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A comparison of the mitochondrial proteome and lipidome in the mouse and long-lived Pipistrelle bats
Author(s) -
Amelia K. Pollard,
Thomas L. Ingram,
Catharine A. Ortori,
Freya Shephard,
Margaret Brown,
Susan Liddell,
David A. Barrett,
Lisa Chakrabarti
Publication year - 2019
Publication title -
aging
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.473
H-Index - 90
ISSN - 1945-4589
DOI - 10.18632/aging.101861
Subject(s) - lipidome , caenorhabditis elegans , biology , proteome , lipidomics , mitochondrion , proteomics , fatty acid binding protein , biochemistry , fatty acid , skeletal muscle , microbiology and biotechnology , gene , anatomy
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.

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