Modulation of cellular morphology and locomotory activity by antibodies against myosin.
Open Access
- 1 December 1988
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 107 (6) , 2181-2189
- https://doi.org/10.1083/jcb.107.6.2181
Abstract
Three monoclonal antibodies directed against chicken brush border myosin were used to study the possible function of myosin in microfilament organization and locomotion of chicken fibroblasts. These antibodies bind to distinct and separate epitopes on the heavy chain of chicken nonmuscle myosin and display differential effects of myosin filament formation and actin-myosin interaction (Citi, S., and J. Kendrick-Jones. 1988. J. Musc. Res. Cell Motil. 9: 306-319). When injected into chicken fibroblasts, all antibodies induced breakdown of stress fibers. Concomitantly, a large proportion of the cells developed extensive lamellae which altered their morphology drastically. These cells showed also increased locomotory activity. All effects were concentration dependent and reversible. The most drastic alterations were observed with cells injected with antibody quantities exceeding the quantity of cellular myosin (molar ratios of antibody to myosin greater than 3:1). The finding that antibodies with different effects on myosin filament formation in vitro all induce similar intracellular processes suggests that it is the antibody-induced decrease in functional myosin that triggers an increase in plasma membrane dynamics and locomotory activity, rather than differences in myosin filament length or conformation.Keywords
This publication has 28 references indexed in Scilit:
- Antisense RNA Inactivation of Myosin Heavy Chain Gene Expression in Dictyostelium discoideumScience, 1987
- The molecular organization of myosin in stress fibers of cultured cells.The Journal of cell biology, 1986
- Purification from Dictyostelium discoideum of a low-molecular-weight myosin that resembles myosin I from Acanthamoeba castellanii.Journal of Biological Chemistry, 1985
- The 110,000-dalton actin- and calmodulin-binding protein from intestinal brush border is a myosin-like ATPase.Journal of Biological Chemistry, 1984
- Localization of actin and myosin for the study of ameboid movement in Dictyostelium using improved immunofluorescence.The Journal of cell biology, 1984
- Disruption of microfilament organization after injection of F-actin capping proteins into living tissue culture cellsNature, 1983
- DIFFERENTIAL RESPONSE OF 3 TYPES OF ACTIN FILAMENT BUNDLES TO DEPLETION OF CELLULAR ATP LEVELS1983
- Evidence that myosin does not contribute to force production in chromosome movement.The Journal of cell biology, 1982
- Stress fiber sarcomeres of fibroblasts are contractileCell, 1980
- Multiple forms of Acanthamoeba myosin I.Journal of Biological Chemistry, 1979