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Am J Physiol Cell Physiol 280: C1645-C1656, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 6, C1645-C1656, June 2001

SPECIAL TOPIC
Leiomodin and tropomodulin in smooth muscle

Catharine A. Conley

Space Life Sciences, National Aeronautics and Space Administration Ames Research Center, Moffett Field, California 94035-1000

Evidence is accumulating to suggest that actin filament remodeling is critical for smooth muscle contraction, which implicates actin filament ends as important sites for regulation of contraction. Tropomodulin (Tmod) and smooth muscle leiomodin (SM-Lmod) have been found in many tissues containing smooth muscle by protein immunoblot and immunofluorescence microscopy. Both proteins cofractionate with tropomyosin in the Triton-insoluble cytoskeleton of rabbit stomach smooth muscle and are solubilized by high salt. SM-Lmod binds muscle tropomyosin, a biochemical activity characteristic of Tmod proteins. SM-Lmod staining is present along the length of actin filaments in rat intestinal smooth muscle, while Tmod stains in a punctate pattern distinct from that of actin filaments or the dense body marker alpha -actinin. After smooth muscle is hypercontracted by treatment with 10 mM Ca2+, both SM-Lmod and Tmod are found near alpha -actinin at the periphery of actin-rich contraction bands. These data suggest that SM-Lmod is a novel component of the smooth muscle actin cytoskeleton and, furthermore, that the pointed ends of actin filaments in smooth muscle may be capped by Tmod in localized clusters.

actin cytoskeleton; tropomyosin binding protein; contraction bands; human 64-kDa autoantigen D1


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