Skeletal muscle can bear a high load at constant length, or shorten rapidly when the load is low. This force-velocity relationship is the primary determinant of muscle performance in vivo. Here we exploited the quasi-crystalline order of myosin II motors in muscle filaments to determine the molecular basis of this relationship by X-ray interference and mechanical measurements on intact single cells. We found that, during muscle shortening at a wide range of velocities, individual myosin motors maintain a force of about 6 pN while pulling an actin filament through a 6 nm stroke, then quickly detach when the motor reaches a critical conformation. Thus we show that the force-velocity relationship is primarily a result of a reduction in the number of motors attached to actin in each filament in proportion to the filament load. These results explain muscle performance and efficiency in terms of the molecular mechanism of the myosin motor.

Skeletal muscle performance determined by modulation of number of myosin motors rather than motor force or stroke size / G. PIAZZESI; M. RECONDITI; M. LINARI; L. LUCII; P. BIANCO; E. BRUNELLO; V. DECOSTRE; A. STEWART; D.G. GORE; T.C. IRVING; M. IRVING; V. LOMBARDI. - In: CELL. - ISSN 0092-8674. - STAMPA. - 131:(2007), pp. 784-795. [10.1016/j.cell.2007.09.045]

Skeletal muscle performance determined by modulation of number of myosin motors rather than motor force or stroke size

PIAZZESI, GABRIELLA;RECONDITI, MASSIMO;LINARI, MARCO;BIANCO, PASQUALE;BRUNELLO, ELISABETTA;LOMBARDI, VINCENZO
2007

Abstract

Skeletal muscle can bear a high load at constant length, or shorten rapidly when the load is low. This force-velocity relationship is the primary determinant of muscle performance in vivo. Here we exploited the quasi-crystalline order of myosin II motors in muscle filaments to determine the molecular basis of this relationship by X-ray interference and mechanical measurements on intact single cells. We found that, during muscle shortening at a wide range of velocities, individual myosin motors maintain a force of about 6 pN while pulling an actin filament through a 6 nm stroke, then quickly detach when the motor reaches a critical conformation. Thus we show that the force-velocity relationship is primarily a result of a reduction in the number of motors attached to actin in each filament in proportion to the filament load. These results explain muscle performance and efficiency in terms of the molecular mechanism of the myosin motor.
2007
131
784
795
G. PIAZZESI; M. RECONDITI; M. LINARI; L. LUCII; P. BIANCO; E. BRUNELLO; V. DECOSTRE; A. STEWART; D.G. GORE; T.C. IRVING; M. IRVING; V. LOMBARDI
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/255564
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