Literature DB >> 2956572

Nonuniform myosin expression along single fibers of chronically stimulated and contralateral rabbit tibialis anterior muscles.

R S Staron, D Pette.   

Abstract

Using a combined histochemical and biochemical technique, single fiber analyses were performed on chronically stimulated and contralateral tibialis anterior (TA) muscles of the rabbit. The major fiber population (60%) in 30 days stimulated TA was transforming fibers (type IIC). Some of these fibers displayed a nonuniform distribution of histochemically assessed myofibrillar actomyosin ATPase (mATPase) activity. This heterogeneity of mATPase activity along the fibers was verified in longitudinal sections and by microphotometric evaluation of mATPase staining intensities in serial cross-sections. Biochemical analyses of single fiber segments revealed that these C fibers not only coexpressed fast- and slow-myosin subunits but did so nonuniformly along their length. The distribution of fast- and slow-myosin subunits in these fibers was not random but focal. Variations in myosin expression were also observed in some of the C fibers in the contralateral TA. As opposed to the transforming fibers in the stimulated TA, heterogeneities of mATPase activity and myosin subunits in these contralateral C fibers were less focal and more gradual. These findings suggest that muscle fibers in chronically stimulated TA and the contralateral muscle do not transform synchronously or uniformly along their length.

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Year:  1987        PMID: 2956572     DOI: 10.1007/bf00584751

Source DB:  PubMed          Journal:  Pflugers Arch        ISSN: 0031-6768            Impact factor:   3.657


  16 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.  The time course of glycogen depletion in single fibers of chronically stimulated rabbit fast-twitch muscle.

Authors:  A Maier; D Pette
Journal:  Pflugers Arch       Date:  1987-04       Impact factor: 3.657

3.  Differences in maximum velocity of shortening along single muscle fibres of the frog.

Authors:  K A Edman; C Reggiani; G te Kronnie
Journal:  J Physiol       Date:  1985-08       Impact factor: 5.182

4.  Principle and method of kinetic microphotometric enzyme activity determination in situ.

Authors:  D Pette; H Wasmund; M Wimmer
Journal:  Histochemistry       Date:  1979-11

5.  Heterogeneity in regard to enzymes and metabolites within individual muscle fibers.

Authors:  C S Hintz; M M Chi; O H Lowry
Journal:  Am J Physiol       Date:  1984-03

6.  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

7.  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

8.  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

9.  The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit tibialis anterior muscle.

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

10.  Degeneration-regeneration as a mechanism contributing to the fast to slow conversion of chronically stimulated fast-twitch rabbit muscle.

Authors:  A Maier; B Gambke; D Pette
Journal:  Cell Tissue Res       Date:  1986       Impact factor: 5.249

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  29 in total

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Authors:  A Wernig; A Irintchev; P Weisshaupt
Journal:  J Physiol       Date:  1990-09       Impact factor: 5.182

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.  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

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Authors:  Tertius Abraham Kohn; Kathryn Helen Myburgh
Journal:  J Anat       Date:  2007-01       Impact factor: 2.610

5.  Calcium and strontium activation characteristics of skeletal muscle fibres from the small marsupial Sminthopsis macroura.

Authors:  G J Wilson; D G Stephenson
Journal:  J Muscle Res Cell Motil       Date:  1990-02       Impact factor: 2.698

6.  Functional diversity among a family of human skeletal muscle myosin motors.

Authors:  Daniel I Resnicow; John C Deacon; Hans M Warrick; James A Spudich; Leslie A Leinwand
Journal:  Proc Natl Acad Sci U S A       Date:  2009-12-28       Impact factor: 11.205

7.  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

8.  New method for the accurate characterization of single human skeletal muscle fibres demonstrates a relation between mATPase and MyHC expression in pure and hybrid fibre types.

Authors:  J A Sant'ana Pereira; A Wessels; L Nijtmans; A F Moorman; A J Sargeant
Journal:  J Muscle Res Cell Motil       Date:  1995-02       Impact factor: 2.698

9.  Spatial and temporal patterns of myosin heavy chain expression in developing rat extraocular muscle.

Authors:  J K Brueckner; O Itkis; J D Porter
Journal:  J Muscle Res Cell Motil       Date:  1996-06       Impact factor: 2.698

10.  Myosin Heavy Chain Expression Can Vary over the Length of Jaw and Leg Muscles.

Authors:  J A M Korfage; K E Kwee; V Everts; G E J Langenbach
Journal:  Cells Tissues Organs       Date:  2016-03-08       Impact factor: 2.481

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