Literature DB >> 7191084

Associated changes in Ca2+ and Sr2+ activation properties and fiber proteins in cross-reinnervated rabbit soleus.

D J Secrist, W G Kerrick.   

Abstract

Changes in the Ca2+ and Sr2+ activation properties of functionally skinned slow-twitch soleus fibers were measured and compared with those of normal fast-twitch extensor digitorum longus (EDL) following cross-reinnervation of soleus with the nerve to EDL. Most of the fibers showed either complete transformation of activtion properties (66%) or remained unchanged (34%). The change in sensitivity to divalent cations was correlated with changes in the proteins present in fibers pooled on the basis of their activation properties. The banding patterns of the 35,000- and 37,500-dalton proteins (tropomyosin and troponin T) in cross-reinnervated soleus were correspondingly transformed to those of normal EDL. Slow and fast myosin light chains were present in the pooled cross-reinnervated fibers. Fiber distributions based on activation properties were confirmed by histochemical features. For the first time it has been demonstrated that cross-reinnervation produced changes in the activation properties of soleus fibers and associated changes in the regulatory proteins measured.

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Year:  1980        PMID: 7191084     DOI: 10.1007/bf00584556

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


  34 in total

1.  Time dependent effects on contractile properties, fibre population, myosin light chains and enzymes of energy metabolism in intermittently and continuously stimulated fast twitch muscles of the rabbit.

Authors:  D Pette; W Müller; E Leisner; G Vrbová
Journal:  Pflugers Arch       Date:  1976-07-30       Impact factor: 3.657

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.  The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils.

Authors:  J D Potter
Journal:  Arch Biochem Biophys       Date:  1974-06       Impact factor: 4.013

4.  The subunits and biological activity of polymorphic forms of tropomyosin.

Authors:  P Cummins; S V Perry
Journal:  Biochem J       Date:  1973-08       Impact factor: 3.857

5.  Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits.

Authors:  J B Peter; R J Barnard; V R Edgerton; C A Gillespie; K E Stempel
Journal:  Biochemistry       Date:  1972-07-04       Impact factor: 3.162

6.  Procedure for the histochemical demonstration of actomyosin ATPase.

Authors:  L Guth; F J Samaha
Journal:  Exp Neurol       Date:  1970-08       Impact factor: 5.330

7.  Muscle fiber types: how many and what kind?

Authors:  M H Brooke; K K Kaiser
Journal:  Arch Neurol       Date:  1970-10

8.  The effect of cross reinnervation on the synthesis of myosin light chains.

Authors:  F A Sréter; J Gergely
Journal:  Biochem Biophys Res Commun       Date:  1974-01       Impact factor: 3.575

9.  The components of troponin from chicken fast skeletal muscle. A comparison of troponin T and troponin I from breast and leg muscle.

Authors:  J M Wilkinson
Journal:  Biochem J       Date:  1978-01-01       Impact factor: 3.857

10.  Rabbit diaphragm: two types of fibres determined by calcium strontium activation and protein content.

Authors:  P E Hoar; W G Kerrick
Journal:  J Physiol       Date:  1979-10       Impact factor: 5.182

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  2 in total

1.  Temperature-dependent calcium sensitivity changes in skinned muscle fibres of rat and toad.

Authors:  D G Stephenson; D A Williams
Journal:  J Physiol       Date:  1985-03       Impact factor: 5.182

2.  Myosin isozymes in normal and cross-reinnervated cat skeletal muscle fibers.

Authors:  G F Gauthier; R E Burke; S Lowey; A W Hobbs
Journal:  J Cell Biol       Date:  1983-09       Impact factor: 10.539

  2 in total

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