Institute of Arctic Biology, University of Alaska Fairbanks, Fairbanks, AK, USA (author)
  • Barnes, Brian M.Center for Transformative Research in Metabolism, Institute of Arctic Biology, University of Alaska Fairbanks, Fairbanks, AK, USA (author)
  • Tøien, ØivindCenter for Transformative Research in Metabolism, Institute of Arctic Biology, University of Alaska Fairbanks, Fairbanks, AK, USA (author)
  • Drew, Kelly L.Center for Transformative Research in Metabolism, Institute of Arctic Biology, University of Alaska Fairbanks, Fairbanks, AK, USA (author)
  • Sprenger, Ryan J.Department of Zoology, University of British Columbia, Vancouver, BC, Canada (author)
  • Ochala, JulienDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark (author)
  • Department of Biomedical Sciences, University of Copenhagen, Copenhagen, DenmarkDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark; Centre for Human and Applied Physiological Sciences, Faculty of Life Sciences & Medicine, King's College London, London, UK (creator_code:org_t)

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