Abstract
Smooth muscles have traditionally been classified as phasic or tonic, the tonic muscles being those which maintain a steady tension indefinitely with a low consumption of energy. Until ten years ago it was considered that the differences between smooth muscle types reflected different innervation or excitation-contraction coupling. However, recent work makes it clear that the contractile apparatus itself is adapted in tonic muscles.
References
Brenner, B. (1987) Mechanical and structural approaches to correlation of crossbridge action in muscle with actomyosin ATPase in solution.Ann. Rev. Physiol. 49, 655–72.
Chattergee, M. &Murphy, R. A. (1983) Ca2+-dependent tension maintenance without myosin phosphorylation in ‘skinned’ smooth muscle.Science 221, 464–6.
Cross, R. A. (1988) Smooth muscle contraction. What is 10-S myosin for?J. Musc. Res. Cell Motility 9, 108–10.
Dantzig, J. A., Walker, J. W., Trentham, D. R. &Goldman, Y. E. (1988) Relaxation of muscle fibres with ATP γ-S and by laser photolysis of caged ATP γ-S: evidence for Ca2+-dependent affinity of rapidly detaching zero-force crossbridges.Proc. natn. Acad. Sci. U.S.A. 85, 6716–20.
Driska, S. P. &Hartshorne, D. J. (1975) The contractile properties of smooth muscle. Properties and components of a calcium-sensitive actomyosin from chicken gizzard.Arch. Biochem. Biophys. 167, 203–12.
Guth, K. &Junge, J. (1982) Low Ca2+ impedes crossbridge detachment in chemically skinned taenia coli.Nature 300, 775–6.
Hai, C. M. &Murphy, R. M. (1988a) Crossbridge phosphorylation and regulation of latch state in smooth muscles.Am. J. Physiol. 255, C99–106.
Hai, C. M. &Murphy, R. A. (1988b) Regulation of shortening velocity by crossbridge phosphorylation in smooth muscle.Am. J. Physiol. 255, C86–94.
Hartshorne, D. J. &Gorecka, A. (1981) Biochemistry of the contractile proteins of smooth muscle. InHandbook of Physiology, Section 2,The Cardiovascular system, Vol. II, Vascular smooth muscle (edited byBohr, D. F., Somlyo, A. P. &Sparks, H. V.) pp. 93–120. Bethesda, Maryland: Am Physiol Soc.
Hemric, M. E. &Chalovich, J. M. (1988) Effect of caldesmon on the ATPase activity and binding of smooth and skeletal myosin subfragments to actin.J. biol. Chem. 263, 1878–85.
Hoar, P. E., Pato, M. D. &Kerrick, W. G. (1985) Myosin light chain phosphatase — effect on the activation and relaxation of gizzard smooth muscle skinned fibres.J. biol. Chem. 260, 8760–4.
Horiuchi, K. Y., Miyata, H. &Chacko, S. (1986) Modulation of smooth muscle actomyosin ATPase by thin filament associated proteins.Biochem. Biophys. Res. Commun. 136, 962–8.
Ikebe, M. &Reardon, S. (1988) Binding of caldesmon to smooth muscle myosin.J. biol. Chem. 263, 3055–8.
Imai, M., Dunn, L., Lee, R., Cook, R., May, G. &Bryan, J. (1988) Molecular cloning of caldesmon cDNAJ. Cell Biol. 107, 681a.
Ishii, N., Simpson, A. W. M. &Ashley, C. C. (1988) Intracellular free calcium ([Ca2+]i) and the ‘catch’ contraction in isolated molluscan smooth-muscle (ABRM) cells.J. Musc. Res. Cell Motility 9, 463.
Kamm, K. E. &Stull, J. T. (1985) The function of myosin light chain kinase phosphorylation in smooth muscle.Ann. Rev. Pharmac. 25, 593–620.
Lash, J. A., Sellers, J. R. &Hathaway, D. R. (1986) The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin.J. biol. Chem. 261, 16155–60.
Marston, S. B. (1982) The regulation of smooth muscle contractile proteins.Progr. Biophys. molec. Biol. 41, 1–41.
Marston, S. B. (1988) Aorta caldesmon inhibits actin activation of thiophosphorylated heavy meromyosin MgATPase activity by slowing the rate of product release.FEBS Lett. 238, 147–51.
Marston, S. B. (1989) A tight binding interaction between smooth muscle native thin filaments and heavy meromyosin in the presence of MgATP.J. biol. Chem. (submitted).
Marston, S. B., Pritchard, K., Redwood, C. &Taggart, M. (1988a) Ca2+ regulation of the thin filaments: biochemical mechanism and physiological role.Trans. Biochem. Soc. 16, 494–7.
Marston, S. B., Redwood, C. S. &Lehman, W. (1988b) Reversal of caldesmon function by anti-caldesmon antibodies confirms its role in the calcium regulation of vascular smooth muscle thin filaments.Biochem. Biophys. Res. Commun. 155, 197–203.
Marston, S. B. &Smith, C. W. J. (1984) Purification and properties of Ca2+-regulated thin filaments and F-actin from sheep aorta smooth muscle.J. Musc. Res. Cell Motility 5, 559–75.
Marston, S. B., Trevett, R. M. &Walters, M. (1980) Calcium ion regulated thin filaments from vascular smooth muscle.Biochem. J. 185, 355–65.
Moreland, S., Moreland, R. S. &Singer, H. A. (1986) Apparent dissociation between myosin light chain phosphorylation and maximal velocity of shortening in KCl depolarised swine carotid artery: Effect of temperature and KC1 concentration.Pflügers Arch. ges. Physiol. 408, 139–45.
Morgan, J. P. &Morgan, K. G. (1984) Stimulus specific patterns of intracellular calcium levels in smooth muscle of ferret portal vein.J. Physiol., Lond. 351, 155–67.
Morgan, K. G., Brozovich, F. V. &Jiang, M. J. (1988) Measurements of intracellular calcium concentration in mammalian vascular muscle cells during agonist induced contractions.Trans. Biochem. Soc. 16, 493.
Ngai, P. K. &Walsh, M. P. (1987) The effects of phosphorylation on smooth muscle caldesmon.Biochem. J. 244, 417–25.
Park, S. &Rasmussen, H. (1986) Carbachol-induced protein phosphorylation changes in bovine tracheal smooth muscle.J. biol. Chem. 261, 15731–9.
Pfitzer, G., Takai, A. &Ruegg, J. C. (1989) The coupling between myosin phosphorylation and contraction in smooth muscle.J. Musc. Res. Cell Motility 10, 166.
Pritchard, K. P. &Marston, S. B. (1989) Ca2+-Calmodulin binding to caldesmon and the caldesmonactin-tropomyosin complex. Its role in Ca2+ regulation of the activity of synthetic smooth muscle thin filaments.Biochem. J. 257 (in press).
Rasmussen, H., Takuwa, Y. &Park, S. (1987) Protein kinase C in the regulation of smooth muscle contraction.FASEB J. 1, 177–85.
Rembold, C. M. &Murphy, R. A. (1988) Myoplasmic [Ca2+] determines myosin phosphorylation in agonist-stimulated swine arterial muscle.Circ. Res. 63, 593–603.
Ruegg, J. C. (1971) Smooth muscle tone.Physiol. Rev. 51, 201–48.
Sellers, J. R., Eisenberg, E. &Adelstein, R. S. (1982) The binding of smooth muscle heavy meromyosin to actin in the presence of ATP.J. biol. Chem. 257, 13880–2.
Small, J. V., Furst, D. O. &Demey, J. (1986) Localisation of filamin in smooth muscle.J. cell. Biol. 102, 210–20.
Smith, C. W. J., Pritchard, K. &Marston, S. (1987) The mechanism of Ca2+ regulation of vascular smooth muscle thin filaments by caldesmon and calmodulin.J. biol. Chem. 262, 116–22.
Sobieszek, A. &Bremel, R. D. (1975) Preparation and properties of vertebrate smooth muscle myofibrils and actomyosin.Eur. J. Biochem. 55, 49–60.
Sobue, K., Morimoto, K., Inui, M., Kanda, K. &Kakiuchi, S. (1982) Control of actin-myosin interaction of gizzard smooth muscle by calmodulin and caldesmon linked flip-flop mechanism.Biomed. Res. 3, 188–96.
Sutherland, C. &Walsh, M. P. (1989) Phosphorylation of caldesmon prevents its interaction with smooth muscle myosin.J. biol. Chem. (in press).
Taggart, M. J. &Marston, S. B. (1988) the effects of vascular smooth muscle caldesmon on force production of ‘desensitised’ skeletal muscle fibres.FEBS Lett. 242, 171–4.
Ueki, N., Sobue, K., Kanda, T. &Higashino, K. (1987) Expression of high and low molecular weight caldesmons during phenotypic modulation of smooth muscle cells.Proc. natn. Acad. Sci. U.S.A. 84, 9049–53.
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Marston, S.B. What is latch? New ideas about tonic contraction in smooth muscle. J Muscle Res Cell Motil 10, 97–100 (1989). https://doi.org/10.1007/BF01739965
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DOI: https://doi.org/10.1007/BF01739965