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Biochem Biophys Res Commun. 2015 Feb 20;457(4):669-75. doi: 10.1016/j.bbrc.2015.01.046. Epub 2015 Jan 21.

Long-lived species have improved proteostasis compared to phylogenetically-related shorter-lived species.

Author information

1
Linus Pauling Institute, Oregon State University, USA.
2
Department of Chemistry and Biochemistry, University of Michigan-Flint, MI 48502, USA.
3
Department of Physiology, The University of Texas Health Science Center, San Antonio, TX, USA; Barshop Institute for Longevity and Aging Studies, The University of Texas Health Science Center, San Antonio, TX, USA.
4
Department of Physiology, The University of Texas Health Science Center, San Antonio, TX, USA; Barshop Institute for Longevity and Aging Studies, The University of Texas Health Science Center, San Antonio, TX, USA; South Texas Veteran's Health Care System, Audie L Murphy Division, San Antonio, TX 78249, USA.
5
Barshop Institute for Longevity and Aging Studies, The University of Texas Health Science Center, San Antonio, TX, USA; Department of Cell and Structural Biology, The University of Texas Health Science Center, San Antonio, TX, USA.
6
Linus Pauling Institute, Oregon State University, USA; Department of Biochemistry and Biophysics, Corvallis, OR 97331, USA. Electronic address: viviana.perez@oregonstate.edu.

Abstract

Our previous studies have shown that the liver from Naked Mole Rats (NMRs), a long-lived rodent, has increased proteasome activity and lower levels of protein ubiquitination compared to mice. This suggests that protein quality control might play a role in assuring species longevity. To determine whether enhanced proteostasis is a common mechanism in the evolution of other long-lived species, here we evaluated the major players in protein quality control including autophagy, proteasome activity, and heat shock proteins (HSPs), using skin fibroblasts from three phylogenetically-distinct pairs of short- and long-lived mammals: rodents, marsupials, and bats. Our results indicate that in all cases, macroautophagy was significantly enhanced in the longer-lived species, both at basal level and after induction by serum starvation. Similarly, basal levels of most HSPs were elevated in all the longer-lived species. Proteasome activity was found to be increased in the long-lived rodent and marsupial but not in bats. These observations suggest that long-lived species may have superior mechanisms to ensure protein quality, and support the idea that protein homeostasis might play an important role in promoting longevity.

KEYWORDS:

Autophagy; Heat shock response; Long-lived species; Proteasome; Protein homeostasis

PMID:
25615820
DOI:
10.1016/j.bbrc.2015.01.046
[Indexed for MEDLINE]

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