Myosin cross-bridge kinetics and the mechanism of catch.

Abstract:

:Catch force in molluscan smooth muscle requires little, if any, energy input and is controlled by the phosphorylation state of the thick filament-associated mini-titin, twitchin. The kinetic parameters of myosin cross-bridge turnover in permeabilized catch muscle, and how they are potentially modified by the catch mechanism, were determined by single turnover measurements on myosin-bound ADP. Under isometric conditions, there are fast and slow components of cross-bridge turnover that probably result from kinetic separation of calcium-bound and calcium-free cross-bridge pools. The structure responsible for catch force maintenance at intermediate [Ca+2] does not alter the processes responsible for the fast and slow components under isometric conditions. Also, there is no measurable turnover of myosin-bound ADP during relaxation of catch force by phosphorylation of twitchin at pCa > 8. The only effects of the catch link on myosin-bound ADP turnover are 1), a small, very slow extra turnover when catch force is maintained at very low [Ca+2] (pCa > 8); and 2), attenuation of the shortening-induced increase in turnover at subsaturating [Ca(+2)]. These limited interactions between the catch link and myosin cross-bridge turnover are consistent with the idea that catch force is maintained by a thick and thin filament linkage other than the myosin cross-bridge.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Franke AS,Mooers SU,Narayan SR,Siegman MJ,Butler TM

doi

10.1529/biophysj.107.105577

subject

Has Abstract

pub_date

2007-07-15 00:00:00

pages

554-65

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(07)71307-3

journal_volume

93

pub_type

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