Literature DB >> 6186242

Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres.

G Salviati, R Betto, D Danieli Betto.   

Abstract

Rabbit predominantly fast-twitch-fibre and predominantly slow-twitch-fibre skeletal muscles of the hind limbs, the psoas, the diaphragm and the masseter muscles were fibre-typed by one-dimensional polyacrylamide-gel electrophoresis of the myofibrillar proteins of chemically skinned single fibres. Investigation of the distribution of fast-twitch-fibre and slow-twitch-fibre isoforms of myosin light chains and the type of myosin heavy chains, based on peptide 'maps' published in Cleveland. Fischer, Kirschner & Laemmli [(1977) J. Biol. Chem. 252, 1102-1106], allowed a classification of muscle fibres into four classes, corresponding to histochemical types I, IIA, IIB and IIC. Type I fibres with a pure slow-twitch-type of myosin were found to be characterized by a unique set of isoforms of troponins I, C and T, in agreement with the immunological data of Dhoot & Perry [(1979) Nature (London) 278, 714-718], by predominance of the beta-tropomyosin subunit and by the presence of a small amount of an additional tropomyosin subunit, apparently dissimilar from fast-twitch-fibre alpha-tropomyosin subunit. The myofibrillar composition of type IIB fast-twitch white fibres was the mirror image of that found for slow-twitch fibres in that the fast-twitch-fibre isoforms only of the troponin subunits were present and the alpha-tropomyosin subunit predominated. Type IIA fast-twitch red fibres showed a troponin subunit composition identical with that of type IIB fast-twitch white fibres. On the other hand, a unique type of myosin heavy chains was found to be associated with type IIA fibres. Furthermore, the myosin light-chain composition of these fibres was invariably characterized by a small amount of LC3F light chain and by a pattern that was either a pure fast-twitch-fibre light-chain pattern or a hybrid LC1F/LC2F/LC3F/LC1Sb light-chain pattern. By these criteria type IIA fibres could be distinguished from type IIC intermediate fibres, which showed coexistence of fast-twitch-fibre and slow-twitch-fibre forms of myosin light chains and of troponin subunits.

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Year:  1982        PMID: 6186242      PMCID: PMC1153856          DOI: 10.1042/bj2070261

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  41 in total

1.  Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscle.

Authors:  A G Weeds; R Hall; N C Spurway
Journal:  FEBS Lett       Date:  1975-01-01       Impact factor: 4.124

2.  Changes in tropomyosin subunit pattern in chronic electrically stimulated rabbit fast muscles.

Authors:  R K Roy; K Mabuchi; S Sarkar; C Mis; F A Sreter
Journal:  Biochem Biophys Res Commun       Date:  1979-07-12       Impact factor: 3.575

3.  Immunohistochemical evidence for myosin polymorphism in the chicken heart.

Authors:  S Sartore; S Pierobon-Bormioli; S Schiaffino
Journal:  Nature       Date:  1978-07-06       Impact factor: 49.962

4.  Discrimination between fiber populations in mammalian skeletal muscle by using ultrastructural parameters.

Authors:  B R Eisenberg; A M Kuda
Journal:  J Ultrastruct Res       Date:  1976-01

5.  A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels.

Authors:  R C Switzer; C R Merril; S Shifrin
Journal:  Anal Biochem       Date:  1979-09-15       Impact factor: 3.365

6.  Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

Authors:  D W Cleveland; S G Fischer; M W Kirschner; U K Laemmli
Journal:  J Biol Chem       Date:  1977-02-10       Impact factor: 5.157

7.  Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle.

Authors:  L Guth; F J Samaha
Journal:  Exp Neurol       Date:  1969-09       Impact factor: 5.330

8.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

9.  Gene expression of myofibrillar proteins in single muscle fibers of adult chicken: micro two dimensional gel electrophoretic analysis.

Authors:  T Mikawa; S Takeda; T Shimizu; T Kitaura
Journal:  J Biochem       Date:  1981-06       Impact factor: 3.387

10.  Electrophoretic analysis of proteins from single bovine muscle fibres.

Authors:  O A Young; C L Davey
Journal:  Biochem J       Date:  1981-04-01       Impact factor: 3.857

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  39 in total

Review 1.  Vertebrate tropomyosin: distribution, properties and function.

Authors:  S V Perry
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

2.  Hybrid fibres under slow-to-fast transformations: expression is of myosin heavy and light chains in rat soleus muscle.

Authors:  Laurence Stevens; Bruno Bastide; Cyril Bozzo; Yvonne Mounier
Journal:  Pflugers Arch       Date:  2004-05-07       Impact factor: 3.657

3.  Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat.

Authors:  Oleg Andruchov; Stefan Galler
Journal:  Pflugers Arch       Date:  2007-10-25       Impact factor: 3.657

4.  Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation.

Authors:  D M Helfman; S Cheley; E Kuismanen; L A Finn; Y Yamawaki-Kataoka
Journal:  Mol Cell Biol       Date:  1986-11       Impact factor: 4.272

5.  Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibers.

Authors:  R S Staron; D Pette
Journal:  Histochemistry       Date:  1986

6.  Myosin light chains of avian and mammalian slow muscles: peptide mapping of 2S light chains.

Authors:  L Dalla Libera; R Betto; R Lodolo; U Carraro
Journal:  J Muscle Res Cell Motil       Date:  1984-08       Impact factor: 2.698

7.  Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres.

Authors:  R Bottinelli; R Betto; S Schiaffino; C Reggiani
Journal:  J Physiol       Date:  1994-07-15       Impact factor: 5.182

8.  Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibres.

Authors:  H Baumann; M Jäggi; F Soland; H Howald; M C Schaub
Journal:  Pflugers Arch       Date:  1987-08       Impact factor: 3.657

9.  Maximum shortening velocity and coexistence of myosin heavy chain isoforms in single skinned fast fibres of rat skeletal muscle.

Authors:  R Bottinelli; R Betto; S Schiaffino; C Reggiani
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

10.  Contractile properties and myosin isoenzymes of various kinds of Xenopus twitch muscle fibres.

Authors:  J Lännergren
Journal:  J Muscle Res Cell Motil       Date:  1987-06       Impact factor: 2.698

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