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1 Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, IN, USA
* To whom correspondence should be addressed. E-mail: sgunst{at}iupui.edu.
Contractile stimulation has been shown to initiate actin polymerization in smooth muscle tissues, and this actin polymerization is required for active tension development. We evaluated whether N-WASp (Neuronal Wiskott-Aldrich Syndrome Protein)-mediated activation of the Arp 2/3 (Actin-Related Protein) complex regulates actin polymerization and tension development initiated by muscarinic stimulation in canine tracheal smooth muscle tissues. In vitro, the carboxy-terminal CA domain of N-WASp acts as an inhibitor of N-WASp-mediated actin polymerization; whereas the carboxy-terminal VCA domain of N-WASp is constitutively active and is sufficient by itself to catalyze actin polymerization. Plasmids encoding EGFP-tagged wild type N-WASp, the N-WASp VCA and CA domains, or EGFP alone were introduced into tracheal smooth muscle tissues by reversible permeabilization, and the tissues were incubated for 2 days to allow for expression of the proteins. Expression of the N-WASp CA domain inhibited actin polymerization and tension development in response to ACh, whereas expression of wild type N-WASp, the N-WASp VCA domain, or EGFP did not. The increase in myosin light chain (MLC) phosphorylation in response to contractile stimulation was not affected by expression of either the CA or VCA domains of N-WASp. Stimulation of the tissues with ACh increased the association of the Arp2/3 complex with N-WASp and this was inhibited by expression of the CA domain. The results demonstrate that N-WASP-mediated activation of the Arp2/3 complex is necessary for actin polymerization and tension development in response to muscarinic stimulation in tracheal smooth muscle tissues, and that these effects are independent of the regulation of MLC phosphorylation.
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