Attenuation of Ca2+-activated ATPase and shortening velocity in hypertrophied fast twitch skeletal muscle from aged Japanese quail

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Abstract

The effect of aging on the in vitro contractile properties of the patagialis (PAT) muscle of 35 young adult (YA; 8 weeks of age) and 35 aged adult (AA, 110 weeks of age) Coturnix quails was examined after 0-30 days of stretch-overload. Overload was achieved by placing a weight equivalent to 12% of the birds' body weight on one wing. The contralateral wing served as the intra-animal control. Overload increased the weight of the PAT by 45.1±2.1% in YA, and 24.1±2.6% in AA. Twitch contraction time increased with loading from 43.2±1.2 to 67.3±2.2ms in YA birds and 57.2±1.7 to 77.4±1.9ms in AA birds. Unloaded shortening velocity (Vo) decreased by 40.1±2.2 and 38.8±3.2% in YA and aged birds, respectively. The decrease in fast myosin expression was greater in overloaded muscles of YA (20%) as compared to AA birds (12%). However, this was accompanied by a greater decrease in total muscle ATPase activity in aged birds (61%) compared to YA birds (40%). Myosin isozyme Ca2+-ATPase activity was 26% lower in FM1 but not other fast myosins in YA birds, but it was ∼30% lower in all fast myosins in PAT muscles of aged birds. These data show that the reduction of Vo and the increase in twitch duration with aging may be due in part to reductions in ATPase activity in all myosin isoforms, as compared to myosin isoforms isolated from YA birds.

Original languageEnglish (US)
Pages (from-to)665-678
Number of pages14
JournalExperimental Gerontology
Volume37
Issue number5
DOIs
StatePublished - Mar 25 2002
Externally publishedYes

Fingerprint

Coturnix
Calcium-Transporting ATPases
Birds
Adenosine Triphosphatases
Muscle
Skeletal Muscle
Myosins
Muscles
Protein Isoforms
Aging of materials
Weights and Measures
Quail
Isoenzymes
Young Adult
Animals
Body Weight

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Aging
  • Molecular Biology
  • Genetics
  • Endocrinology
  • Cell Biology

Cite this

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title = "Attenuation of Ca2+-activated ATPase and shortening velocity in hypertrophied fast twitch skeletal muscle from aged Japanese quail",
abstract = "The effect of aging on the in vitro contractile properties of the patagialis (PAT) muscle of 35 young adult (YA; 8 weeks of age) and 35 aged adult (AA, 110 weeks of age) Coturnix quails was examined after 0-30 days of stretch-overload. Overload was achieved by placing a weight equivalent to 12{\%} of the birds' body weight on one wing. The contralateral wing served as the intra-animal control. Overload increased the weight of the PAT by 45.1±2.1{\%} in YA, and 24.1±2.6{\%} in AA. Twitch contraction time increased with loading from 43.2±1.2 to 67.3±2.2ms in YA birds and 57.2±1.7 to 77.4±1.9ms in AA birds. Unloaded shortening velocity (Vo) decreased by 40.1±2.2 and 38.8±3.2{\%} in YA and aged birds, respectively. The decrease in fast myosin expression was greater in overloaded muscles of YA (20{\%}) as compared to AA birds (12{\%}). However, this was accompanied by a greater decrease in total muscle ATPase activity in aged birds (61{\%}) compared to YA birds (40{\%}). Myosin isozyme Ca2+-ATPase activity was 26{\%} lower in FM1 but not other fast myosins in YA birds, but it was ∼30{\%} lower in all fast myosins in PAT muscles of aged birds. These data show that the reduction of Vo and the increase in twitch duration with aging may be due in part to reductions in ATPase activity in all myosin isoforms, as compared to myosin isoforms isolated from YA birds.",
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N2 - The effect of aging on the in vitro contractile properties of the patagialis (PAT) muscle of 35 young adult (YA; 8 weeks of age) and 35 aged adult (AA, 110 weeks of age) Coturnix quails was examined after 0-30 days of stretch-overload. Overload was achieved by placing a weight equivalent to 12% of the birds' body weight on one wing. The contralateral wing served as the intra-animal control. Overload increased the weight of the PAT by 45.1±2.1% in YA, and 24.1±2.6% in AA. Twitch contraction time increased with loading from 43.2±1.2 to 67.3±2.2ms in YA birds and 57.2±1.7 to 77.4±1.9ms in AA birds. Unloaded shortening velocity (Vo) decreased by 40.1±2.2 and 38.8±3.2% in YA and aged birds, respectively. The decrease in fast myosin expression was greater in overloaded muscles of YA (20%) as compared to AA birds (12%). However, this was accompanied by a greater decrease in total muscle ATPase activity in aged birds (61%) compared to YA birds (40%). Myosin isozyme Ca2+-ATPase activity was 26% lower in FM1 but not other fast myosins in YA birds, but it was ∼30% lower in all fast myosins in PAT muscles of aged birds. These data show that the reduction of Vo and the increase in twitch duration with aging may be due in part to reductions in ATPase activity in all myosin isoforms, as compared to myosin isoforms isolated from YA birds.

AB - The effect of aging on the in vitro contractile properties of the patagialis (PAT) muscle of 35 young adult (YA; 8 weeks of age) and 35 aged adult (AA, 110 weeks of age) Coturnix quails was examined after 0-30 days of stretch-overload. Overload was achieved by placing a weight equivalent to 12% of the birds' body weight on one wing. The contralateral wing served as the intra-animal control. Overload increased the weight of the PAT by 45.1±2.1% in YA, and 24.1±2.6% in AA. Twitch contraction time increased with loading from 43.2±1.2 to 67.3±2.2ms in YA birds and 57.2±1.7 to 77.4±1.9ms in AA birds. Unloaded shortening velocity (Vo) decreased by 40.1±2.2 and 38.8±3.2% in YA and aged birds, respectively. The decrease in fast myosin expression was greater in overloaded muscles of YA (20%) as compared to AA birds (12%). However, this was accompanied by a greater decrease in total muscle ATPase activity in aged birds (61%) compared to YA birds (40%). Myosin isozyme Ca2+-ATPase activity was 26% lower in FM1 but not other fast myosins in YA birds, but it was ∼30% lower in all fast myosins in PAT muscles of aged birds. These data show that the reduction of Vo and the increase in twitch duration with aging may be due in part to reductions in ATPase activity in all myosin isoforms, as compared to myosin isoforms isolated from YA birds.

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