Abstract
At the biochemical level, agonist-induced force generation of airways and other smooth muscles can be divided into two components: a rapid increase in force which occurs seconds after the addition of a spasmogen followed by, or maybe partly coincident with, a slower, tonic, well maintained contracture. This chapter reviews how airways smooth muscle (ASM) generates force, the contractile proteins involved and their regulation by second and third messenger molecules. Current hypotheses regarding the biochemical basis of force maintenance in ASM is the subject of chapter 6 of this volume.
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References
Huxley AF, Niedergerke R. Structural changes in muscle during shortening. Nature 1954; 173: 971–973.
Huxley HE, Hanson J. Changes in the cross striations of muscle during contraction and stretch and their structural interpretation. Nature 1954 173: 973–976.
Periasamy A, Burns DH, Holdren DN, Pollack GH, Trombit, K. A-Band shortening in single fibres of frog skeletal muscle. Biophys J 1990; 57: 815–828.
Pease DC, Molinari S. Electron microscopy of muscular arteries; pial vessels of the cat and monkey. J Ultrastruct Res 1960; 3: 447–468.
Choi JK. The fine ultrastructure of the urinary bladder of the toad, Bufo marinus. J Cell Biol 1963; 16: 53–72.
Takano-Ohmuro H, Obinata T, Mikawa T, Masaki T. Changes in myosin isozymes during development of chicken gizzard muscle. J Biochem (Tokyo) 1983; 93: 903–908.
Pagani F, Faris R, Shemin R, Julian FJ. Evidence for smooth muscle myosin isozymes. Biophys J 1985; 47: 310a.
Mohammad MA, Sparrow MP. Changes in myosin heavy chain stoichiometry in pig tracheal smooth muscle during development. FEBS Letts 1988; 228: 109–112.
Rovner AS, Thompson MM, Murphy RA. Two different heavy chains are found in smooth muscle myosin. Am J Physiol 1986; 250: C861–C970.
Kawamoto S, Adelstein RS. Characterization of myosin heavy chains in cultured aorta smooth muscle cells. A comparative study. J Biol Chem 1987; 262: 7282–7288.
Borrioni AC, Zanellato AMC, Scannapieco G, Pauletto P, Sartore S. Myosin heavy chain isoforms in adult and developing rabbit vascular smooth muscle. Eur J Biochem 1989; 183: 413–417.
Mohammad MA, Sparrow MP. The distribution of heavy chain isoforms of myosin in airways smooth muscle from adult and neonate humans. Biochem J 1988; 260: 421–426.
Schildmeyer LA, Seidel CL. Quantitative and qualitative heterogeneity in smooth muscle myosin heavy chains. Life Sci 1989; 45: 1617–1625.
Sparrow MP, Arner A, Mohammad MA, Hellstrand P, Ruegg JC. Isoforms of myosin in smooth muscle. In: Siegman, M. (Ed), Regulation and Contraction of Smooth Muscle, Vol 245, Alan R. Liss Inc, 1987: 67–79.
Helper DJ, Lash JA, Hathaway DR. Distribution of isoelectric variants of the 17, 000-dalton myosin light chains in mammalian smooth muscle. J Biol Chem 1988; 263: 15748–15753.
Fatigati V, Murphy RA. Actin and tropomyosin variants in smooth muscles. Dependence on tissue type. J Biol Chem 1984; 259: 14383–14388.
Cohen DM, Murphy RA. Actin-myosin ratio differences in porcine smooth muscles. Fed Proc 1977; 36: 602.
Cummins P, Perry SV. Chemical and immunochemical characteristics of tropomyosins from striated and smooth muscles. Biochem J 1973; 141: 43–49.
Marston SB, Smith CWJ. The thin filaments of smooth muscles. J Muscle Res Cell Motility 1985; 6: 669–708.
Merkel L, Meisheri KD, Pfizer G. The variable relation between myosin light chain phosphorylation and actin-activated ATPase activity in chicken gizzard smooth muscle. Modulation by tropomyosin. FEBS Letts 1984; 138: 429–434.
Nag S, Seidel JC. Dependence on Ca2+ and tropomyosin of the actin-activated ATPase activity of phosphorylated gizzard myosin in the presence of low concentrations of Mg2+. J Biol Chem 1983; 258: 6444–6449.
Ebashi S. Regulation of muscle contraction. Proc R Soc Lond Ser B 1980; 207: 259–286.
Bremel RD. Myosin-linked calcium regulation in vertebrate smooth muscle. Nature 1974; 252: 405–407.
Seow CY, Stephens NL. Time-dependence of series elasticity in tracheal smooth muscle. J Appl Physiol 1987; 62: 1556–1561.
Chatterjee M, Murphy RA. Calcium-dependent stress maintenance without myosin phosphorylation in skinned smooth muscle. Science 1983; 221: 464–466.
Small JV, Sobieszek A. Ca regulation of smooth muscle actomyosin via a kinase-phosphatase-dependent phosphorylation and dephosphorylation of the 20,000-Mr light chain of myosin. Eur J Biochem 1977; 76: 521–530.
Sobieszek A, Small JV. Regulation of actin-myosin interaction in vertebrate smooth muscle: activation via a myosin-light-chain-kinase and the effect of tropomyosin. J Mol Biol 1977; 112: 559–576.
Aksoy MO, Williams D, Sharkey EM, Hartshorne DJ. A relationship between Ca2+ sensitivity and phosphorylation of gizzard actomyosin. Biochem Biophys Res Comm 1976; 69: 35–41.
Kamm KE, Leachman SA, Michnoff CH, Nunnally MH, Persechini A, Richardson AL, Stull JT. Myosin light chain kinases and kinetics of myosin phosphorylation in smooth muscle cells. In: Siegman M. Ed, Regulation and Contraction of Smooth Muscle, Vol 245, Alan R. Liss Inc, 1987: 183–193.
Felbel J, Trockur B, Ecker T, Landgraf W, Hofmann F. Regulation of cytosolic calcium by cAMP and cGMP in freshly isolated smooth muscle cells from bovine trachea. J Biol Chem 1988; 263: 16764–16771.
Fujiwara T, Sumimoto K, Itoh T, Suzuki H, Kuriyama H. Relaxing actions of procaterol, a β 2-adrenoceptor stimulant, on smooth muscle cells of the dog trachea. Br J Pharmacol 1988; 93: 199–209.
Kotlikoff MI, Murray RK, Reynolds EE. Histamine-induced calcium release and phorbol antagonism in cultured airway smooth muscle cells. Am J Physiol 1987; 253: C561–566.
Takuwa T, Takuwa N, Rasmussen H. The effect of isoproterenol on intracellular calcium concentration. J Biol Chem 1988; 263; 762–768.
Taylor DA, Stull JT. Calcium dependence of myosin light chain phosphorylation in smooth muscle cells. J Biol Chem 1988; 263: 14456–14462.
Taylor DA, Bowman BF, Stull JT. Cytoplasmic Ca2+ is a primary determinant for myosin phosphorylation in smooth muscle cells. J Biol Chem 1989; 264: 6207–6213.
Adelstein RS, Eisenberg E. Regulation and kinetics of the actin-myosin-ATP interaction. Ann Rev Biochem 1980; 49: 921–956.
Rasmussen H, Barratt PQ. Calcium messenger system: An integrated view. Physiol Rev 1984; 64: 938–984.
Manalan AS, Klee CB. Calmodulin. Adv Cyclic Nucl Protein Phosphorylation Res 1984; 18: 227–278.
Stull JT, Nunnally MH, Michnoff CH. Calmodulin-dependent protein kinases. In: Krebs, E.G. and Boyer, P.D Eds. The Enzymes. Academic Press, 1986: 113–166.
Persechini A, Kamm KE, Stull JT. Different phosphorylated forms of myosin in contracting tracheal smooth muscle. J Biol Chem 1986; 261: 6293–6299.
Kamm KE, Stull JT. Contractile mechanisms. Am Rev Resp Dis 1987; 136; S12–S14.
Colburn JC, Michnoff CH, Hsu L-C, Slaughter CA, Kamm KE, Stull JT. Sites phosphorylated in myosin light chain in contracting smooth muscle. J Biol Chem 1988; 263: 19166–19173.
de Lanerolle P, Condit JR, Tanenbaum M, Adelstein RS. Myosin phosphorylation, agonist concentration and contraction of tracheal smooth muscle. Nature 1982; 298: 871–872.
Silver PJ, Stull JT. Phosphorylation of myosin light chain and phosphorylase in tracheal smooth muscle is response to KC1 and carbachol. Mol Pharmacol 1984; 25: 267–274.
de Lanerolle P, Stull JT. Myosin phosphorylation during contraction and relaxation of tracheal smooth muscle. J Biol Chem 1980; 255: 9993–10000.
Ikebe M, Hartshorne DJ. Effects of Ca2+ on the conformation and enzymatic activity of smooth muscle myosin. J Biol Chem 1985; 260: 10027–10031.
Tanaka T, Sobue K, Owada MK, Hakura A. Linear relationship between diphosphorylation of 20 kDa light chain of gizzard myosin and the actin-activated myosin ATPase activity. Biochem Biophys Res Comm 1985; 131: 987–993.
Silver PJ, Stull JT. Regulation of mysoin light chain and phosphorylase phosphorylation in tracheal smooth muscle. J Biol Chem 1982; 257: 6145–6150.
Gerthoffer WT, Murphy RA. Myosin phosphorylation and regulation of cross-bridge cycle in tracheal smooth muscle. Am J Physiol 1983; 244: C182–C187.
Kamm KE, Stull JT. Myosin phosphorylation, force and maximal shortening velocity in neurally stimulated tracheal smooth muscle. Am J Physiol 1985; 249: C238–C247.
Stephens NL. Physical properties of contractile systems. In: Daniel EE, Paton, DM, Eds Methods in Pharmacology. Plenum Press; 1975: 265–296.
Kamm KE, Stull JT. Activation of smooth muscle contraction: Relation between myosin phosphorylation and stiffness. Science 1986; 232: 80–82.
Miller-Hance WC, Miller JR, Wells JN, Stull JT, Kamm KE. Biochemical events associated with activation of smooth muscle contraction. J Biol Chem 1988; 263: 13979–13982.
Kamm KE. Myosin light chain phosphorylation during phasic contractions of tracheal smooth muscle. Pflugers Arch 1987; 408: 474–478.
Giembycz MA, Rodger IW. Electrophysiological and other aspects of excitation-contraction coupling and uncoupling in mammalian airway smooth muscle. Life Sci 1987; 41: 111–132.
Itoh T, Ikebe M, Kargacin GJ, Hartshorne DJ, Kemp BE, Fay FS. Effects of modulators of myosin light chain kinase activity in single smooth muscle cells. Nature 1989; 338: 164–167.
Tansey MG, Word RA, Hidaka H, Singer HA, Schworer CM, Kamm KE, Stull JT. Phosphorylation of myosin light chain kinase by the multifunctional calmodulin-dependent protein kinase II in smooth muscle cells. J Biol Chem 1992; 267: 12511–12516.
Gilman AG. G-Proteins: transducers of receptor-generated signals. Ann Rev Physiol 1987; 56: 615–649.
Kitazawa T, Kobayashi S, Horiuti K, Somlyo AV, Somlyo AP. Receptor-coupled, permeabilized smooth muscle. Role of the phosphatidylinositol cascade, G-proteins, and modulation of the contractile response to Ca2+. J Biol Chem 1989; 264: 5339–5342.
Fujiwara T, Itoh T, Kubota Y, Kuriyama H. Effect of guanosine nucleotides on skinned smooth muscle tissue of the rabbit mesenteric artery. J Physiol 1989; 408: 535–547.
Kubota Y, Nomura M, Kamm KE, Murphy MC, Stull JT. GTPγ S-dependent regulation of smooth muscle contractile elements. Am J Physiol 1992; 262: C405—C410.
Chacko S, Conti MA, Adelstein R.S. The effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation. Proc Natl Acad Sci USA 1977; 74: 129–133.
Rees DD, Fredericksen DW. Calcium regulation of porcine aortic myosin. J Biol Chem 1981; 256: 357–364.
Chacko S, Rosenfeld A. Regulation of actin-activated ATP hydrolysis by arterial myosin. Proc Natl Acad Sci USA 1982; 79: 292–296.
Nag S, Seidel JC. Dependence on Ca2+ and tropomyosin of the actin-activated ATPase activity of phosphorylated gizzard myosin in the presence of low Mg2+. J Biol Chem 1983; 258: 6444–6449.
Kaminski EA, Chacko S. Effects of Ca2+ and Mg2+ on the actin-activated ATP hydrolysis by phosphorylated heavy meromyosin from arterial smooth muscle. J Biol Chem 1984; 259: 9104–9108.
Ebashi S, Mikawa T, Hirata M, Toyooka T, Nonomura Y. Regulatory proteins of smooth muscle. In: Casteels R, Godfraind T, Ruegg JC. Eds, Excitation-Contraction Coupling in Smooth Muscles, Elsevier, 1977: 325–334.
Ebashi S, Nonomura Y, Hirata M. Mode of calcium binding to smooth muscle contractile systems. In: Kakiuchi S, Hidaka H, Means A.R Eds, Calmodulin and Intracellular Calcium receptors, Plenum Press, 1982; 49–54.
Hirata M, Mikawa T, Nonomura V, Ebashi S. Ca2+-regulation-regulation in vascular smooth muscle. II. Ca2+ binding of aorta leiotonin. J Biochem (Tokyo) 1980; 78: 369–378.
Ebashi S, Nonomura Y, Nakamura S, Nakasone H, Kohama K. Regulatory mechanism in smooth muscle: actin-linked regulation. Fed Proc 1982; 41: 2863–2867.
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Giembycz, M.A. (1994). Current Concepts on Mechanisms of Force Generation in Airways Smooth Muscle. In: Raeburn, D., Giembycz, M.A. (eds) Airways Smooth Muscle: Biochemical Control of Contraction and Relaxation. Respiratory Pharmacology and Pharmacotherapy. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7681-0_3
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DOI: https://doi.org/10.1007/978-3-0348-7681-0_3
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