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MgADP activation contributes to force enhancement during fast stretch of isolated skeletal myofibrils.

Abstract：

BACKGROUND:When an activated muscle is rapidly stretched, force rises and peaks while muscle lengthens. The peak force is normally called critical-force (Pc). The mechanism behind this increase in force is not well understood, but it has been associated with crossbridges operating in different states. METHODS:Myofibrils were attached between a cantilever and a micro-needle, and activated with Ca(2+) or MgADP. During activation, the myofibrils were stretched by 3% SLo at 10 SLo·s(-1). A crossbridge model was developed to better understand the effects of MgADP in myofibrils activation. RESULTS:Despite a similar stretch magnitude, MgADP activation produced a higher Pc (1.37 ± 0.07 P/Po) than Ca(2+) activation (Pc = 1.23 ± 0.03 P/Po). These results suggest that myofibrils activated with MgADP become stiffer than myofibrils activated with Ca(2+). CONCLUSIONS:MgADP induces a fraction of crossbridges to form a "rigor-like" state that precedes ADP release, and that may not contribute to isometric forces. Such interpretation was strengthened by the results obtained with the developed crossbridge model, which showed that MgADP bias crossbridges into the rigor-like state. This state would be crucial to initiate a cooperative activation of crossbridges and actin, and to resist to unbinding from actin when the myofibrils are stretched. SIGNIFICANCE:Our results suggest a new mechanism contributing for force output during stretch, which underlies basic mechanisms of muscle contraction.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Minozzo FC,Altman D,Rassier DE

doi

10.1016/j.bbrc.2015.06.070

subject

Has Abstract

pub_date

2015-08-07 00:00:00

pages

1129-34

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(15)30115-7

journal_volume

463

pub_type

杂志文章

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