Research Paper Volume 11, Issue 6 pp 1664—1685
A comparison of the mitochondrial proteome and lipidome in the mouse and long-lived Pipistrelle bats
- 1 School of Veterinary Medicine and Science, University of Nottingham, Sutton Bonington, LE12 5RD, UK
- 2 School of Biosciences, University of Nottingham, Sutton Bonington, LE12 5RD, UK
- 3 Centre for Analytical Bioscience, School of Pharmacy University of Nottingham, NG7 2RD, UK
- 4 West Yorkshire Bat Hospital, Otley, West Yorkshire, LS21 1AJ, UK
- 5 MRC-ARUK Centre for Musculoskeletal Ageing Research, UK
received: November 14, 2018 ; accepted: March 6, 2019 ; published: March 19, 2019 ;https://doi.org/10.18632/aging.101861
How to Cite
Copyright: Pollard et al. This is an open‐access article distributed under the terms of the Creative Commons Attribution License (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
It is accepted that smaller mammals with higher metabolic rates have shorter lifespans. The very few species that do not follow these rules can give insights into interesting differences. The recorded maximum lifespans of bats are exceptional - over 40 years, compared with the laboratory mouse of 4 years. We investigated the differences in the biochemical composition of mitochondria between bat and mouse species. We used proteomics and ultra-high-performance liquid chromatography coupled with high resolution mass spectrometry lipidomics, to interrogate mitochondrial fractions prepared from Mus musculus and Pipistrellus pipistrellus brain and skeletal muscle. Fatty acid binding protein 3 was found at different levels in mouse and bat muscle mitochondria and its orthologues were investigated in Caenorhabditis elegans knock-downs for LBP 4, 5 and 6. In the bat, high levels of free fatty acids and N-acylethanolamine lipid species together with a significantly greater abundance of fatty acid binding protein 3 in muscle (1.8-fold, p=0.037) were found. Manipulation of fatty acid binding protein orthologues in C. elegans suggest these proteins and their role in lipid regulation are important for mitochondrial function.