Recent studies of myoglobin (Mb) knockout (myo−/−) mice have extended our
understanding of Mb's diverse functions and have demonstrated a complex array of …

Myoglobin is a well-characterized, cytoplasmic hemoprotein that is expressed primarily in
cardiomyocytes and oxidative skeletal muscle fibers. However, recent studies also suggest …

Mice lacking myoglobin survive to adulthood and meet the circulatory demands of exercise
and pregnancy without cardiac decompensation. In the present study, we show that many …

Myoglobin knockout mice (myo−/−) adapt to the loss of myoglobin by the activation of a
variety of compensatory mechanisms acting on the structural and functional level. To …

Myoglobin (Myg) is an oxygen-binding hemoprotein that is widely thought to be expressed
exclusively in oxidative skeletal and cardiac myocytes, where it plays a key role in coping …

Myoglobin (Mb) is an oxygen-binding muscular hemeprotein regulated via Ca2+-signaling
pathways involving calcineurin (CN), with Mb increases attributed to hypoxia, exercise, and …

Myoglobin (Mb) is an intensely studied hemoprotein that is restricted mainly to the heart and
oxidative myofibers in skeletal muscle. Previous physiologic and pharmacologic studies …

Myoglobin (Mb) is a large protein that reversibly binds oxygen in the muscle cell and is
thought to be critical for O2 supply to the mitochondria during exercise. The role of Mb in …

Myoglobin (Mb) is an important intracellular oxygen-binding hemoprotein found in the
cytoplasm of skeletal and cardiac muscle tissue playing a well-known role in O2 storage and …

SUMMARY A key cellular adaptation to diving in Weddell seals is enhanced myoglobin
concentrations in their skeletal muscles, which serve to store oxygen to sustain a lipid-based …