Literature DB >> 3197085

A combined histochemical and immunohistochemical study on the dynamics of fast-to-slow fiber transformation in chronically stimulated rabbit muscle.

A Maier1, L Gorza, S Schiaffino, D Pette.   

Abstract

Chronically stimulated fast-twitch muscles of the rabbit were histochemically and immunohistochemically analyzed in serial cross sections (1) for percentages of fiber types, and (2) for the presence of myosin heavy chain isoforms during fast-to-slow transformation. By four weeks of stimulation the number of type-I fibers had increased more than fourfold, while only about 6% of the original IIB fibers remained. Type-IC and -IIC fibers transiently rose to 20% of the total fiber population. After 16 weeks, the number of type-I fibers had increased to 42%. With prolonged stimulation fewer fibers reacted with antibodies against embryonic and neonatal myosins and more with the antibody against slow myosin. The reaction for embryonic myosin was most often detected in the C fibers (IC, IIC). Immunohistochemical subtypes were observed for each fiber type in the stimulated muscles. The greatest number was seen in type-IIC fibers, which, in addition to their reaction for fast/neonatal and slow myosins, might also react with the antibodies against neonatal/embryonic and embryonic myosins. These findings indicated that the transforming fibers temporarily expressed myosin heavy chain isoforms normally not detectable in adult skeletal muscle. Myotubes reacted strongly with the antibodies against fast/neonatal and embryonic myosins, and some of them also with the antibody against slow myosin. Thus, it appears that under the influence of the low frequency stimulus pattern some of the newly formed myotubes developed into type-I fibers.

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Year:  1988        PMID: 3197085     DOI: 10.1007/bf00220017

Source DB:  PubMed          Journal:  Cell Tissue Res        ISSN: 0302-766X            Impact factor:   5.249


  38 in total

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

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

2.  Coexistence of fast and slow type myosin light chains in single muscle fibres during transformation as induced by long term stimulation.

Authors:  D Pette; U Schnez
Journal:  FEBS Lett       Date:  1977-11-01       Impact factor: 4.124

3.  Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles.

Authors:  J F Hoh; G P Yeoh
Journal:  Nature       Date:  1979-07-26       Impact factor: 49.962

4.  Three "myosin adenosine triphosphatase" systems: the nature of their pH lability and sulfhydryl dependence.

Authors:  M H Brooke; K K Kaiser
Journal:  J Histochem Cytochem       Date:  1970-09       Impact factor: 2.479

5.  Regenerating adult chicken skeletal muscle and satellite cell cultures express embryonic patterns of myosin and tropomyosin isoforms.

Authors:  R Matsuda; D H Spector; R C Strohman
Journal:  Dev Biol       Date:  1983-12       Impact factor: 3.582

6.  A monoclonal antibody to the embryonic myosin heavy chain of rat skeletal muscle.

Authors:  B Gambke; N A Rubinstein
Journal:  J Biol Chem       Date:  1984-10-10       Impact factor: 5.157

7.  Ipsi- and contralateral fibre transformations by cross-reinnervation. A principle of symmetry.

Authors:  H Reichmann; T Srihari; D Pette
Journal:  Pflugers Arch       Date:  1983-05       Impact factor: 3.657

8.  Myosin isozymes in avian skeletal muscles. I. Sequential expression of myosin isozymes in developing chicken pectoralis muscles.

Authors:  S Lowey; P A Benfield; D D LeBlanc; G S Waller
Journal:  J Muscle Res Cell Motil       Date:  1983-12       Impact factor: 2.698

9.  Ipsi-and contralateral changes in rabbit soleus myosins by cross-reinnervation.

Authors:  T Srihari; U Seedorf; D Pette
Journal:  Pflugers Arch       Date:  1981-06       Impact factor: 3.657

10.  The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle.

Authors:  R S Staron; D Pette
Journal:  Biochem J       Date:  1987-05-01       Impact factor: 3.857

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  22 in total

1.  Transient expression of myosin heavy chain MHCI alpha in rabbit muscle during fast-to-slow transition.

Authors:  H Peuker; A Conjard; C T Putman; D Pette
Journal:  J Muscle Res Cell Motil       Date:  1999-02       Impact factor: 2.698

2.  Partial fast-to-slow conversion of regenerating rat fast-twitch muscle by chronic low-frequency stimulation.

Authors:  Dirk Pette; Janez Sketelj; Dejan Skorjanc; Elmi Leisner; Irmtrud Traub; Fajko Bajrović
Journal:  J Muscle Res Cell Motil       Date:  2002       Impact factor: 2.698

3.  Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi.

Authors:  M J Kushmerick; T S Moerland; R W Wiseman
Journal:  Proc Natl Acad Sci U S A       Date:  1992-08-15       Impact factor: 11.205

4.  Assessment of muscle mass and strength in mice.

Authors:  Andrea Bonetto; Daniel C Andersson; David L Waning
Journal:  Bonekey Rep       Date:  2015-08-19

5.  Relations between chronic stimulation-induced changes in contractile properties and the Ca2+-sequestering system of rat and rabbit fast-twitch muscles.

Authors:  J A Simoneau; M Kaufmann; K T Härtner; D Pette
Journal:  Pflugers Arch       Date:  1989-09       Impact factor: 3.657

6.  In situ hybridization of slow myosin heavy chain mRNA in normal and transforming rabbit muscles with the use of a nonradioactively labeled cRNA.

Authors:  S Aigner; D Pette
Journal:  Histochemistry       Date:  1990

7.  Morphological changes during fiber type transitions in low-frequency-stimulated rat fast-twitch muscle.

Authors:  M D Delp; D Pette
Journal:  Cell Tissue Res       Date:  1994-08       Impact factor: 5.249

8.  Fibre composition of rabbit tibialis anterior and extensor digitorum longus muscles.

Authors:  O Hudlicka
Journal:  J Anat       Date:  1995-04       Impact factor: 2.610

9.  The response of adult and developing rat plantaris muscle to overload.

Authors:  R Frischknecht; D Belverstone; G Vrbová
Journal:  Pflugers Arch       Date:  1995-12       Impact factor: 3.657

10.  Analysis of Ca2+ and Sr2+ activation characteristics in skinned muscle fibre preparations with different proportions of myofibrillar isoforms.

Authors:  G S Lynch; D G Stephenson; D A Williams
Journal:  J Muscle Res Cell Motil       Date:  1995-02       Impact factor: 2.698

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