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Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice.

Publication ,  Journal Article
Grange, RW; Meeson, A; Chin, E; Lau, KS; Stull, JT; Shelton, JM; Williams, RS; Garry, DJ
Published in: Am J Physiol Cell Physiol
November 2001

Myoglobin is a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers and facilitates oxygen delivery during periods of high metabolic demand. Myoglobin content in skeletal muscle increases in response to hypoxic conditions. However, we previously reported that myoglobin-null mice are viable and fertile. In the present study, we define important functional, cellular, and molecular compensatory adaptations in the absence of myoglobin. Mice without myoglobin manifest adaptations in skeletal muscle that include a fiber type transition (type I to type II in the soleus muscle), increased expression of the hypoxia-inducible transcription factors hypoxia-inducible factor (HIF)-1alpha and HIF-2 (endothelial PAS domain protein), stress proteins such as heat shock protein 27, and the angiogenic growth factor vascular endothelial growth factor (soleus muscle), as well as increased nitric oxide metabolism (extensor digitorum longus). The resulting changes in angiogenesis, nitric oxide metabolism, and vasomotor regulation are likely to account for preserved exercise capacity of animals lacking myoglobin. These results demonstrate that mammalian organisms are capable of a broad spectrum of adaptive responses that can compensate for a potentially serious defect in cellular oxygen transport.

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Published In

Am J Physiol Cell Physiol

DOI

ISSN

0363-6143

Publication Date

November 2001

Volume

281

Issue

5

Start / End Page

C1487 / C1494

Location

United States

Related Subject Headings

  • Reverse Transcriptase Polymerase Chain Reaction
  • Regional Blood Flow
  • Physiology
  • Myoglobin
  • Mutation
  • Muscle, Skeletal
  • Muscle Fibers, Skeletal
  • Muscle Contraction
  • Mice, Knockout
  • Mice
 

Citation

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Grange, R. W., Meeson, A., Chin, E., Lau, K. S., Stull, J. T., Shelton, J. M., … Garry, D. J. (2001). Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice. Am J Physiol Cell Physiol, 281(5), C1487–C1494. https://doi.org/10.1152/ajpcell.2001.281.5.C1487
Grange, R. W., A. Meeson, E. Chin, K. S. Lau, J. T. Stull, J. M. Shelton, R. S. Williams, and D. J. Garry. “Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice.Am J Physiol Cell Physiol 281, no. 5 (November 2001): C1487–94. https://doi.org/10.1152/ajpcell.2001.281.5.C1487.
Grange RW, Meeson A, Chin E, Lau KS, Stull JT, Shelton JM, et al. Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice. Am J Physiol Cell Physiol. 2001 Nov;281(5):C1487–94.
Grange, R. W., et al. “Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice.Am J Physiol Cell Physiol, vol. 281, no. 5, Nov. 2001, pp. C1487–94. Pubmed, doi:10.1152/ajpcell.2001.281.5.C1487.
Grange RW, Meeson A, Chin E, Lau KS, Stull JT, Shelton JM, Williams RS, Garry DJ. Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice. Am J Physiol Cell Physiol. 2001 Nov;281(5):C1487–C1494.

Published In

Am J Physiol Cell Physiol

DOI

ISSN

0363-6143

Publication Date

November 2001

Volume

281

Issue

5

Start / End Page

C1487 / C1494

Location

United States

Related Subject Headings

  • Reverse Transcriptase Polymerase Chain Reaction
  • Regional Blood Flow
  • Physiology
  • Myoglobin
  • Mutation
  • Muscle, Skeletal
  • Muscle Fibers, Skeletal
  • Muscle Contraction
  • Mice, Knockout
  • Mice