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PMID: 141653 Published · ppublish English Journal Article

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

Pflugers Archiv : European journal of physiology ·Vol. 369 ·No. 1 ·1977-05-06 ·Pages 85-9

Syrový I, Gutmann E

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.

MeSH Terms
Adenosine Triphosphatases/metabolism Age Factors Animals Calcium/metabolism Electrophoresis, Polyacrylamide Gel Guinea Pigs Muscle Contraction Muscle Development Muscles/enzymology,physiology Myosins/physiology Rabbits Rats
Chemicals
Adenosine Triphosphatases Myosins Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Syrový I
Gutmann E
References (24)
24 references, click to expand
  1. Substructure of the myosin molecule. II. The light chains of myosin.
    J Mol Biol. 1971 Nov 14;61(3):701-25 PMID: 4257244
  2. The polymorphic forms of tropomyosin and troponin I in developing rabbit skeletal muscle.
    FEBS Lett. 1976 Mar 15;63(1):22-6 PMID: 1261686
  3. Dynamic properties of mammalian skeletal muscles.
    Physiol Rev. 1972 Jan;52(1):129-97 PMID: 4256989
  4. Erroneous interpretations which may result from application of the "myofibrillar ATPase" histochemical procedure to developing muscle.
    Exp Neurol. 1972 Mar;34(3):465-75 PMID: 4260028
  5. Myosin light chains of developing fast and slow rabbit skeletal muscle.
    FEBS Lett. 1976 Aug 1;67(1):68-74 PMID: 133822
  6. Developmental changes in contraction time, myosin properties and fibre pattern of fast and slow skeletal muscles.
    Physiol Bohemoslov. 1974;23(1):19-27 PMID: 4280575
  7. Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscle.
    FEBS Lett. 1975 Jan 1;49(3):320-4 PMID: 122817
  8. Differentiation of myosin in chick embryos.
    J Biochem. 1974 Jul;76(1):123-31 PMID: 4612026
  9. Development of a mammalian fast muscle: dynamic and biochemical properties correlated.
    J Physiol. 1973 Oct;234(1):29-42 PMID: 4271901
  10. Quantification of Coomassie Blue stained proteins in polyacrylamide gels based on analyses of eluted dye.
    Anal Biochem. 1975 Feb;63(2):595-602 PMID: 47719
  11. ATPase activity of myosin correlated with speed of muscle shortening.
    J Gen Physiol. 1967 Jul;50(6):Suppl:197-218 PMID: 4227924
  12. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
    J Biol Chem. 1969 Aug 25;244(16):4406-12 PMID: 5806584
  13. The total nitrogen content of egg albumin and other proteins.
    Biochem J. 1943 Sep;37(3):354-9 PMID: 16747652
  14. The role of myosin in muscular contraction.
    Symp Soc Exp Biol. 1968;22:1-16 PMID: 4235101
  15. Biological activity and the 3-methylhistidine content of actin and myosin.
    Biochem J. 1970 Sep;119(2):293-8 PMID: 4249861
  16. The essentiality of histo- and cytochemical studies of skeletal muscle in the investigation of neuromuscular disease. 1962.
    Neurology. 1998 Sep;51(3):655 and 17 pages following PMID: 9748002
  17. Regulation of isometric contraction in skeletal muscle.
    Exp Neurol. 1976 Mar;50(3):673-83 PMID: 130247
  18. Structural and functional changes of myosin during development: comparison with adult fast, slow and cardiac myosin.
    Dev Biol. 1975 Oct;46(2):317-25 PMID: 241672
  19. Contraction properties and myosin-ATPase activity of fast and slow senile muscles of the rat.
    Gerontologia. 1974;20(4):239-44 PMID: 4282483
  20. DYNAMIC PROPERTIES OF FAST AND SLOW SKELETAL MUSCLES OF THE RAT DURING DEVELOPMENT.
    J Physiol. 1964 Sep;173:74-95 PMID: 14205033
  21. Excitation-contraction latencies in postnatal rat skeletal muscle fibers.
    Exp Neurol. 1970 Oct;29(1):142-51 PMID: 4249101
  22. Developmental changes in the structure and kinetic properties of myosin adenosinetriphosphatase of rabbit skeletal fast muscle.
    J Biochem. 1975 Dec;78(6):1123-33 PMID: 5417
  23. Light chains of myosins from white, red, and cardiac muscles.
    Proc Natl Acad Sci U S A. 1971 May;68(5):946-50 PMID: 4252540
  24. Adaptive transformation of rat soleus motor units during growth.
    J Neurol Sci. 1976 Mar;27(3):269-89 PMID: 131182
Article Info
Journal
Pflugers Archiv : European journal of physiology
Abbr.
Pflugers Arch
ISSN
0031-6768
Published
1977-05-06
Pages
85-9
Language
English
Region
Germany
NLM ID
0154720
Subset
IM
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