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PMID: 2529371 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Journal of physiology ·Vol. 410 ·1989-03-00 ·Pages 351-66

Stephenson DG, Stewart AW, Wilson GJ

Abstract

1. Single fast-twitch fibres from the extensor digitorum longus muscle of the rat, Rattus norvegicus, and single twitch fibres from the iliofibularis muscle of the cane toad, Bufo marinus, were mechanically skinned and then used to measure maximally Ca2+-activated [( Ca2+] greater than 0.03 mmol l-1) isometric force production, myofibrillar MgATPase activity and fibre stiffness at different sarcomere lengths. MgATP hydrolysis was linked by an enzyme cascade to the oxidation of NADH (nicotinamide adenine dinucleotide, reduced form) and was monitored by a microfluorimetric system. Fibre stiffness was measured from the amplitude of force oscillations generated by small sinusoidal length changes. 2. At sarcomere lengths which were optimal for isometric force production (around 2.7 microns for rat and 2.2 microns for toad fibres) the myofibrillar MgATPase activity (mean +/- S.E.M.) at 21-22 degrees C was found to be 3.80 +/- 0.53 molecules MgATP hydrolysed s-1 per myosin head for eight rat fibres and 6.35 +/- 0.77 s-1 per myosin head for four toad fibres. 3. At sarcomere lengths shorter than 2.7 microns in rat fibres and 2.2 microns in toad fibres, MgATPase and stiffness remained elevated and close to their respective values at 2.7 microns in rat fibres and 2.2 microns in toad fibres even when the isometric force decreased to near zero levels. 4. The dissociation at short sarcomere lengths of myofibrillar MgATPase activity and fibre stiffness from isometric force suggests that the cross-bridge cycle is not greatly affected by double actin filament overlap with the myosin filaments at short sarcomere lengths. Moreover, the results suggest that cross-bridges can be formed by myosin with actin filaments projecting from the nearest Z-line and from the Z-line in the other half of the sarcomere. 5. These results help to reconcile energetic and mechanical data obtained by others at short sarcomere lengths and can be explained within the framework of the sliding filament theory.

MeSH Terms
Adenosine Triphosphate/metabolism Animals Bufo marinus Ca(2+) Mg(2+)-ATPase/metabolism Calcium/pharmacology Isometric Contraction Muscle Contraction Myofibrils/enzymology NAD/metabolism Rats Sarcomeres/metabolism
Chemicals
NAD Adenosine Triphosphate Ca(2+) Mg(2+)-ATPase Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stephenson D G
Department of Zoology, La Trobe University, Bundoora, Melbourne, Victoria, Australia.
Stewart A W
Wilson G J
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Article Info
Journal
The Journal of physiology
Abbr.
J Physiol
ISSN
0022-3751
Published
1989-03-00
Pages
351-66
Language
English
Region
England
NLM ID
0266262
PMCID
PMC1190483
Subset
IM
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