BIOMAT Database Logo BIOMAT Database Logo

Metabolic and morphologic properties of single muscle fibers in the rat after spaceflight, Cosmos 1887. 1990

B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Department of Kinesiology, University of California, Los Angeles 90024.

The adaptation of a slow (soleus, Sol) and a fast (medial gastrocnemius, MG) skeletal muscle to spaceflight was studied in five young male rats. The flight period was 12.5 days and the rats were killed approximately 48 h after returning to 1 g. Five other rats that were housed in cages similar to those used by the flight rats were maintained at 1 g for the same period of time to serve as ground-based controls. Fibers were classified as dark or light staining for myosin adenosine triphosphatase (ATPase). On the average, the fibers in the Sol of the flight rats atrophied twice as much as those in the MG. Further, the fibers located in the deep (close to the bone and having the highest percentage of light ATPase and high oxidative fibers in the muscle cross section) region of the MG atrophied more than the fibers located in the superficial (away from the bone and having the lowest percentage of light ATPase and high oxidative fibers in the muscle cross-section) region of the muscle. Based on quantitative histochemical assays of single muscle fibers, succinate dehydrogenase (SDH) activity per unit volume was unchanged in fibers of the Sol and MG. However, in the Sol, but not the MG, the total amount of SDH activity in a 10-microns-thick section of a fiber decreased significantly in response to spaceflight. Based on population distributions, it appears that the alpha-glycerophosphate dehydrogenase (GPD) activities were elevated in the dark ATPase fibers in the Sol, whereas the light fibers in the Sol and both fiber types in the MG did not appear to change. The ratio of GPD to SDH activities increased in the dark (but not light) fibers of the Sol and was unaffected in the MG. Immunohistochemical analyses indicate that approximately 40% of the fibers in the Sol of flight rats expressed a fast myosin heavy chain compared with 22% in control rats. Further, 31% of the fibers in the Sol of flight rats expressed both fast and slow myosin heavy chains compared with 8% in control rats. Immunohistochemical changes in the MG were minimal. These data suggest that the magnitude and direction of enzymatic activity and cell volume changes are dependent on the muscle, the region of the muscle, and the type of myosin expressed in the fibers. Further, the ability of fibers to maintain normal or even elevated activities per unit volume of some metabolic enzymes is remarkable considering the marked and rapid decrease in fiber volume.

UI MeSH Term Description Entries
D007150 Immunohistochemistry Histochemical localization of immunoreactive substances using labeled antibodies as reagents. Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D008297 Male Males
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009218 Myosins A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D011919 Rats, Inbred Strains Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding. August Rats,Inbred Rat Strains,Inbred Strain of Rat,Inbred Strain of Rats,Inbred Strains of Rats,Rat, Inbred Strain,August Rat,Inbred Rat Strain,Inbred Strain Rat,Inbred Strain Rats,Inbred Strains Rat,Inbred Strains Rats,Rat Inbred Strain,Rat Inbred Strains,Rat Strain, Inbred,Rat Strains, Inbred,Rat, August,Rat, Inbred Strains,Rats Inbred Strain,Rats Inbred Strains,Rats, August,Rats, Inbred Strain,Strain Rat, Inbred,Strain Rats, Inbred,Strain, Inbred Rat,Strains, Inbred Rat
D005993 Glycerolphosphate Dehydrogenase Alpha-Glycerophosphate Dehydrogenase,Glycerol-3-Phosphate Dehydrogenase,Glycerophosphate Dehydrogenase,Glycerophosphate Oxidase,Alpha Glycerophosphate Dehydrogenase,Dehydrogenase, Alpha-Glycerophosphate,Dehydrogenase, Glycerol-3-Phosphate,Dehydrogenase, Glycerolphosphate,Dehydrogenase, Glycerophosphate,Glycerol 3 Phosphate Dehydrogenase,Oxidase, Glycerophosphate
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013026 Space Flight Travel beyond the earth's atmosphere. Space Exploration,Space Travel,Spaceflight,Exploration, Space,Explorations, Space,Flight, Space,Flights, Space,Space Explorations,Space Flights,Space Travels,Spaceflights,Travel, Space,Travels, Space
D013385 Succinate Dehydrogenase A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II. Succinic Oxidase,Fumarate Reductase,Succinic Dehydrogenase,Dehydrogenase, Succinate,Dehydrogenase, Succinic,Oxidase, Succinic,Reductase, Fumarate

Related Publications

B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Structural and metabolic properties of rat muscle exposed to weightlessness aboard Cosmos 1887.
January 1991, European journal of applied physiology and occupational physiology,
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Preosteoblast production 55 hours after a 12.5-day spaceflight on Cosmos 1887.
January 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology,
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Size and metabolic properties of single muscle fibers in rat soleus after hindlimb suspension.
June 1987, Journal of applied physiology (Bethesda, Md. : 1985),
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Myonuclear number and myosin heavy chain expression in rat soleus single muscle fibers after spaceflight.
July 1996, Journal of applied physiology (Bethesda, Md. : 1985),
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Altered distribution of mitochondria in rat soleus muscle fibers after spaceflight.
August 1992, Journal of applied physiology (Bethesda, Md. : 1985),
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Metabolic effects of spaceflight: Cosmos missions overview.
January 1994, Advances in space biology and medicine,
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Functional properties of slow and fast gastrocnemius muscle fibers after a 17-day spaceflight.
June 2001, Journal of applied physiology (Bethesda, Md. : 1985),
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Effect of spaceflight on the isotonic contractile properties of single skeletal muscle fibers in the rhesus monkey.
January 2000, Journal of gravitational physiology : a journal of the International Society for Gravitational Physiology,
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
[Effect of a flight on the Cosmos-936 biosatellite on the contractile properties of rat muscle fibers].
January 1981, Kosmicheskaia biologiia i aviakosmicheskaia meditsina,
B Miu, and T P Martin, and R R Roy, and V Oganov, and E Ilyina-Kakueva, and J F Marini, and J J Leger, and S C Bodine-Fowler, and V R Edgerton
Metabolic properties of muscle fibers.
December 1986, Federation proceedings,
Copied contents to your clipboard!