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This Article Full Text Full Text (PDF) All Versions of this Article: 287/3/C723    most recent 00029.2004v1 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 ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (8) Citing Articles via Google Scholar Google Scholar Articles by Babu, G. J. Articles by Periasamy, M. Search for Related Content PubMed PubMed Citation Articles by Babu, G. J. Articles by Periasamy, M.

VASCULAR BIOLOGY

Isoform switching from SM-B to SM-A myosin results in decreased contractility and altered expression of thin filament regulatory proteins

¹Department of Physiology and Cell Biology, College of Medicine and Public Health, Ohio State University, Columbus 43210; ²Department of Molecular and Cellular Physiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267; and ³Department of Pharmacology and ⁴Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont 05405

Submitted 16 January 2004 ; accepted in final form 7 May 2004

We previously generated an isoform-specific gene knockout mouse in which SM-B myosin is permanently replaced by SM-A myosin. In this study, we examined the effects of SM-B myosin loss on the contractile properties of vascular smooth muscle, specifically peripheral mesenteric vessels and aorta. The absence of SM-B myosin leads to decreased velocity of shortening and increased isometric force generation in mesenteric vessels. Surprisingly, the same changes occur in aorta, which contains little or no SM-B myosin in wild-type animals. Calponin and activated mitogen-activated protein kinase expression is increased and caldesmon expression is decreased in aorta, as well as in bladder. Light chain-17b isoform (LC_17b) expression is increased in aorta. These results suggest that the presence or absence of SM-B myosin is a critical determinant of smooth muscle contraction and that its loss leads to additional changes in thin filament regulatory proteins.

aorta; mesenteric vessels; calponin; caldesmon

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