Literature DB >> 141653

Differentiation of myosin in soleus and extensor digitorum longus muscle in differnt animal species during development.

I Syrový, E Gutmann.   

Abstract

CA2+-ATPase activity and light chains of myosin prepared from fast and slow muscles of rat guinea-pig and rabbit were studied during development from embryonic to old age to establish further correlation with the well-known developmental changes in contraction properties of these muscles. The changes involve the slow soleus muscle much more than the fast extensor digitorum longus muscle. Myosin-ATPase activity of the soleus muscle before or at birth is higher than in the muscle of adult animals. Myosin from the soleus muscle of embryos or newborn animals reveals light chains of myosin of both fast and slow type (with a preponderance of light chains of fast type in 26-days-old rabbit embryos). During postnatal development the amount of light chains of the fast type decreases, that of the slow type increases. Myosin from the soleus muscle of adult animals contains only light chains of the slow type. However, myosin from the soleus muscle of 30-months-old rats exhibits high myosin ATPase activity and contains light chains of myosin of both slow and fast type as in perinatal development. This is in agreement with the shortening of contraction time observed in this muscle in very old age. Thus developmental differentiation of myosine in the soleus muscle is followed by a trend of levelling out of the differences between fast and slow muscles of senescent animals. No such "biphasic" development is observed with respect to the fast extensor digitorum longus muscle.

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Year:  1977        PMID: 141653     DOI: 10.1007/bf00580815

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


  24 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.  The polymorphic forms of tropomyosin and troponin I in developing rabbit skeletal muscle.

Authors:  G W Amphlett; H Syska; S V Perry
Journal:  FEBS Lett       Date:  1976-03-15       Impact factor: 4.124

3.  Myosin light chains of developing fast and slow rabbit skeletal muscle.

Authors:  G Pelloni-muller; M Ermini; E Jenny
Journal:  FEBS Lett       Date:  1976-08-01       Impact factor: 4.124

4.  Differentiation of myosin in chick embryos.

Authors:  T Masaki; C Yoshizaki
Journal:  J Biochem       Date:  1974-07       Impact factor: 3.387

5.  Erroneous interpretations which may result from application of the "myofibrillar ATPase" histochemical procedure to developing muscle.

Authors:  L Guth; F J Samaha
Journal:  Exp Neurol       Date:  1972-03       Impact factor: 5.330

6.  Substructure of the myosin molecule. II. The light chains of myosin.

Authors:  A G Weeds; S Lowey
Journal:  J Mol Biol       Date:  1971-11-14       Impact factor: 5.469

Review 7.  Dynamic properties of mammalian skeletal muscles.

Authors:  R I Close
Journal:  Physiol Rev       Date:  1972-01       Impact factor: 37.312

8.  Developmental changes in contraction time, myosin properties and fibre pattern of fast and slow skeletal muscles.

Authors:  E Gutmann; J Melichna; I Syrový
Journal:  Physiol Bohemoslov       Date:  1974

9.  Quantification of Coomassie Blue stained proteins in polyacrylamide gels based on analyses of eluted dye.

Authors:  C Fenner; R R Traut; D T Mason; J Wikman-Coffelt
Journal:  Anal Biochem       Date:  1975-02       Impact factor: 3.365

10.  Development of a mammalian fast muscle: dynamic and biochemical properties correlated.

Authors:  D B Drachman; D M Johnston
Journal:  J Physiol       Date:  1973-10       Impact factor: 5.182

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  14 in total

1.  Arrest of developmental conversion of type II to type I fibres after suspension hypokinesia.

Authors:  G Asmussen; T Soukup
Journal:  Histochem J       Date:  1991-07

2.  Atrial and ventricular myosin ATPase--divergence with increasing animal species size.

Authors:  I Syrový
Journal:  Pflugers Arch       Date:  1985-05       Impact factor: 3.657

3.  Contractile protein isozymes in muscle development: identification of an embryonic form of myosin heavy chain.

Authors:  R G Whalen; K Schwartz; P Bouveret; S M Sell; F Gros
Journal:  Proc Natl Acad Sci U S A       Date:  1979-10       Impact factor: 11.205

4.  Changes in rat ventricular myosin in old age.

Authors:  I Syrový
Journal:  Experientia       Date:  1984-01-15

5.  Independent development of contractile properties and myosin light chains in embryonic chick fast and slow muscle.

Authors:  D Pette; G Vrbová; R C Whalen
Journal:  Pflugers Arch       Date:  1979-01-31       Impact factor: 3.657

Review 6.  Contractile proteins in muscle disease.

Authors:  P Cummins
Journal:  J Muscle Res Cell Motil       Date:  1983-02       Impact factor: 2.698

7.  The myofibrillar ATPase activity and the substructure of myosin in the hypertrophied left ventricle of the rat.

Authors:  I Medugorac
Journal:  Basic Res Cardiol       Date:  1980 Jan-Feb       Impact factor: 17.165

8.  Myosin isoform transitions in four rabbit muscles during postnatal growth.

Authors:  F Gondret; L Lefaucheur; A D'Albis; M Bonneau
Journal:  J Muscle Res Cell Motil       Date:  1996-12       Impact factor: 2.698

9.  Molecular cloning and characterization of different expression of MYOZ2 and MYOZ3 in Tianfu goat.

Authors:  Lu Wan; Jisi Ma; Nianlu Wang; Daihua Wang; Gangyi Xu
Journal:  PLoS One       Date:  2013-12-18       Impact factor: 3.240

10.  Myofibril and sarcoplasmic reticulum changes with exercise and growth.

Authors:  A N Belcastro; H Wenger
Journal:  Eur J Appl Physiol Occup Physiol       Date:  1982
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