scholarly journals Distribution of myosin isoenzymes among skeletal muscle fiber types.

1979 ◽  
Vol 81 (1) ◽  
pp. 10-25 ◽  
Author(s):  
G F Gauthier ◽  
S Lowey
Keyword(s):  
Skeletal Muscle ◽  
The Other ◽  
Light Chains ◽  
Antigenic Determinants ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Limited Region ◽  
Fast Red ◽  
Wide Range ◽  
Myosin Isoenzymes

Using an immunocytochemical approach, we have demonstrated a preferential distribution of myosin isoenzymes with respect to the pattern of fiber types in skeletal muscles of the rat. In an earlier study, we had shown that fluorescein-labeled antibody against "white" myosin from the chicken pectoralis stained all the white, intermediate and about half the red fibers of the rat diaphragm, a fast-twitch muscle (Gauthier and Lowey, 1977). We have now extended this study to include antibodies prepared against the "head" (S1) and "rod" portions of myosin, as well as the alkali- and 5,5'dithiobis (2-nitrobenzoic acid) (DTNB)-light chains. Antibodies capable of distinguishing between alkali 1 and alkali 2 type myosin were also used to localize these isoenzymes in the same fast muscle. We observed, by both direct and indirect immunofluorescence, that the same fibers which had reacted previously with antibodies against white myosin reacted with antibodies to the proteolytic subfragments and to the low molecular-weight subunits of myosin. These results confirm our earlier conclusion that the myosins of the reactive fibers in rat skeletal muscle are sufficiently similar to share antigenic determinants. The homology, furthermore, is not confined to a limited region of the myosin molecule, but includes the head and rod portions and all classes of light chains. Despite the similarities, some differences exist in the protein compositions of these fibers: antibodies to S1 did not stain the reactive (fast) red fiber as strongly as they did the white and intermediate fibers. Non-uniform staining was also observed with antibodies specific for A2 myosin; the fast red fiber again showed weaker fluorescence than did the other reactive fibers. These results could indicate a variable distribution of myosin isoenzymes according to their alkali-light chain composition among fiber types. Alternatively, there may exist yet another myosin isoenzyme which is localized in the fast red fiber. Those red fibers which did not react with any of the antibodies to pectoralis myosin, did react strongly with an antibody against myosin isolated from the anterior latissimus dorsi (ALD), a slow red muscle of the chicken. The myosin in these fibers (slow red fibers) is, therefore, distinct from the other myosin isoenzymes. In the rat soleus, a slow-twitch muscle, the majority of the fibers reacted only with antibody against ALD myosin. A minority, however, reacted with antiboddies to pectoralis as well as ALD myosin, which indicates that both fast and slow myosin can coexist within the same fiber of a normal adult muscle. These immunocytochemical studies have emphasized that a wide range of isoenzymes may contribute to the characteristic physiological properties of individual fiber types in a mixed muscle.

scholarly journals Polymorphism of myosin among skeletal muscle fiber types

1977 ◽  
Vol 74 (3) ◽  
pp. 760-779 ◽  
Author(s):  
GF Gauthier ◽  
S Lowey
Keyword(s):  
Skeletal Muscle ◽  
Motor Units ◽  
Small Region ◽  
Antigenic Determinants ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Rat Diaphragm ◽  
Mitochondrial Content ◽  
Slow Twitch Muscle ◽  
Fast Twitch Muscle

An immunocytochemical approach was used to localize myosin with respect to individual fibers in rat skeletal muscle. Transverse cryostat sections of rat diaphragm, a fast-twitch muscle, were exposed to fluorescein-labeled immunoglobulin against purified chicken pectoralis myosin. Fluorescence microscopy revealed a differential response among fiber types, identified on the basis of mitochondrial content. All white and intermediate fiber but only about half of the red fiber reacted with his antimyosin. In addition, an alkali-stable ATPase had the same pattern of distribution among fibers, which is consistent with the existence of two categories of red fibers. The positive response of certain red fibers indicates either that their myosin has antigenic determinants in common with "white" myosin, or that the immunogen contained a "red" myosin. Myosin, extracted from a small region of the pectorlis which consists entirely of white fibers, was used to prepare an immunoadsorbent column to isolate antibodies specific for white myosin. This purified anti-white myosin reacted with the same fibers of the rat diaphragm that had reacted with the white, intermediate, and some red fibers are sufficiently homologous to share antigenic determinants. In a slow-twitch muscle, the soleus, only a minority of the fiber reacted with antipectoralis myosin. The majority failed to respond; hence, they are not equivalent to intermediate fibers of the diaphragm; despite their intermediate mitochondrial content. Immunocytochemical analysis of two different musles of the rat has demonstrated that more than one isoenzyme of myosin can exist in a single muscle, and that individual fiber types can be recognized by immunological differences in their myosin. We conclude that, in the rat diaphragm, there are at least two immunochemically distinct types of myosin and four types of muscle fibers: white, intermediate, and two red. We suggest that these fibers correspond to the four types of motor units described by Burke et al. (Burke, R. E., D. N. Levine, P. Tsairis, and F. E. Zajac, III 1973. J. Physiol. (Lond) 234:723-748.)in the cat gastrocnemius.`

Characteristics of Skeletal Muscle Fiber Types in the Miniature Pig and the Effect of Training

1973 ◽  
Vol 51 (11) ◽  
pp. 825-831 ◽  
Author(s):  
R. H. Fitts ◽  
F. J. Nagle ◽  
R. G. Cassens
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Histochemistry ◽  
Fiber Type ◽  
Skeletal Muscle Fiber ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Miniature Pig ◽  
Fast Red ◽  
Fiber Type Distribution ◽  
White Fiber

The fiber types present in miniature pig skeletal muscle were determined with enzyme histochemical techniques. Three distinct fiber types were found: a fast white fiber, a fast intermediate fiber, and a slow red fiber. The fiber types found in miniature pig (large mammal) skeletal muscle were different from those in rat (rodent) skeletal muscle where the fiber types are classified as fast white, slow intermediate, and fast red. The fiber type distribution in miniature pig skeletal muscle was not altered by either an endurance or sprint running program, despite physiologically measurable training effects. It is concluded that enzyme histochemistry is a good qualitative tool for assessing the fiber types present in a muscle but lacks the sensitivity to measure or quantitate changes due to training.

Blood flow to different skeletal muscle fiber types during contraction

1983 ◽  
Vol 245 (2) ◽  
pp. H265-H275 ◽  
Author(s):  
B. G. Mackie ◽  
R. L. Terjung
Keyword(s):  
Skeletal Muscle ◽  
Blood Flow ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Oxidative Capacity ◽  
Skeletal Muscle Fiber ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Blood Flows ◽  
Fast Twitch

Blood flow to fast-twitch red (FTR), fast-twitch white (FTW), and slow-twitch red (STR) muscle fiber sections of the gastrocnemius-plantaris-soleus muscle group was determined using 15 +/- 3-microns microspheres during in situ stimulation in pentobarbital-anesthetized rats. Steady-state blood flows were assessed during the 10th min of contraction using twitch (0.1, 0.5, 1, 3, and 5 Hz) and tetanic (7.5, 15, 30, 60, and 120/min) stimulation conditions. In addition, an earlier blood flow determination was begun at 3 min (twitch series) or at 30 s (tetanic series) of stimulation. Blood flow was highest in the FTR (220-240 ml X min-1 X 100 g-1), intermediate in the STR (140), and lowest in the FTW (70-80) section during tetanic contraction conditions estimated to coincide with the peak aerobic function of each fiber type. These blood flows are fairly proportional to the differences in oxidative capacity among fiber types. Further, their absolute values are similar to those predicted from the relationship between blood flow and oxidative capacity found by others for dog and cat muscles. During low-frequency contraction conditions, initial blood flow to the FTR and STR sections were excessively high and not dependent on contraction frequency. However, blood flows subsequently decreased to values in keeping with the relative energy demands. In contrast, FTW muscle did not exhibit this time-dependent relative hyperemia. Thus, besides the obvious quantitative differences between skeletal muscle fiber types, there are qualitative differences in blood flow response during contractions. Our findings establish that, based on fiber type composition, a heterogeneity in blood flow distribution can occur within a whole muscle during contraction.

Influence of training on skeletal muscle enzymatic adaptations in normal and diabetic rats

1985 ◽  
Vol 249 (4) ◽  
pp. E360-E365 ◽  
Author(s):  
E. G. Noble ◽  
C. D. Ianuzzo
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Citrate Synthase ◽  
Diabetic Rats ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Marker Enzymes ◽  
Oxidative Potential ◽  
Hydroxyacyl Coa Dehydrogenase ◽  
Fast Twitch

Muscle homogenates representing slow-twitch oxidative, fast-twitch oxidative-glycolytic, fast-twitch glycolytic, and mixed fiber types were prepared from normal, diabetic, and insulin-treated diabetic rats. Diabetes was induced by injection of 80 mg . kg-1 of streptozotocin. The activities of citrate synthase, succinate dehydrogenase, and 3-hydroxyacyl-CoA dehydrogenase were employed as markers of oxidative potential, whereas phosphorylase, hexokinase, and phosphofructokinase activities were used as an indication of glycolytic capacity. Diabetes was associated with a general decrement in the activity of oxidative marker enzymes for all fiber types except the fast-twitch glycolytic fiber. In contrast, the fast-twitch glycolytic fibers demonstrated the greatest decline in glycolytic enzymatic activity. Insulin-treated animals, either trained or untrained, exhibited enzyme activities similar to their normal counterparts. Exercise training of diabetic rats mimicked the effect of insulin treatment and caused a near normalization of the activity of the marker enzymes. These findings suggest that the enzymatic potential of all skeletal muscle fiber types of diabetic rats may be normalized by exercise training even in the absence of significant amounts of insulin.

Human Skeletal Muscle Fiber Types: Delineation, Development, and Distribution

1997 ◽  
Vol 22 (4) ◽  
pp. 307-327 ◽  
Author(s):  
Robert S. Staron
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Human Skeletal Muscle ◽  
Fiber Type ◽  
Skeletal Muscle Fiber ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Key Words Aging ◽  
Fiber Number ◽  
Human Limb

This brief review attempts to summarize a number of studies on the delineation, development, and distribution of human skeletal muscle fiber types. A total of seven fiber types can be identified in human limb and trunk musculature based on the pH stability/ability of myofibrillar adenosine triphosphatase (mATPase). For most human muscles, mATPase-based fiber types correlate with the myosin heavy chain (MHC) content. Thus, each histochemically identified fiber has a specific MHC profile. Although this categorization is useful, it must be realized that muscle fibers are highly adaptable and that innumerable fiber type transients exist. Also, some muscles contain specific MHC isoforms and/or combinations that do not permit routine mATPase-based fiber typing. Although the major populations of fast and slow are, for the most part, established shortly after birth, subtle alterations take place throughout life. These changes appear to relate to alterations in activity and/or hormonal levels, and perhaps later in life, total fiber number. Because large variations in fiber type distribution can be found within a muscle and between individuals, interpretation of data gathered from human muscle is often difficult. Key words: aging, myosin heavy chains, myogenesis, myofibrillar adenosine triphosphate

scholarly journals Identification of Differentially Expressed Genes in Different Types of Broiler Skeletal Muscle Fibers Using the RNA-seq Technique

2020 ◽  
Vol 2020 ◽  
pp. 1-13
Author(s):  
Han Wang ◽  
Zhonghao Shen ◽  
Xiaolong Zhou ◽  
Songbai Yang ◽  
Feifei Yan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Differentially Expressed Genes ◽  
Muscle Fiber ◽  
Muscle Development ◽  
Skeletal Muscle Fiber ◽  
Differentially Expressed ◽  
Muscle Fiber Types ◽  
Type I ◽  
Fiber Types ◽  
Rna Seq

The difference in muscle fiber types is very important to the muscle development and meat quality of broilers. At present, the molecular regulation mechanisms of skeletal muscle fiber-type transformation in broilers are still unclear. In this study, differentially expressed genes between breast and leg muscles in broilers were analyzed using RNA-seq. A total of 767 DEGs were identified. Compared with leg muscle, there were 429 upregulated genes and 338 downregulated genes in breast muscle. Gene Ontology (GO) enrichment indicated that these DEGs were mainly involved in cellular processes, single organism processes, cells, and cellular components, as well as binding and catalytic activity. KEGG analysis shows that a total of 230 DEGs were mapped to 126 KEGG pathways and significantly enriched in the four pathways of glycolysis/gluconeogenesis, starch and sucrose metabolism, insulin signalling pathways, and the biosynthesis of amino acids. Quantitative real-time reverse transcription polymerase chain reaction (qRT-PCR) was used to verify the differential expression of 7 selected DEGs, and the results were consistent with RNA-seq data. In addition, the expression profile of MyHC isoforms in chicken skeletal muscle cells showed that with the extension of differentiation time, the expression of fast fiber subunits (types IIA and IIB) gradually increased, while slow muscle fiber subunits (type I) showed a downward trend after 4 days of differentiation. The differential genes screened in this study will provide some new ideas for further understanding the molecular mechanism of skeletal muscle fiber transformation in broilers.

PASSIVE CUTANEOUS ANAPHYLAXIS INDUCED IN GUINEA PIGS BY INSULINS AND THEIR COMPONENT CHAINS

1966 ◽  
Vol 44 (7) ◽  
pp. 989-996 ◽  
Author(s):  
S. Wilson ◽  
Marie A. Aprile ◽  
Louise Sasaki
Keyword(s):  
Guinea Pigs ◽  
Competitive Inhibition ◽  
The Other ◽  
Passive Cutaneous Anaphylaxis ◽  
Antigenic Determinants ◽  
Enzymic Digestion ◽  
Heterologous Antiserum ◽  
Wide Range ◽  
Homologous Antiserum

Small amounts of purified ox insulin and its component chains provoked passive cutaneous anaphylaxis (PCA) in guinea pigs previously injected intradermally with antiserum to ox insulin. Cod insulin and its chains also yielded a PCA reaction with antiserum to cod insulin, indicating that antibody-combining sites are located on both the A- and B-chains of insulin Enzymic digestion of the chain preparations essentially destroyed their ability to combine with anaphylactic antibodies, although the B-chain digests had some residual PCA reactivity.Ox and cod insulins gave positive PCA reactions with the heterologous antiserum but at higher levels than with the homologous antiserum, and none of the four chain preparations reacted with the heterologous antiserum. These results demonstrated differences between the antibody-combining sites on the chains of ox and cod insulins.Insulins from a wide range of species also yielded a PCA reaction with antisera to cod and ox insulins, suggesting that the different hormone preparations have certain antigenic determinants in common. Immunologic relationships between several insulins were derived from the competitive inhibition of one antiserum by the other when both were present in the same animal.

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