Distribution of fiber types in locomotory muscles of dogs. 1982

R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor

The distribution of Type I and Type II fibers, as determined from histochemical estimation of myofibrillar ATPase activity, was studied within and among the locomotory muscles of the forelimb, trunk, and hindlimb of three mongrel dogs. All Type II fibers had high oxidative capacities as estimated from the histochemical assay for reduced nicotinamide adenine dinucleotide tetrazolium reductase, so they were not further divided into subpopulations. Furthermore, Type I and Type II fibers had similar oxidative potentials as indicated by both histochemistry and biochemistry. Type I fiber populations ranged between 14% and 100% in the muscles sampled. The highest percentages of Type I fibers were found in deep muscles of physiological extensor groups in the arm and thigh that serve to resist gravity (antigravity muscles) when the dog is in the quadrupedal standing position. More superficial muscles in these same groups had fewer Type I fibers. The patterns of Type I fiber distribution among muscles in the antigravity groups of the forearm and leg were the opposite of those in the arm and thigh, with the more superficial muscles of the distal limb segments having more Type I fibers than the deeper muscles. In all limb segments, muscle groups that do not serve to resist gravity did not show as much intermuscular variation. Type I fiber populations in these muscles did not exceed 50%. A stratification of fiber types also existed within muscles, both in extensor and flexor groups, with the deeper portions of the muscles having more Type I fibers than the more superficial portions.

UI MeSH Term Description Entries
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009246 NADH Tetrazolium Reductase Catalyzes the reduction of tetrazolium compounds in the presence of NADH. NAD(P)H Nitroblue Tetrazolium Reductase,NADH2 Tetrazolium Reductase,Reductase, NADH Tetrazolium,Reductase, NADH2 Tetrazolium,Tetrazolium Reductase, NADH,Tetrazolium Reductase, NADH2
D009929 Organ Size The measurement of an organ in volume, mass, or heaviness. Organ Volume,Organ Weight,Size, Organ,Weight, Organ
D010732 Phosphofructokinase-1 An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. D-tagatose- 6-phosphate and sedoheptulose-7-phosphate also are acceptors. UTP, CTP, and ITP also are donors. In human phosphofructokinase-1, three types of subunits have been identified. They are PHOSPHOFRUCTOKINASE-1, MUSCLE TYPE; PHOSPHOFRUCTOKINASE-1, LIVER TYPE; and PHOSPHOFRUCTOKINASE-1, TYPE C; found in platelets, brain, and other tissues. 6-Phosphofructokinase,6-Phosphofructo-1-kinase,Fructose-6-P 1-Kinase,Fructose-6-phosphate 1-Phosphotransferase,6 Phosphofructokinase,Phosphofructokinase 1
D005121 Extremities The farthest or outermost projections of the body, such as the HAND and FOOT. Limbs,Extremity,Limb
D006651 Histocytochemistry Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods. Cytochemistry
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
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

R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
August 1998, Journal of morphology,
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
May 1989, The Anatomical record,
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
January 1992, Journal of craniomandibular disorders : facial & oral pain,
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
October 1990, Journal of applied physiology (Bethesda, Md. : 1985),
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
August 1988, Shigaku = Odontology; journal of Nihon Dental College,
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
October 2011, Physiological reviews,
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
February 1987, Developmental biology,
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
January 2001, The Journal of experimental biology,
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
April 1987, Journal of applied physiology (Bethesda, Md. : 1985),
R B Armstrong, and C W Saubert, and H J Seeherman, and C R Taylor
December 1980, The Journal of experimental zoology,
Copied contents to your clipboard!