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This Article Full Text Full Text (PDF) All Versions of this Article: 296/5/C1024    most recent 00565.2008v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Liou, Y.-M. Articles by Ishiwata, S. Search for Related Content PubMed PubMed Citation Articles by Liou, Y.-M. Articles by Ishiwata, S.

MUSCLE CELL BIOLOGY AND CELL MOTILITY

Regulatory mechanism of smooth muscle contraction studied with gelsolin-treated strips of taenia caeci in guinea pig

¹Department of Life Sciences, National Chung-Hsing University, Taichung, Taiwan; ²Department of Physiology, Tokyo Medical University, Tokyo; ³Department of Anesthesiology, The Jikei University School of Medicine, Tokyo; and ⁴Department of Physics, Faculty of Science and Engineering, and ⁵Consolidated Research Institute for Advanced Science and Medical Care, Waseda University, Tokyo, Japan

Submitted 4 November 2008 ; accepted in final form 4 February 2009

The potential roles of the regulatory proteins actin, tropomyosin (Tm), and caldesmon (CaD), i.e., the components of the thin filament, in smooth muscle have been extensively studied in several types of smooth muscles. However, controversy remains on the putative physiological significance of these proteins. In this study, we intended to determine the functional roles of Tm and CaD in the regulation of smooth muscle contraction by using a reconstitution system of the thin filaments. At appropriate conditions, the thin (actin) filaments within skinned smooth muscle strips of taenia caeci in guinea pigs could be selectively removed by an actin-severing protein, gelsolin, without irreversible damage to the contractile apparatus, and then the thin filaments were reconstituted with purified components of thin filaments, i.e., actin, Tm, and CaD. We found that the structural remodeling of actin filaments or thin filaments was functionally linked to the Ca²⁺-induced force development and reduction in muscle cross-sectional area (CSA). That is, after the reconstitution of the gelsolin-treated skinned smooth muscle strips with pure actin, the Ca²⁺-dependent force development was partially restored, but the Ca²⁺-induced reduction in CSA occurred once. In contrast, the reconstitution with actin, followed by Tm and CaD, restored not only the force generation but also both its Ca²⁺ sensitivity and the reversible Ca²⁺-dependent reduction in CSA. We confirmed that both removal of the thin filaments by gelsolin treatment and reconstitution of the actin (thin) filaments with Tm and CaD caused no significant changes in the level of myosin regulatory light chain phosphorylation. We thus conclude that Tm and CaD are necessary for the full regulation of smooth muscle contraction in addition to the other regulatory systems, including the myosin-linked one.

confocal fluorescence microscopy; force development; reduction in muscle cross-sectional area; thin filament-linked regulation; phalloidin; phosphorylation of myosin regulatory light chain