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Published 13 October 2003. doi:10.1083/jcb.200303194
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© The Rockefeller University Press, 0021-9525/2003/10/119 $8.00
The Journal of Cell Biology, Volume 163, Number 1, 119-129

Article

Skeletal myosin heavy chain function in cultured lung myofibroblasts



Nancy A. Rice and Leslie A. Leinwand

Department of Molecular, Cellular, and Developmental Biology, University of Colorado at Boulder, Boulder, CO 80309

Address correspondence to Leslie A. Leinwand, Department of Molecular, Cellular, and Developmental Biology, UCB 347, University of Colorado at Boulder, Boulder, CO 80309. Tel.: (303) 492-7606. Fax: (303) 492-8907. email: Leslie.Leinwand{at}colorado.edu

Myofibroblasts are unique contractile cells with both muscle and nonmuscle properties. Typically myofibroblasts are identified by the expression of {alpha} smooth muscle actin (ASMA); however some myofibroblasts also express sarcomeric proteins. In this study, we show that pulmonary myofibroblasts express three of the eight known sarcomeric myosin heavy chains (MyHCs) (IIa, IId, and embryonic) and that skeletal muscle myosin enzymatic activity is required for pulmonary myofibroblast contractility. Furthermore, inhibition of skeletal myosin activity and myofibroblast contraction results in a decrease in both ASMA and skeletal MyHC promoter activity and ASMA protein expression, suggesting a potential coupling of skeletal myosin activity and ASMA expression in myofibroblast differentiation. To understand the molecular mechanisms whereby skeletal muscle genes are regulated in myofibroblasts, we have found that members of the myogenic regulatory factor family of transcription factors and Ca2+-regulated pathways are involved in skeletal MyHC promoter activity. Interestingly, the regulation of skeletal myosin expression in myofibroblasts is distinct from that observed in muscle cells and suggests that cell context is important in its control.

Key Words: myofibroblast; skeletal myosin; actin; contraction; lung

The online version of this paper contains supplementary material.

N.A. Rice's present address is Department of Biology, Western Kentucky University, 1 Big Red Way, Bowling Green, KY 42101.

Abbreviations used in this paper: ASMA, {alpha} smooth muscle actin; BDM, 2,3-butanedione monoxime; BTS, N-benzyl-p-toluene sulfonamide; ca, constitutively active; CaM, calmodulin; CMV, cytomegalovirus; cn, constitutively nuclear; CsA, cyclosporin A; MEF2, myocyte enhancer factor 2; MRF, myogenic regulatory factor; MyHC, myosin heavy chain; NFAT, nuclear factor of activated T cells; VIC, valvular interstitial cell.


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