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Articles in PresS, published online ahead of print January 16, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00554.2001
Submitted on November 18, 2001
Accepted on December 31, 1969
1 Pharmacology/Therapeutics, University of British Columbia, Vancouver, BC, Canada; McDonald Research Laboratories /The iCAPTURE Centre, University of British Columbia, Vancouver, BC, Canada
2 Krannert Institute of Cardiology, Indiana University, Indianapolis, IN, USA
3 Anatomy, University of British Columbia, Vancouver, BC, Canada; McDonald Research Laboratories /The iCAPTURE Centre, University of British Columbia, Vancouver, BC, Canada
4 Pathology/Lab Medicine, University of British Columbia, Vancouver, BC, Canada; Pharmacology/Therapeutics, University of British Columbia, Vancouver, BC, Canada; McDonald Research Laboratories /The iCAPTURE Centre, University of British Columbia, Vancouver, BC, Canada
* To whom correspondence should be addressed. E-mail: cseow{at}interchange.ubc.ca.
Phosphorylation of the 20-kD regulatory myosin light chain (MLC) of smooth muscle is known to cause monomeric myosins in solution to self-assemble into thick filaments. The role of MLC phosphorylation in thick filament formation in intact muscle however is not clear. It is not known whether the phosphorylation is necessary to initiate thick filament assembly in vivo. Here we show, by using a potent inhibitor of MLC kinase (wortmannin), that the MLC phosphorylation and isometric force in trachealis could be abolished without affecting calcium transients. By measuring cross-sectional densities of the thick filaments electron microscopically, we also show that inhibition of MLC phosphorylation alone did not cause disassembly of the filaments. The unphosphorylated thick filaments, however, partially dissolved when the muscle was subjected to oscillatory strains (which caused a 25% decrease in the thick filament density). The post-oscillation filament density recovered to the pre-oscillation level only when wortmannin was removed and the muscle stimulated. The data suggest that in vivo thick filament reassembly following mechanical perturbation is facilitated by the cyclic MLC phosphorylation associated with repeated stimulation.
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