Literature DB >> 3699015

Comparison of myosins from the masseter muscle of adult rat, mouse and guinea-pig. Persistence of neonatal-type isoforms in the murine muscle.

A d'Albis, C Janmot, J J Bechet.   

Abstract

Adult rat, mouse, and guinea-pig masseter muscles display distinct myosin electrophoretic patterns. The rat muscle contains four main forms which by reference to the myosins of the IIB tensor fasciae latae, of the IIA mylohyoid, and of the red and white portions of the sternomastoid muscles, correspond respectively to the intermediate-type and to the three fast-type isoforms. The mouse masseter muscle contains only three main myosins, the intermediate-type and two fast-type isoforms. The guinea-pig muscle also displays only three bands, whose assignment is, however, less straightforward than in the murine species; their electrophoretic mobilities are not strictly the same as those of their homologous forms in rat and mouse. Comparison with the myosins of the tensor fasciae latae and of the sternomastoid muscles of guinea-pig allows their identification as intermediate and fast-type myosins. In addition to these typical adult-type forms, adult murine masseter muscles are observed to contain between zero and 30% of neonatal-type myosins. The comparison of the developmental transitions of myosins in the rat masseter with those in the skeletal muscles of the same animal indicates a delay in the appearance of the adult as well as in the disappearance of the neonatal-type myosins in the masseter muscle. Both the variability in myosin types with the animal species and the atypical presence of neonatal forms in the murine adults suggest that myosin expression in the masseter muscle is subjected to unusual regulations.

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Year:  1986        PMID: 3699015     DOI: 10.1111/j.1432-1033.1986.tb09580.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  16 in total

1.  Presence of cardiac alpha-myosin correlates with histochemical myosin Ca2+ ATPase activity in rabbit masseter muscle.

Authors:  J J Bredman; W A Weijs; A F Moorman
Journal:  Histochem J       Date:  1992-05

2.  Intrinsic properties of the adult human mylohyoid muscle: neural organization, fiber-type distribution, and myosin heavy chain expression.

Authors:  Min Ren; Liancai Mu
Journal:  Dysphagia       Date:  2005       Impact factor: 3.438

3.  Immunocytochemical and electrophoretic analyses of changes in myosin gene expression in cat posterior temporalis muscle during postnatal development.

Authors:  J F Hoh; S Hughes; C Chow; P T Hale; R B Fitzsimons
Journal:  J Muscle Res Cell Motil       Date:  1988-02       Impact factor: 2.698

4.  Comparison of the foetal development of fibre types in four bovine muscles.

Authors:  B Picard; J Robelin; F Pons; Y Geay
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

5.  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

6.  Identification and pattern of transitions of some developmental and adult isoforms of fast troponin T in some human and rat skeletal muscles.

Authors:  M A Sabry; G K Dhoot
Journal:  J Muscle Res Cell Motil       Date:  1991-10       Impact factor: 2.698

7.  Myosin heavy chain expression in rabbit masseter muscle during postnatal development.

Authors:  J J Bredman; W A Weijs; H A Korfage; P Brugman; A F Moorman
Journal:  J Anat       Date:  1992-04       Impact factor: 2.610

8.  Myosin isoform transitions during development of extra-ocular and masticatory muscles in the fetal rat.

Authors:  F Mascarello; A M Rowlerson
Journal:  Anat Embryol (Berl)       Date:  1992

9.  Force-velocity relation and isomyosins in soleus muscles from two strains of mice (C57 and NMRI).

Authors:  G Maréchal; G Beckers-Bleukx
Journal:  Pflugers Arch       Date:  1993-09       Impact factor: 3.657

10.  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

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