The long lifespan of two bat species is correlated with resistance to protein oxidation and enhanced protein homeostasis.
Altered structure, and hence function, of cellular macromolecules caused by oxidation can contribute to loss of physiological function with age. Here, we tested whether the lifespan of bats, which generally live far longer than predicted by their size, could be explained by reduced protein damage relative to short-lived mice. We show significantly lower protein oxidation (carbonylation) in Mexican free-tailed bats (Tadarida brasiliensis) relative to mice, and a trend for lower oxidation in samples from cave myotis bats (Myotis velifer) relative to mice. Both species of bat show in vivo and in vitro resistance to protein oxidation under conditions of acute oxidative stress. These bat species also show low levels of protein ubiquitination in total protein lysates along with reduced proteasome activity, suggesting diminished protein damage and removal in bats. Lastly, we show that bat-derived protein fractions are resistant to urea-induced protein unfolding relative to the level of unfolding detected in fractions from mice. Together, these data suggest that long lifespan in some bat species might be regulated by very efficient maintenance of protein homeostasis.
Salmon
Adam B
AB
Sam and Ann Barshop Institute for Longevity and Aging Studies, University of Texas Health Science Center at San Antonio, 15355 Lambda Dr., San Antonio, TX 78245-3207, USA.
Leonard
Shanique
S
Masamsetti
Venkata
V
Pierce
Anson
A
Podlutsky
Andrej J
AJ
Podlutskaya
Natalia
N
Richardson
Arlan
A
Austad
Steven N
SN
Chaudhuri
Asish R
AR
D000818:Animals; D002685:Chiroptera; D006706:Homeostasis; D008136:Longevity; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011489:Protein Denaturation; D011506:Proteins / Q000378:metabolism*; D013045:Species Specificity; D054875:Ubiquitination
D011506:Proteins; D046988:Proteasome Endopeptidase Complex