2 edition of Electrophoretic myosin isoforms of skeletal muscles and single muscle fibers found in the catalog.
Electrophoretic myosin isoforms of skeletal muscles and single muscle fibers
Written in English
|Statement||by Sally Blank.|
|The Physical Object|
|Pagination||ix, 93 leaves, bound :|
|Number of Pages||93|
Two kinds of slow skeletal muscle fibers which differ in their myosin light chain complements. FEBS Lett. Dec 15; (1)– [Google Scholar] Sorenson MM, Reuben JP, Eastwood AB, Orentlicher M, Katz GM. Functional heterogeneity of the sarcoplasmic reticulum within sarcomeres of skinned muscle by: Human skeletal muscle is composed of three main fiber types. These fibers are commonly classified on the basis of their myosin ATPase content (i.e., I, IIa, IIb) or myosin heavy chain (MHC) composition (i.e., I, IIa, IIx) ().Individual muscle fibers may contain more than one MHC isoform (i.e., I/IIa, IIa/IIx, I/IIa/IIx); however, these “hybrid” fibers are difficult to detect with.
Billeter R, Heizmann CW, Howald H, Jenny E. Analysis of myosin light and heavy chain types in single human skeletal muscle fibers. Eur J Biochem. May 15; (2)– Biral D, Damiani E, Volpe P, Salviati G, Margreth A. Polymorphism of myosin light chains. An electrophoretic and immunological study of rabbit skeletal-muscle by: To our knowledge, the current study is the first to directly examine the single-fiber MyHC isoform composition of rodent laryngeal muscle. This approach yielded 3 unique findings. First, results of the single-fiber analyses clearly demonstrate that most fibers in both the PCA and TA muscles exhibit MyHC by:
Myosin Isoforms-help to identify the fiber type of a given muscle -regular skeletal muscles-only contract. Stretch Reflex-simplest, monosynaptic -group of specialized muscle fibers found between regular skeletal muscle fibers (extrafusal)-consists of small, specialized intrafusal fibers and nerve endings (sensory and motor). discovery of the variability of myosin isoforms and the resulting molecular heterogeneity of muscle fibers, the dominant MHC isoform has been considered to be responsible for functional differences of skeletal muscles. The plasticity of muscle phenotype in response to different factors was documented in numerous studies.
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Electrophoretic analysis of single muscle fibers from elite athletes revealed a MHC phenotype composition of 46 +/- 6% type I, 21 +/- 6% type IIa, and 0% type IIx, whereas 34% of the single fibers.
The MHC protein expressed in a single muscle fiber is correlated to its maximum contraction velocity (5, 28, 32), which is related to the maximum myosin ATPase activity of a muscle (2).
The myofibrillar and myosin ATPase activities of a muscle are related to the isoforms of myosin expressed in the muscle. The functional role of MHC isoforms has been in part clarified by correlated biochemical-physiological studies on single skinned fibers: these studies, in agreement with results from in vitro motility assays, indicate that both MHC and MLC isoforms determine the maximum velocity of shortening of skeletal muscle fibers.
the MHC IIa and MHC IIx isoforms. Second, approxi-mately fibers per muscle sample are required to deter-mine the muscle’s fiber type. Multiple sampling periods and the number of subjects for longitudinal studies can therefore result in the need for identification of a large number of fibers; thus the duration of each electrophoreticCited by: Immunological studies and proteolytic analysis of myosin heavy chains from the three type of fibers have demonstrated the presence of distinct myosin isoforms.
By using typed single muscle fibers and improving an electrophoretic method we are able to resolve three distinct polypeptides which are demonstrate to correspond to type 1, 2A and 2B Cited by: muscles of different mammalian species contain four major myosin heavy- chain (MHC) isoforms: the “slow” or,&MHC and the three “fast” IIa- 11x- and IIb-MHCs; and three major myosin light-chain (MLC) isoforms, theFile Size: 2MB.
A new technique for the sodium dodecyl sulfate-polyacrylamide gel electrophoretic separation of rat skeletal muscle myosin heavy-chain (MHC) isoforms is presented. This technique allows for the separation of the four identified MHC isoforms known to be present in adult rat skeletal by: KEY WORDS myosin isoforms; skeletal muscle; muscle ﬁber types ABSTRACT Skeletal muscle is an extremely heterogeneous tissue composed of a variety of fast and slow ﬁber types and subtypes.
Moreover, muscle ﬁbers are versatile entities capable of adjusting their phenotypic properties in response to altered functional demands. Major differencesFile Size: KB. It has been demonstrated that extraocular muscles exhibit higher ATPase activi- ties than skeletal muscles .
The sum ofMHCeom and MHCIIb, the fastest among the skeletal MHC isoforms , amounts to % of the total MHC isoforms in the oculorotatory muscles. This predominance of fast isoforms is the basis for fast cross-bridge by: Muscles containing predominantly 2X-MHC display a velocity of shortening intermediate between that of slow muscles and that of fast muscles composed predominantly of 2B fibres.
Mammalian skeletal muscles consist of three main fibre types, type 1, 2A and 2B fibres, with different myosin heavy chain (MHC) by: (MyHC) isoforms have been identified in adult skeletal muscle of a number of species: types I, IIa, IIx or IId, and IIb.
The aim of this study was to investigate the distribution of various MyHC isoforms in the equine gluteus medius and gluteus profundus muscles in relation with several morpho- metric variables of muscle by: MyLC isoforms pattern in horse, rat, and human skeletal muscle to clarify the role of myosin isoforms in skeletal muscles of small and large mammalian and human mus- cle as well as in muscle with differences in twitch char- acteristics.
MATERIALS AND METHODS. Declaration. 10 sedentary male humans (body mass ± kg,File Size: KB. ) Termin, A., Staron, R. & Pette, D. Changes in myosin heavy chain isoforms during chronic low-frequency stimulation of rat fast hindlimb muscles: a single-fiber study.
Eur. : Masanobu Wada, Shigeru Katsuta. Combined histochemical and biochemical analyses were performed on rat skeletal muscles in order to determine the myosin heavy chain patterns in specific fiber types. Four myosin heavy chain isoforms were separated by gradient polyacrylamide gel electrophoresis of extracts from single fibers and whole muscle homogenates.
Their electrophoretic mobility increased in the order Cited by: Four myosin heavy chain isoforms were separated by gradient polyacrylamide gel electrophoresis of extracts from single fibers and whole muscle homogenates.
Their electrophoretic mobility increased. Key words: Horse, Gluteus medius, Muscle fiber type, Electrophoresis Myosin is the predominant protein in skeletal mus- cle, and it makes up the largest portion of the contrac- tile apparatus of muscle fibers. This protein consists of four light chains and two heavy chains.
Myosin heavy chain (MyHC) isoforms are encoded by a multigeneCited by: Diversity in muscle contractile properties is based on the variability of contractile properties of single muscle fibers which in turn is related to the presence of different myosin heavy-chain (MyHC) isoforms.
Human jaw muscles are featured by many hybrid fibers expressing more than one MyHC by: Two populations of histochemically identified type-I fibres were found differing in the number of light-chain isoforms of the constituent myosin, whereas the pattern of light chains of fast myosin of type-IIA and type-IIB fibres was by: myosin and type I fibers only slow myosin , but there are conflicting results about the number of light chains in human myosin [6- One approach to the study of myosin types in mixed muscles is to analyse isolated single fibers.
In the only previous study of this kind on human muscle Cited by: There is a significant technical obstacle, however, in estimating the number of cross bridges in a single fiber.
In this study, we have developed a procedure for extraction and quantification of myosin heavy chains (MHCs) that permits the routine and direct measurement of the myosin content in single muscle fibers.
Chemomechanical transduction was studied in single fibers isolated from human skeletal muscle containing different myosin isoforms. Permeabilized fibers were activated by laser-pulse photolytic release of mM ATP from p(2-nitrophenyl)ethylester of ATP. The ATP hydrolysis rate in the muscle fibers was determined with a fluorescently labeled phosphate-binding by: FIGURE 1.
15% SDS-PAGE gel of purified proteins. The lane with soleus myosin displays both light chains (LC) and the lane with sol S1 only a single essential light chain(MLC2s).The light chain content differs for the fast and slow isoform as it can be seen in comparison to lanes for pso S1 and for skeletal S1 (bulk preparation from the back and leg rabbit muscles) which both contain .().
Two fiinctionally distinct myosin heavy chain isoforms in slow skeletal muscle fibres. FEBSLett(). Type 1, 2A and 2B myosm heavy cham electrophoretic analysis of rat muscle fibers Author: Susan Kate Bortolotto.