Skip to main content

Cellular Control Mechanisms in Airway Smooth Muscle

  • Chapter
Airway Smooth Muscle in Health and Disease

Abstract

The regulation of smooth muscle contraction is really an exercise in understanding the regulation of a number of protein phosphorylation/dephosphorylation reactions. By this I mean the enzyme-catalyzed transfer (by a class of enzymes known as protein kinases) of the terminal phosphate of ATP to a serine or threonine* residue on a protein with the formation of a covalent phosphoester linkage and, equally important, the enzyme-catalyzed dephosphorylation (by enzymes known as phosphoprotein phosphatases) of the phosphorylated proteins. This type of reversible phosphorylation is known to be important in regulating Cellular processes (reviewed by Krebs and Beavo, 1979). As we shall see, smooth muscles contain Ca2+ /calmodulin-dependent, cyclic nucleotide-dependent, and Ca2+ /phospholipid-dependent protein kinases and at least three different phosphatases. In many ways, the contractile properties of smooth muscles can be visualized as being determined by the balance between the activities of these kinases and phosphatases. Consequently, much of the research emphasis on smooth muscle regulation has been directed at understanding the properties of kinases and phosphatases purified from smooth muscles. These studies have proved important for two reasons. First, they have resulted in a greater understanding of the regulation of smooth muscle contraction. Second, they serve as an important model for studying the role of protein hosphorylation reaction in other biological systems.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Adelstein, R. S., and Conti, M. A., 1975, Phosphorylation of platelet myosin increases actinactivated myosin ATPase activity, Nature (Lond.) 256:597–598.

    CAS  Google Scholar 

  • Adelstein, R. S., Conti, M. A., Hathaway, D. R., and Klee, C. B., 1978, Phosphorylation of smooth muscle myosin light chain kinase by the catalytic subunit of adenosine 3:5-monophosphate-dependent protein kinase, J. Biol. Chem. 253:8347–8350.

    PubMed  CAS  Google Scholar 

  • Adelstein, R. S., and Eisenberg, E., 1980, Regulation and kinetics of the actinmyosin-ATP interaction, Annu. Rev. Biochem. 49:921–956.

    PubMed  CAS  Google Scholar 

  • Adelstein, R. S., and Klee, C. B., 1981, Purification and characterization of smooth muscle myosin light chain kinase, J. Biol. Chem. 256:7501–7509.

    PubMed  CAS  Google Scholar 

  • Aitken, A., Bilham, T., and Cohen, P., 1982, Complete primary structure of protein phosphatase inhibitor-1 from rabbit skeletal muscle, Eur. J. Biochem. 126:235–246.

    PubMed  CAS  Google Scholar 

  • Aitken, A., Klee, C. B., and Cohen, P., 1984, The structure of the B subunit of calcineurin, Eur. J. Biochem. 139:663–671.

    PubMed  CAS  Google Scholar 

  • Aksoy, M. O., Murphy, R. A., and Kamm, K. E., 1982, Role of Ca2+ and myosin light chain phosphorylation in regulation of smooth muscle, Am. J. Physiol. 242:C109–C116.

    PubMed  CAS  Google Scholar 

  • Aksoy, M. O., Mras, S., Kamm, K. E., and Murphy, R. A., 1983, Ca2+, cAMP, and changes in myosin phosphorylation during contraction of smooth muscle, Am. J. Physiol. 245:C255–C270.

    PubMed  CAS  Google Scholar 

  • Arner, A., and Hellstrand, P., 1985, Effects of calcium and substrate on force-velocity relation and energy turnover in skinned smooth muscle of the guinea pig, J. Physiol. (Lond.) 360:347–365.

    CAS  Google Scholar 

  • Barron, J. T., Barany, M., Barany, K., and Storti, R. V., 1980, Reversible phosphorylation and dephosphorylation of the 20,000 dalton light chain of myosin during the contraction-relaxation-contraction cycle of arterial smooth muscle, J. Biol. Chem. 255:6238–6244.

    PubMed  CAS  Google Scholar 

  • Bialojan, C, Merkel, L., Ruegg, J. C, Gifford, D., and D. Salvo, J., 1985, Prolonged relaxation of detergent-skinned smooth muscle involves decreased endogenous phosphatase activity, Am. J. Physiol. 178:648–652.

    CAS  Google Scholar 

  • Bretscher, A., 1986, Thin filament regulatory proteins of smooth and non-muscle Cells, Nature (Lond.) 321:726–727.

    CAS  Google Scholar 

  • Bretscher, A., and Lynch, W. J., 1985, Identification and localization of immunoreactive forms of caldesmon in smooth and nonmuscle Cells: A comparison with the distributions of tropomyosin and of a-actinin. J. Cell. Biol. 100:1656–1663.

    PubMed  CAS  Google Scholar 

  • Bulbring, E., and den Hertog, A., 1980, The action of isoprenaline on the smooth muscle of the guineapig taenia coli, J. Physiol. (Lond.) 304:277–296.

    CAS  Google Scholar 

  • Butler, T. M., Siegman, M. J., and Mooers, S. U., 1983, Chemical energy usage during shortening and work production in mammalian smooth muscle, Am. J. Physiol. 244:C234–C242.

    PubMed  CAS  Google Scholar 

  • Carlson, F. D., and Wilkie, D. R., 1974, Muscle Physiology, Prentice-Hall, Englewood Cliffs, New Jersey.

    Google Scholar 

  • Cassidy, P. S., Kerrick, W. G. L., Hoar, P. E., and Malencik, D. A., 1981, Exogenous calmodulin increases Ca2+ sensitivity of isometric tension, activation and myosin phosphorylation in skinned smooth muscle, Pflugers Arch. 392:115–120.

    PubMed  CAS  Google Scholar 

  • Chacko, S., and Rosenfeld, A., 1982, Regulation of actin-activated ATP hydrolysis by arterial myosin, Proc. Natl. Acad. Sci. USA 79:292–296.

    PubMed  CAS  Google Scholar 

  • Chacko, S., Conti, M. A., and Adelstein, R. S., 1977, Effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation, Proc. Natl. Acad. Sci. USA 74:129–133.

    PubMed  CAS  Google Scholar 

  • Chatterjee, M., and Murphy, R. A., 1983, Calcium-dependent stress maintenance without myosin phosphorylation in skinned smooth muscle, Science 221:464–466.

    PubMed  CAS  Google Scholar 

  • Cohen, P., 1985, The coordinated control of metabolic pathways by broad-specificity protein kinases and phosphatases, Current Topics Cell. Regul. 27:23–37.

    CAS  Google Scholar 

  • Conti, M. A., and Adelstein, R. S., 1981, The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3:5 cAMP-dependent protein kinase, J. Biol. Chem. 256:3178–3181.

    PubMed  CAS  Google Scholar 

  • Csabina, S., Barany, M., and Barany, K., 1986, Stretch-induced myosin light chain phosphorylation in rat uterus, Arch. Biochem. Biophys. 249:374–381.

    PubMed  CAS  Google Scholar 

  • Dabrowska, R., Aromatorio, D., Sherry, J. M. F., and Hartshorne, D. J., 1977, Composition of the myosin light chain kinase from chicken gizzard, Biochem. Biophys. Res. Commun. 78:1263–1272.

    PubMed  CAS  Google Scholar 

  • Dabrowska, R., Sherry, J. M. F., Aromatorio, D. K., and Hartshorne, D. J., 1978, Modulator protein as a component of myosin light chain kinase from chicken gizzard, Biochemistry 17:253–258.

    PubMed  CAS  Google Scholar 

  • de Lanerolle, P., 1979, Myosin Phosphorylation and the Contractile State of Tracheal Smooth Muscle, Ph.D. thesis, University of California, San Diego

    Google Scholar 

  • de Lanerolle, P., and Stull, J. T., 1980, Myosin phosphorylation during contraction and relaxation of tracheal smooth muscle, J. Biol. Chem. 255:9993–10000.

    PubMed  Google Scholar 

  • de Lanerolle, P., Condit, J. R., Jr., Tanenbaum, M., and Adelstein, R. S., 1982, Myosin phosphorylation, agonist concentration and contraction of tracheal smooth muscle, Nature (Lond.) 298:871–872.

    Google Scholar 

  • de Lanerolle, P., Nishikawa, M., Yost, D. A., and Adelstein, R. S., 1984, Increased phosphorylation of myosin light chain kinase after an increase in cyclic AMP in intact smooth muscle, Science 223:1415–1417.

    PubMed  Google Scholar 

  • Diamond, J., and Chu, E. B., 1983, Possible role for cyclic GMP in endothelium-dependent relaxation of rabbit aorta by acetylcholine. Comparison with nitroglycerin, Res. Commun. Chem. Pathol. Pharmacol. 41:369–381.

    PubMed  CAS  Google Scholar 

  • Dillon, P. F., Aksoy, M. O., Driska, S. P., and Murphy, R. A., 1981, Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle, Science 211:495–497.

    PubMed  CAS  Google Scholar 

  • Driska, S. P., Aksoy, M. O., and Murphy, R. A., 1981, Myosin light chain phosphorylation associated with contraction in arterial smooth muscle, Am. J. Physiol. 240:C222–C233.

    PubMed  CAS  Google Scholar 

  • Ebashi, S., 1980, The Croonian Lecture, 1979: Regulation of muscle contraction, Proc. R. Soc. Biol. B.207:259–286.

    CAS  Google Scholar 

  • Ebashi, S., and Endo, M., 1968, Calcium ion and muscle contraction, Prog. Biophys. Mol. Biol. 18:123–183.

    PubMed  CAS  Google Scholar 

  • Eisenberg, E., and Hill, T. L., 1985, Muscle contraction and free energy transduction in biological systems, Science 227:999–1006.

    PubMed  CAS  Google Scholar 

  • Endo, M., Kitazawa, T., Yagi, S., Lino, M., and Kakuta, Y., 1977, Some properties of chemically skinned smooth muscle fibers, in: Excitation-Contraction Coupling in Smooth Muscle (R. Casteels, T. Godfraind, J. C. Ruegg, eds.), pp. 199–209, Elsevier/North–Holland, Amsterdam.

    Google Scholar 

  • Flavahan, N. A., Aarhus, L. L., Rimele, T. J., and Vanhoutte, P. M., 1985, Respiratory epithelium inhibits bronchial smooth muscle tone, J. Appl. Physiol. 58:834–838.

    PubMed  CAS  Google Scholar 

  • Furchgott, R., 1983, Role of endothelium in responses of vascular smooth muscle, Circ. Res. 53:557–573.

    PubMed  CAS  Google Scholar 

  • Ganz, P., Davies, P. F., Leopold, J. A., Gimbrone, M. A., Jr., and Alexander, R. W., 1986, Short and long-term interactions of endothelium and vascular smooth muscle in coculture: Effects on cyclic GMP production, Proc. Natl. Acad. Sci. USA 83:3552–3556.

    PubMed  CAS  Google Scholar 

  • Gerthoffer, W. T., 1986, Calcium dependence of myosin phosphorylation and airway smooth muscle contraction and relaxation, Am. J. Physiol. 250:C597–C604.

    PubMed  CAS  Google Scholar 

  • Gerthoffer, W. T., and Murphy, R. S., 1983a, Myosin phosphorylation and regulation of the cross-bridge cycle in tracheal smooth muscle, Am. J. Physiol. 244:C182–C187.

    PubMed  CAS  Google Scholar 

  • Gerthoffer, W. T., and Murphy, R. A., 1983b, Ca2+, myosin phosphorylation, and relaxation of arterial smooth muscle, Am. J. Physiol. 245:C271–C277.

    PubMed  CAS  Google Scholar 

  • Gilman, A. G., 1984, Proteins and dual control of adenylate cyclase, Cell 36:577–579.

    PubMed  CAS  Google Scholar 

  • Gold, W. M., 1980, The role of cyclic nucleotides in airway smooth muscle, in: Physiology and Pharmacology of the Airways (J. A. Nadel, ed.), pp. 123–190, Dekker, New York.

    Google Scholar 

  • Goldberg, N. D., Haddox, M. K., Nicol, S. E., Glass, D. B., Sanford, C. H., Kuehl, F. A., Jr., and Estensen, R., 1975, Biological regulation through opposing influences of cyclic GMP and cyclic AMP: The Yin-Yang hypothesis, Adv. Cyclic Nucleotide Res. 5:307–330.

    PubMed  CAS  Google Scholar 

  • Gordon, A. R., 1978, Contraction of detergent-treated smooth muscle, Proc. Natl. Acad. Sci. USA 75:3527–3530.

    PubMed  CAS  Google Scholar 

  • Haeberle, J. R., Hathaway, D. R., and DiPauli-Roach, A. A., 1985a, Dephosphorylation of myosin by the catalytic subunit of a type-2 phosphatase produces relaxation of a chemically skinned uterine smooth muscle, J. Biol. Chem. 260:9965–9968.

    CAS  Google Scholar 

  • Haeberle, J. R., Hott, J. W., and Hathaway, D. R., 1985b, Regulation of isometric force and isotonic shortening velocity by phosphorylation of the 20,000 dalton myosin light chain of rat utering smooth muscle, Pflugers Arch. 403:215–219.

    CAS  Google Scholar 

  • Hay, D. W. P., Robinson, V. A., Fleming, W. W., and Fedan, J. S., 1985, Role of the epithelium in contractile responses of guinea pig isolated trachea, Fed. Proc. 44:506A.

    Google Scholar 

  • Hoar, P. E., Kerrick, W. G. L., and Cassidy, P. S., 1979, Chicken gizzard: Relation between calcium activated phosphorylation and contraction, Science 204:503–506.

    PubMed  CAS  Google Scholar 

  • Huang, F. L., and Glinsman, W. H., 1976, Separation and characterization of two Phosphorylase phosphatase inhibitors from rabbit skeletal muscle, Eur. J. Biochem. 70:419–426.

    PubMed  CAS  Google Scholar 

  • Punter, T., and Cooper, J. A., 1985, Protein-tyrosine kinases, Annu. Rev. Biochem. 54:897–930.

    Google Scholar 

  • Huxley, A. F., and Niedergerke, R., 1954, Structural change in muscle during contraction, Nature (Lond.) 173:971–973.

    CAS  Google Scholar 

  • Inagaki, M., Kawamoto, S., and Hidaka, H., 1984, Serotonin secretion from human platelets may be modified by a Ca2+-activated, phospholipid-dependent myosin phosphorylation, J. Biol. Chem. 259:14321–14323.

    PubMed  CAS  Google Scholar 

  • Itoh, T., Izumi, H., and Kuriyama, H., 1982, Mechanisms of relaxation induced by activation of ß-adrenoreceptors in smooth muscle Cells of the guinea-pig mesenteric artery, J. Physiol. (Lond.) 326:475–493.

    CAS  Google Scholar 

  • Janis, R. A., Barany, K., Barany, M., and Saraiiento, J. G., 1981, Association between myosin light chain phosphorylation and contraction of rat uterine smooth muscle, Mol. Physiol. 1:3–11.

    CAS  Google Scholar 

  • Kamm, K. E., and Stull, J. T., 1985, Myosin phosphorylation, force, and maximal shortening velocity in neurally stimulated tracheal smooth muscle, Am. J. Physiol. 249:C238–C247.

    PubMed  CAS  Google Scholar 

  • Katsuki, S., and Murad, F., 1977, Regulation of adenosine cyclic 3,5-monophosphate and guanosine cyclic 3,5 monophosphate levels and contractility in bovine tracheal smooth muscle, Mol. Pharmacol. 13:330–341.

    PubMed  CAS  Google Scholar 

  • Kerrick, W. G. L., and Hoar, P. E., 1981, Inhibition of smooth muscle tension by cyclic AMP-dependent protein kinase, Nature (Lond.) 292:253–255.

    CAS  Google Scholar 

  • Kerrick, W. G. L., Hoar, P. E., and Cassidy, P. S., 1980, Calcium-activated tension: The role of myosin light chain phosphorylation, Fed. Proc. 39:1558–1563.

    PubMed  CAS  Google Scholar 

  • Klee, C. B., and Krinks, M. H., 1978, Purification of cyclic 3,5nucleotide phosphodiesterase inhibitory protein by affinity chromatography on activator protein coupled to sepharose, Biochemistry 17:120–126.

    PubMed  CAS  Google Scholar 

  • Krebs, E. G., and Beavo, J. A., 1979, Phosphorylation-dephosphorylation of enzymes, Annu. Rev. Biochem. 48:923–959.

    PubMed  CAS  Google Scholar 

  • Ledvora, R. F., Barany, K., Van der Meulen, D. L., Barron, J. T., and Barany, M., 1983, Stretch-induced phosphorylation of the 20,000–dalton light chain of myosin in arterial smooth muscle, J. Biol. Chem. 258:14080–14083.

    PubMed  CAS  Google Scholar 

  • Marston, S. B., and Smith, C. W. J., 1985, The thin filaments of smooth muscles, J. Muscle Res. Cell Motil. 6:669–708.

    PubMed  CAS  Google Scholar 

  • Meisheri, K. D., and Ruegg, J. C, 1983, Dependence of cyclic-AMP-induced relaxation on Ca2+ and calmodulin in skinned smooth muscle of guinea pig taenia coli, Pflugers Arch. 399:315–320.

    PubMed  CAS  Google Scholar 

  • Meisheri, K. D., and van Breemen, C, 1982, Effects of ß-adrenergic stimulation on calcium movements in rabbit aortic smooth muscle: Relationship with cyclic AMP, J. Physiol. (Lond.) 331:429–441.

    CAS  Google Scholar 

  • Miller, J. R., Silver, P. J., and Stull, J. T., 1983, The role of myosin light chain kinase phosphorylation in ß adrenergic relaxation of tracheal smooth muscle, Mol. Pharmacol. 24:235–242.

    PubMed  CAS  Google Scholar 

  • Morgan, J. P., and Morgan, K. G., 1984, Alteration of cytoplasmic ionized calcium levels in smooth muscle by vasodilators in the ferret, J. Physiol. (Lond.) 357:539–551.

    CAS  Google Scholar 

  • Mueller, E., and van Breeman, C, 1979, Role of intraCellular Ca2+ sequestration in ß-adrenergic relaxation of a smooth muscle, Nature (Lond.) 281:682–683.

    CAS  Google Scholar 

  • Nag, S., and Seidel, J. C, 1983, 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. 258:6444–6449.

    PubMed  CAS  Google Scholar 

  • Ngai, P. K., and Walsh, M. P., 1984, Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon, J. Biol. Chem. 259:13656–13659.

    PubMed  CAS  Google Scholar 

  • Nishikawa, M., Hidaka, H., and Adelstein, R. S., 1983, Phosphorylation of smooth muscle heavy meromyosin by calcium-activated phospholipid-dependent protein kinase, J. Biol. Chem. 258: 14069–14072.

    PubMed  CAS  Google Scholar 

  • Nishikawa, M., de Lanerolle, P., Lincoln, T. M., and Adelstein, R. S., 1984, Phosphorylation of mammalian myosin light chain kinases by the catalytic subunit of cyclic AMP-dependent protein kinase and by cyclic GMP-dependent protein kinase, J. Biol. Chem. 259:8429–8436.

    PubMed  CAS  Google Scholar 

  • Nishikori, K., Weisbrodt, N. W., Sherwood, O. D., and Sanborn, B. M., 1983, Effects of relaxin on rat uterine myosin light chain kinase activity and myosin light chain phosphorylation, J. Biol. Chem. 258:2468–2474.

    PubMed  CAS  Google Scholar 

  • Nishizuka, Y., 1986, Studies and perspectives of protein kinase C, Science 233:305–312.

    PubMed  CAS  Google Scholar 

  • Noiman, E. S., 1980, Phosphorylation of smooth muscle myosin light chains by cAMP-dependent protein kinase, J. Biol. Chem. 255:11067–11070.

    PubMed  CAS  Google Scholar 

  • Pato, M. D., and Adelstein, R. S., 1980, Dephosphorylation of the 20,000 dalton light chain of myosin by two different phosphatases from smooth muscle, J. Biol. Chem. 255:6535–6538.

    PubMed  CAS  Google Scholar 

  • Pato, M. D., and Adelstein, R. S., 1983a, Characterization of a Mg2+-dependent phosphatase from turkey gizzard smooth muscle, J. Biol. Chem. 258:7055–7058.

    CAS  Google Scholar 

  • Pato, M. D., and Adelstein, R. S., 1983b, Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle: The effect of calmodulin binding to myosin light chain kinase on dephosphorylation, J. Biol. Chem. 258:7047–7054.

    CAS  Google Scholar 

  • Paul, R. J., Doerman, G., Zeugner, C, and Ruegg, J. C, 1983, The dependence of unloaded shortening velocity on Ca++, calmodulin, and duration of contraction in “chemically skinned” smooth muscle, Circ. Res. 53:342–351.

    PubMed  CAS  Google Scholar 

  • Perrie, W. T., and Perry, S. V., 1970, An electrophoretic study of the low-molecular-weight components of myosin, Biochem. J. 119:31–38.

    PubMed  CAS  Google Scholar 

  • Persechini, A., and Hartshorne, D. J., 1981, Phosphorylation of smooth muscle myosin: Evidence for cooperativity between the myosin heads, Science 213:1383–1385.

    PubMed  CAS  Google Scholar 

  • Pfitzer, G., Hofmann, F., DiSalvo, J., and Ruegg, J. C., 1984, cGMP and cAMP inhibit tension development in skinned coronary arteries, Pflugers Arch. 401:277–280.

    PubMed  CAS  Google Scholar 

  • Pfitzer, G., Merkel, L., Ruegg, J. C, and Hoffman, F., 1986, Cyclic GMP-dependent protein kinase relaxes skinned fibers from guinea pig taenia coli but not from chicken gizzard, Pflugers Arch. 407:87–91.

    PubMed  CAS  Google Scholar 

  • Rapoport, R. M., and Murad, F., 1983, Agonist-induced endothelium-dependent relaxation in rat thoracic aorta may be mediated through cGMP, Circ. Res. 52:352–357.

    PubMed  CAS  Google Scholar 

  • Rees, D. D., and Fredericksen, D. W., 1981, Calcium regulation of porcine aortic myosin, J. Biol. Chem. 256:357–364.

    PubMed  CAS  Google Scholar 

  • Rinard, G. A., Jensen, A., and Puckett, M., 1983, Hydrocortisone and isoproterenol effects on trachealis, cAMP and relaxation, J. Appl. Physiol. 55:1609–1613.

    PubMed  CAS  Google Scholar 

  • Rinard, G. A., Rubinfeld, A. R., Brunton, L. L., and Mayer, S. E., 1979, Depressed cyclic AMP levels in airway smooth muscle from asthmatic dogs, Proc. Natl. Acad. Sci. USA 76:1472–1476.

    PubMed  CAS  Google Scholar 

  • Ringer, S., 1883, A further contribution regarding the influence of the different constituents of the blood on the contraction of the heart, J. Physiol. (Lond.) 4:29–42.

    CAS  Google Scholar 

  • Ruegg, J. C, and Paul, R. J., 1982, Vascular smooth muscle. Calmodulin and cyclic AMP-dependent protein kinase alter calcium sensitivity in porcine carotid skinned fibers, Circ. Res. 50:394–399.

    PubMed  CAS  Google Scholar 

  • Ruegg, J. C, and Pfitzer, G., 1985, Modulation of calcium sensitivity in guinea pig taenia coli: skinned fiber studies, Experientia 41:997–1001.

    PubMed  CAS  Google Scholar 

  • Saida, K., and Nonomura, Y., 1978, Characteristics of Ca2+-and Mg2+-induced tension development in chemically skinned smooth muscle fibers, J. Gen. Physiol. 72:1–14.

    PubMed  CAS  Google Scholar 

  • Scheid, C. R., and Fay, F. S., 1984, ß-Adrenergic effects on transmembrane 45Ca fluxes in isolated smooth muscle Cells, Am. J. Physiol. 246:C431–C438.

    PubMed  CAS  Google Scholar 

  • Scheid, C. R., Honeyman, T. W., and Fay, F. S., 1979, Mechanism of ß-adrenergic relaxation of smooth muscle, Nature (Lond.) 277:32–36.

    CAS  Google Scholar 

  • Sellers, J. R., Pato, M. D., and Adelstein, R. S., 1981, Reversible phosphorylation of smooth muscle myosin, heavy meromyosin, and platelet myosin, J. Biol. Chem. 256:13137–13142.

    PubMed  CAS  Google Scholar 

  • Sellers, J. R., Chock, P. B., and Adelstein, R. S., 1983, The apparently negatively cooperative phosphorylation of smooth muscle myosin at low ionic strength is related to its filamentous state, J. Biol. Chem. 258:14181–14188.

    PubMed  CAS  Google Scholar 

  • Silver, P. J., and Stull, J. T., 1982, Regulation of myosin light chain and Phosphorylase phosphorylation in tracheal smooth muscle, J. Biol. Chem. 257:6145–6150.

    PubMed  CAS  Google Scholar 

  • Singer, H. A., and Peach, M. J., 1982, Calcium-and endothelial-mediated vascular smooth muscle relaxation in rabbit aorta, Hypertension 2(SuppL): 19–25.

    Google Scholar 

  • Sobieszek, A., 1977, Vertebrate smooth muscle myosin. Enzymatic and structural properties, in: The Biochemistry of Smooth Muscle (N. L. Stephens, ed.), pp. 413–443, University Park Press, Baltimore.

    Google Scholar 

  • Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S., 1981, Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin, Proc. Natl. Acad. Sci. USA 78:5652–5655.

    PubMed  CAS  Google Scholar 

  • Sobue, K., Morimoto, K., Inui, M., Kanda, K., and Kakiuchi, S., 1982, Control of actin-myosin interaction of gizzard smooth muscle by calmodulin and caldesmon-linked flip-flop mechanism, Biomed. Res. 3:188–196.

    CAS  Google Scholar 

  • Sparrow, M. P., Pfitzer, G., Gagelmann, M., and Ruegg, J. C, 1984, Effect of calmodulin, Ca2+, and cAMP protein kinase on skinned tracheal smooth muscle, Am. J. Physiol. 246:C308–C314.

    PubMed  CAS  Google Scholar 

  • Squire, J., 1981, Muscle regulation: A decade of the steric blocking model, Nature (Lond.) 291:614–615.

    CAS  Google Scholar 

  • Stewart, A. A., Ingebritsen, T. S., and Cohen, P., 1983, The protein phosphatase involved in Cellular regulation: purification and properties of a Ca2+/Calmodulin-dependent protein phosphatase (2B) from rabbit skeletal muscle, Eur. J. Biochem. 132:289–295.

    PubMed  CAS  Google Scholar 

  • Szentivanyi, A., 1968, The ß-adrenergic theory of the atopic abnormality in bronchial asthma, J. Allergy 42:203–232.

    Google Scholar 

  • Torphy, T. J., and Gerthoffer, W. T., 1986, Biochemical mechanisms of airway smooth muscle contraction and relaxation, in: Current Topics in Pulmonary Pharmacology and Toxicology, Vol. 1 (M. A. Hollinger, ed.), pp. 23–56, Elsevier, New York.

    Google Scholar 

  • Torphy, T. J., Freese, W. B., Rinard, G. A., Brunton, L. L., and Mayer, S. E., 1982, Cyclic nucleotide-dependent protein kinases in airway smooth muscle, J. Biol. Chem. 257:11609–11616.

    PubMed  CAS  Google Scholar 

  • Torphy, T. J., Zheng, L., Peterson, S. M., Fiscus, R. R., Rinard, G. A., and Mayer, S. E., 1985, Inhibitory effect of methacholine on drug-induced relaxation, cyclic AMP accumulation, and cyclic AMP-dependent protein kinase activation in canine tracheal smooth muscle, J. Pharm. Exp. Ther. 233:409–417.

    CAS  Google Scholar 

  • van Breeman, C, 1977, Calcium requirement for activation of intact aortic smooth muscle, J. Physiol. (Lond.) 272:317–329.

    Google Scholar 

  • Van de Vorde, J., and Leusen, I., 1983, The role of endothelium in the vasodilator response of rat thoracic aorta to histamine, Eur. J. Pharmacol. 87:113–120.

    Google Scholar 

  • Walsh, M. P., Bridenbaugh, R., Hartshome, D. J., and Kerrick, W. G. L., 1982a, Phosphorylation-dependent activated tension in skinned gizzard muscle fibers in the absence of Ca2+, J. Biol. Chem. 257:5987–5990.

    CAS  Google Scholar 

  • Walsh, M. P., Dabrowska, R., Hinkins, S., and Hartshome, D. J., 1982b, Calcium-independent myosin light chain kinase from smooth muscle. Preparation by limited chymotryptic digestion of the calcium ion dependent enzyme, purification and characterization, Biochemistry 21:1919–1925.

    CAS  Google Scholar 

  • Walsh, M. P., Persechini, A., Hinkins, S., and Hartshome, D. J., 1981, Is smooth muscle myosin a substrate for cAMP dependent protein kinase?, FEBS Lett. 126:107–110.

    PubMed  CAS  Google Scholar 

  • Werth, D. K., Haeberle, J. R., and Hathaway, D. R., 1982, Purification of a myosin phosphatase from bovine aortic smooth muscle, J. Biol. Chem. 257:7306–7309.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1989 Plenum Press, New York

About this chapter

Cite this chapter

de Lanerolle, P. (1989). Cellular Control Mechanisms in Airway Smooth Muscle. In: Coburn, R.F. (eds) Airway Smooth Muscle in Health and Disease. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0779-2_6

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-0779-2_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-8078-1

  • Online ISBN: 978-1-4613-0779-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics