Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice
Myoglobin is a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative
skeletal myofibers and facilitates oxygen delivery during periods of high metabolic demand …
skeletal myofibers and facilitates oxygen delivery during periods of high metabolic demand …
Molecular insights into the functional role of myoglobin
DJ Garry, PPA Mammen - Hypoxia and tHe circulation, 2007 - Springer
Myoglobin is a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative
skeletal muscle fibers. Myoglobin is a well-characterized protein and numerous studies have …
skeletal muscle fibers. Myoglobin is a well-characterized protein and numerous studies have …
Gene deletional strategies reveal novel physiological roles for myoglobin in striated muscle
SB Kanatous, DJ Garry - Respiratory physiology & neurobiology, 2006 - Elsevier
Myoglobin is an abundant hemoprotein that is expressed in cardiomyocytes and oxidative
skeletal myofibers of vertebrates. Elegant studies using physiological, biochemical and …
skeletal myofibers of vertebrates. Elegant studies using physiological, biochemical and …
Disruption of myoglobin in mice induces multiple compensatory mechanisms
A Gödecke, U Flögel, K Zanger… - Proceedings of the …, 1999 - National Acad Sciences
Myoglobin may serve a variety of functions in muscular oxygen supply, such as O2 storage,
facilitated O2 diffusion, and myoglobin-mediated oxidative phosphorylation. We studied the …
facilitated O2 diffusion, and myoglobin-mediated oxidative phosphorylation. We studied the …
Hypoxia-induced left ventricular dysfunction in myoglobin-deficient mice
PPA Mammen, SB Kanatous… - American Journal …, 2003 - journals.physiology.org
Myoglobin-deficient mice are viable and have preserved cardiac function due to their ability
to mount a complex compensatory response involving increased vascularization and the …
to mount a complex compensatory response involving increased vascularization and the …
Adaptation of the myoglobin knockout mouse to hypoxic stress
G Schlieper, JH Kim, A Molojavyi… - American Journal …, 2004 - journals.physiology.org
Myoglobin knockout (myo-/-) mice were previously reported to show no obvious phenotype
but revealed several compensatory mechanisms that include increases in cardiac capillary …
but revealed several compensatory mechanisms that include increases in cardiac capillary …
Both hypoxia and work are required to enhance expression of myoglobin in skeletal muscle. Focus on “Hypoxia reprograms calcium signaling and regulates …
BA Wittenberg - American Journal of Physiology-Cell …, 2009 - journals.physiology.org
THE EFFECTS OF HYPOXIA on mammalian heart and muscle have fascinated physiologists
for many a day. Myoglobin is expressed adaptively in muscle. In very young animals, and in …
for many a day. Myoglobin is expressed adaptively in muscle. In very young animals, and in …
Hypoxia reprograms calcium signaling and regulates myoglobin expression
SB Kanatous, PPA Mammen… - … of Physiology-Cell …, 2009 - journals.physiology.org
Myoglobin is an oxygen storage molecule that is selectively expressed in cardiac and slow-
twitch skeletal muscles that have a high oxygen demand. Numerous studies have implicated …
twitch skeletal muscles that have a high oxygen demand. Numerous studies have implicated …
Life without myoglobin
Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and
animals. Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and …
animals. Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and …
Aerobic performance and the function of myoglobin in human skeletal muscle
RA Meyer - American Journal of Physiology-Regulatory …, 2004 - journals.physiology.org
THE ROLE OF MYOGLOBIN as an oxygen storage protein in the muscles of diving birds and
mammals is well-established (8). In contrast, the function of the lower myoglobin content in …
mammals is well-established (8). In contrast, the function of the lower myoglobin content in …