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1 Signal Transduction Group, Boston Biomedical Research Institute, Watertown 02472; and 2 Cardiovascular Division, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215
This minireview will cover current concepts on the identity and mechanistic function of smooth muscle actin binding proteins that may regulate actin-myosin interactions. The potential roles of tropomyosin, caldesmon, calponin, and SM22 will be discussed. The review, for purposes of brevity, will be nonexhaustive but will give an overview of available information on the in vitro biochemistry and potential in vivo function of these proteins. Preterm labor is discussed as a possible example of where thin filament regulation may be relevant. Considerable controversy surrounds the putative physiological significance of these proteins, and emphasis will be placed on the need for more experimental work to determine the degree to which tissue- and species-specific effects have clouded the interpretation of functional data.
caldesmon; calponin; tropomyosin; SM22; preterm labor
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Y. Li, H.-D. Je, S. Malek, and K. G. Morgan ERK1/2-mediated phosphorylation of myometrial caldesmon during pregnancy and labor Am J Physiol Regulatory Integrative Comp Physiol, January 1, 2003; 284(1): R192 - R199. [Abstract] [Full Text] [PDF]
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D. D Tang, M.-F. Wu, A. M Opazo Saez, and S. J Gunst The focal adhesion protein paxillin regulates contraction in canine tracheal smooth muscle J. Physiol., July 15, 2002; 542(2): 501 - 513. [Abstract] [Full Text] [PDF]
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P. A. Doevendans and G. van Eys Smooth muscle cells on the move: the battle for actin Cardiovasc Res, June 1, 2002; 54(3): 499 - 502. [Full Text] [PDF]
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