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1 Noll Physiological Research Center, Pennsylvania State University, University Park, Pennsylvania 16802-6900; and 2 Department of Clinical Neuroscience, Karolinska Hospital, SE-17176 Stockholm, Sweden
The effects of aging on
the mechanical properties of myosin were measured in 87 fibers from
muscles of humans (n = 40), rats (n = 21), and mice (n = 26) using a single fiber in vitro
motility assay. Irrespective of species, an 18-25% aging-related
slowing in the speed of actin filaments was observed from 62 single
fibers expressing the slow (type I) 
-myosin heavy chain isoform. The mechanisms underlying the aging-related slowing of motility speed remain unknown, but it is suggested that posttranslational
modifications of myosin by oxidative stress, glycation, or nitration
play an important role. The aging-related slowing in the speed of actin filaments propelled by the type I myosin was confirmed in three mammalian species with an ~3,400-fold difference in body size. Motility speed from human myosin was 3-fold slower than from myosin of
the ~3,400-fold smaller mouse and approximately twofold slower when
compared with the ~130-fold smaller rat, irrespective of age. A
strong correlation was observed between the log values of actin sliding
speed and body mass, suggesting that the effects of scaling is, at
least in part, due to altered functional properties of the motor
protein itself.
in vitro motility; myosin heavy chain; scaling; single muscle fiber
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