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1 Department of Pathology and Laboratory Medicine, The James Hogg iCAPTURE Centre for Cardiovascular and Pulmonary Research, St. Paul's Hospital, University of British Columbia, Vancouver, BC, Canada
* To whom correspondence should be addressed. E-mail: cseow{at}mrl.ubc.ca.
Actin polymerization as part of the normal smooth muscle response to various stimuli has been reported. The actin dynamics is believed to be necessary for cytoskeletal remodeling in smooth muscle in its adaptation to external stress and strain, and maintenance of optimal contractility. We have shown in our previous studies in airway smooth muscle that myosins polymerized in response to contractile activation as well as to adaptation at longer cell lengths. We postulated that the same response could be elicited from actins under the same conditions. In the present study, actin filament formation was quantified electronmicroscopically in cell cross-sections. The nanometer-resolution allowed us to examine regional distribution of the filaments in a cell cross-section. Airway smooth muscle bundles were fixed in the relaxed and activated states at two lengths; the muscle preparations were also fixed after a period of oscillatory strain, a condition known to cause depolymerization of myosin filaments. The results indicate that contractile activation and increased cell length non-synergistically enhanced actin polymerization; the extent of actin polymerization was substantially less than that of myosin polymerization. Oscillatory strain increased thin filament formation. Although thin filament density was found higher in cytoplasmic areas near dense bodies, contractile activation did not preferentially enhanced actin polymerization in these areas. It is concluded that actin thin filaments are dynamic structures whose length and number are regulated by the cell in response to changes in extracellular environment and that polymerization/depolymerization of the thin filaments occurs uniformly across the whole cell cross-section.
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