ISSN:
1432-1017
Keywords:
Actin-myosin interactions
;
Muscle mechanics
;
ATP hydrolysis in skeletal muscle
;
Rigor state of muscle
;
Cross-bridge slippage
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract A sudden stretch (within 0.3 ms) of glycerol-extracted rabbit psoas fibre bundle suspended in ATP-salt solution caused an immediate tension increase followed by a rapid tension decay (quick phase) which was nearly completed within 3 ms. The quick phase was missing or much reduced in the absence of ATP when the fibres were in rigor. Since the immediate stiffness of the fibres was nearly the same at the onset and at the end of the quick phase, the latter cannot be due to cross-bridges detachment per se. However, it may be ascribed to a conformational change (e.g. rotation) of attached bridges as suggested by Huxley and Simmons. Alternatively it might be explained by a slippage of attached cross-bridges. This mechanism would presuppose fast detachment and reattachment of strongly strained cross-bridges during the quick phase. Evidence for such a process was obtained by analysing the tension transients obtained when fibre bundles subjected to a large stretch were subsequently (within 10 ms) released to the initial length, as well as from stiffness measurements during the sudden length change: The stiffness was not found to be constant either during stretch or during the release. This may be taken to mean that the number of attached cross-bridges does not remain constant even during a rapid length change. In view of these results, the model proposed by Huxley and Simmons might be extended to take account of rapid attachment and detachment of crossbridges.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02426087
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