Literature DB >> 1491074

Differences in maximal activation properties of skinned short- and long-sarcomere muscle fibres from the claw of the freshwater crustacean Cherax destructor.

J M West1, D C Humphris, D G Stephenson.   

Abstract

Single fibres of different sarcomere length at rest have been isolated from the claw muscle of the yabby (Cherax destructor), a decapod crustacean. Fibres of either long (SL > 6 microns) or short (SL < 4 microns) sarcomere length have been mechanically skinned and were maximally activated by Ca2+ and Sr2+ under various experimental conditions (ionic strength, in the presence of 2,3 butanedione monoxime (BDM)) to determine differences in their contractile properties. Isometric force was measured simultaneously with either myofibrillar MgATPase or fibre stiffness in both fibre types. The ultrastructure of individual long- and short-sarcomere fibres was also determined by electron microscopy. The long-sarcomere fibres developed greater tension (30.48 +/- 1.72 N cm-2) when maximally activated by Ca2+ compared with the short-sarcomere fibres (18.60 +/- 0.80 N cm-2). The difference in the maximum Ca(2+)-activated force can be explained by the difference in the amount of filament overlap between the two fibre types. The maximum Ca(2+)-activated myofibrillar MgATPase rate in the short-sarcomere fibres (1.60 +/- 0.27 mmol ATP l-1s-1) was higher, but not significantly different from the ATPase rate in fibres with long-sarcomeres (1.09 +/- 0.14 mmol ATP l-1s-1). As the concentration of myosin is estimated to be higher only by a factor of 1.22 in the short-sarcomere preparations there is no evidence to suggest that the myofibrillar MgATPase activity is different in the long- and short-sarcomere preparations. The maximum Ca(2+)-activated force (P0) of both short- and long-sarcomere fibres was quite insensitive to BDM compared with vertebrate muscle. Force decreased to 60.2 +/- 5.3% and 76.1 +/- 2.7% in the short- and long-sarcomere fibres respectively in the presence of 100 mmol l-1 BDM. The difference in the force depression between the long- and short-sarcomere fibres is statistically significant (p < 0.05). Fibre stiffness during maximum Ca(2+)-activation expressed as percentage maximum force per nm per half sarcomere was higher by a factor of 3.5 in short-sarcomere fibres than in long-sarcomere fibres suggesting that the compliance of the filaments in the long-sarcomere fibres is considerably higher than in the short-sarcomere fibres. Sr2+ could not activate the contractile apparatus to the same level as that seen by Ca2+ in either fibre type: the maximum Sr(2+)-activated force was (20 +/- 3%) and (63 +/- 3%) of the maximum Ca(2+)-activated force response in short- and long-sarcomere fibres, respectively.(ABSTRACT TRUNCATED AT 400 WORDS)

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Year:  1992        PMID: 1491074     DOI: 10.1007/bf01738256

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  43 in total

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Journal:  Proc R Soc Lond B Biol Sci       Date:  1964-10-27

2.  Perfusion cuvette for the simultaneous measurement of mechanical, optical and energetic parameters of skinned muscle fibres.

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Journal:  Pflugers Arch       Date:  1986-11       Impact factor: 3.657

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Journal:  J Biol Chem       Date:  1973-02-10       Impact factor: 5.157

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Journal:  J Exp Zool       Date:  1969-05

5.  The relation between stiffness and filament overlap in stimulated frog muscle fibres.

Authors:  L E Ford; A F Huxley; R M Simmons
Journal:  J Physiol       Date:  1981-02       Impact factor: 5.182

6.  Potassium contractures in single muscle fibres of the crayfish.

Authors:  J Zachar; D Zacharová
Journal:  J Physiol       Date:  1966-10       Impact factor: 5.182

7.  Giant Muscle Fibers in a Barnacle, Balanus nubilus Darwin.

Authors:  G Hoyle; T Smyth
Journal:  Science       Date:  1963-01-04       Impact factor: 47.728

8.  Dissociation of force from myofibrillar MgATPase and stiffness at short sarcomere lengths in rat and toad skeletal muscle.

Authors:  D G Stephenson; A W Stewart; G J Wilson
Journal:  J Physiol       Date:  1989-03       Impact factor: 5.182

9.  Thermal dependence of maximum Ca2+-activated force in skinned muscle fibres of the toad Bufo marinus acclimated at different temperatures.

Authors:  B B Rees; D G Stephenson
Journal:  J Exp Biol       Date:  1987-05       Impact factor: 3.312

10.  The fine structure of fast and slow crustacean muscles.

Authors:  W H Fahrenbach
Journal:  J Cell Biol       Date:  1967-10       Impact factor: 10.539

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  13 in total

1.  Shortening properties of two biochemically defined muscle fibre types of the Norway lobster Nephrops norvegicus L.

Authors:  J M Holmes; K Hilber; S Galler; D M Neil
Journal:  J Muscle Res Cell Motil       Date:  1999-04       Impact factor: 2.698

2.  Differential effects of arginine, glutamate and phosphoarginine on Ca(2+)-activation properties of muscle fibres from crayfish and rat.

Authors:  David W Jame; Jan M West; Philip C Dooley; D George Stephenson
Journal:  J Muscle Res Cell Motil       Date:  2005-02-09       Impact factor: 2.698

Review 3.  Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.

Authors:  Scott L Hooper; Kevin H Hobbs; Jeffrey B Thuma
Journal:  Prog Neurobiol       Date:  2008-06-20       Impact factor: 11.685

4.  Effects of myofibrillar bundle diameter on the unloaded shortening velocity of skinned skeletal muscle fibres.

Authors:  K Hilber; S Galler
Journal:  J Muscle Res Cell Motil       Date:  1998-02       Impact factor: 2.698

5.  Characterization of ultrastructural and contractile activation properties of crustacean (Cherax destructor) muscle fibres during claw regeneration and moulting.

Authors:  J M West; D C Humphris; D G Stephenson
Journal:  J Muscle Res Cell Motil       Date:  1995-06       Impact factor: 2.698

6.  Effect of tibial bone resection on the development of fast- and slow-twitch skeletal muscles in foetal sheep.

Authors:  J M West; N A Williams; A R Luff; D W Walker
Journal:  J Muscle Res Cell Motil       Date:  2000-04       Impact factor: 2.698

7.  Ca2+- and Sr2+-activation properties of muscle fibres from a muscle receptor organ and the associated extrafusal muscle of the crab and crayfish.

Authors:  A L Parkinson; A J Bakker; S I Head
Journal:  J Muscle Res Cell Motil       Date:  2000       Impact factor: 2.698

8.  Calcium-activated and stretch-induced force responses in two biochemically defined muscle fibre types of the Norway lobster.

Authors:  S Galler; D M Neil
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

9.  Effects of glycine and proline on the calcium activation properties of skinned muscle fibre segments from crayfish and rat.

Authors:  E L Powney; J M West; D G Stephenson; P C Dooley
Journal:  J Muscle Res Cell Motil       Date:  2003       Impact factor: 2.698

10.  Activation of skinned muscle fibres from the Norway lobster Nephrops norvegicus L. by manganese ions.

Authors:  J M Holmes; K Hilber; S Galler; D M Neil
Journal:  J Muscle Res Cell Motil       Date:  1998-06       Impact factor: 2.698

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