Comparison of fiber types in skeletal muscles from ten animal species based on sensitivity of the myofibrillar actomyosin ATPase to acid or copper.
Abstract: Comparisons were made of the histochemical characteristics of skeletal muscle from 10 animal species. The basic comparison was made from the staining patterns for the myofibrillar actomyosin ATPase produced by preincubation of fresh frozen cross-sections of muscle at alkaline pH (10.30) or acid pH (4.60) with those produced by preincubation in media containing Cu2+ at alkaline pH (10.30), near neutral pH (7.40), or acid pH (4.60). Muscle sections were also stained for reduced nicotinamide adenine dinucleotide tetrazolium reductase and alpha-glycerophosphate dehydrogenase to provide an indication of the relative oxidative and glycolytic capacity of the different fiber types. Type II fibers in mixed fibered muscles were either very sensitive, moderately sensitive, or relatively insensitive to inactivation of the myofibrillar actomyosin ATPase after acid preincubation. These fibers were identified as type IIA1, IIA2, and IIA3, respectively. The myofibrillar actomyosin ATPase of the type I fibers of these muscles, with the exception of those in mouse muscle, was activated by pretreatment with acid. A separation of animal species was possible based on the stability of the IIA1 fibers to inclusion of Cu2+ in the preincubation medium. For one group of animals (rat, mouse, monkey, man, dog, rabbit, and cow), a reciprocal relationship existed between lability to acid and stability to Cu2+ for type IIA1 and IIA3 fibers, respectively. For the second group of animals (horse, ass, and cat) there was a parallel relationship between lability or stability of the type IIA1 and IIA3 fibers to pretreatment with either acid or Cu2+.
Publication Date: 1985-01-01 PubMed ID: 3158628DOI: 10.1007/BF00708203Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research focuses on comparing the characteristics of skeletal muscle from ten animal species by assessing their sensitivity to acid or copper, specifically noting variations in the myofibrillar actomyosin ATPase enzyme.
Objective of the Study
- The main aim of this research was to study and compare the histochemical characteristics of skeletal muscles from ten different animal species.
- The focus was on analyzing the reaction patterns of the myofibrillar actomyosin ATPase, an enzyme involved in muscle contraction, in varying pH environments, including alkaline, near neutral, and acidic conditions.
Methodology
- For the analysis, fresh frozen cross-sections of animal skeletal muscles were preincubated in various pH conditions: alkaline pH (10.30), acid pH (4.60), in media containing Cu2+ at alkaline pH (10.30), near-neutral pH (7.40), or acid pH (4.60).
- Muscle sections were also stained for reduced nicotinamide adenine dinucleotide tetrazolium reductase and alpha-glycerophosphate dehydrogenase. This process provided an estimate of the relative oxidative and glycolytic capacities of the varied fiber types in the tested muscles.
Findings
- The research identified that Type II fibers in muscles varied in their sensitivity levels to inactivation of myofibrillar actomyosin ATPase after acid preincubation. These fibers were categorized as Type IIA1 (very sensitive), Type IIA2 (moderately sensitive), and Type IIA3 (relatively insensitive).
- With the exception of mouse muscles, it was observed that the myofibrillar actomyosin ATPase of Type I fibers was activated by acid pretreatment.
- A distinction could be drawn among the animal species based upon the stability of the Type IIA1 fibers when Cu2+ was included in the preincubation medium.
- A reciprocal relationship was observed among certain animals (rat, mouse, monkey, man, dog, rabbit, and cow) with regards to the sensitivity to acid and stability to copper of Type IIA1 and IIA3 fibers. For another group of animals (horse, ass, and cat), a parallel relationship was observed in the sensitivity/stability of Type IIA1 and IIA3 fibers when pretreated with either acid or copper.
Cite This Article
APA
Matoba H, Allen JR, Bayly WM, Oakley CR, Gollnick PD.
(1985).
Comparison of fiber types in skeletal muscles from ten animal species based on sensitivity of the myofibrillar actomyosin ATPase to acid or copper.
Histochemistry, 82(2), 175-183.
https://doi.org/10.1007/BF00708203 Publication
Researcher Affiliations
MeSH Terms
- Actomyosin / analysis
- Adenosine Triphosphatases / analysis
- Animals
- Cats
- Cattle
- Copper / pharmacology
- Dogs
- Glycerolphosphate Dehydrogenase / analysis
- Haplorhini
- Horses
- Humans
- Hydrogen-Ion Concentration
- Mice
- Muscles / enzymology
- Myofibrils / enzymology
- NADH Tetrazolium Reductase / analysis
- Rabbits
- Rats
- Species Specificity
References
This article includes 21 references
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Citations
This article has been cited 3 times.- Bowtell JL, Marwood S, Bruce M, Constantin-Teodosiu D, Greenhaff PL. Tricarboxylic acid cycle intermediate pool size: functional importance for oxidative metabolism in exercising human skeletal muscle.. Sports Med 2007;37(12):1071-88.
- Jump SS, Schuenke MD, Staron RS. Postmortem alterations in the pH range of myofibrillar ATPase activation/inactivation.. Histochem Cell Biol 2003 Feb;119(2):161-8.
- Takekura H, Yoshioka T. Different metabolic responses to exercise training programmes in single rat muscle fibres.. J Muscle Res Cell Motil 1990 Apr;11(2):105-13.
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