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Departments of 1 Physiology, 2 Internal Medicine, and 3 Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390
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)-1
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.
transgenic mice; oxygen metabolism; hypoxia; vascularization
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