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Am J Physiol Lung Cell Mol Physiol 281: L631-L638, 2001;
1040-0605/01 $5.00
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Vol. 281, Issue 3, L631-L638, September 2001

Calcium sensitization produced by G protein activation in airway smooth muscle

Hayashi Yoshimura, Keith A. Jones, William J. Perkins, Tetsuya Kai, and David O. Warner

Department of Anesthesiology, Mayo Clinic and Mayo Foundation, Rochester, Minnesota 55905

We determined whether activation of G proteins can affect the force developed for a given intracellular Ca2+ concentration ([Ca2+]; i.e., the Ca2+ sensitivity) by mechanisms in addition to changes in regulatory myosin light chain (rMLC) phosphorylation. Responses in alpha -toxin-permeabilized canine tracheal smooth muscle were determined with Ca2+ alone or in the presence of ACh, endothelin-1 (ET-1), or aluminum fluoride (AlF<UP><SUB>4</SUB><SUP>−</SUP></UP>; acute or 1-h exposure). Acute exposure to each compound increased Ca2+ sensitivity without changing the response to high [Ca2+] (maximal force). However, chronic exposure to AlF<UP><SUB>4</SUB><SUP>−</SUP></UP>, but not to chronic ACh or ET-1, increased maximal force by increasing the force produced for a given rMLC phosphorylation. Studies employing thiophosphorylation of rMLC showed that the increase in force produced by chronic AlF<UP><SUB>4</SUB><SUP>−</SUP></UP> exposure required Ca2+ during activation to be manifest. Unlike the acute response to receptor agonists, which is mediated solely by increases in rMLC phosphorylation, chronic direct activation of G proteins further increases Ca2+ sensitivity in airways by additional mechanisms that are independent of rMLC phosphorylation.

regulatory myosin light chain phosphorylation; aluminum fluoride; remodeling; airway inflammation


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