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Myosin Light Chain Phosphorylation in Uterine Smooth Muscle

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Uterine Function

Abstract

The uterus is a unique organ capable of increasing its size enormously during pregnancy. The strong contractions of the myometrium bring about the expulsion of the fetus. An understanding of uterine contractility has been the goal of many workers in the last half century.1 Only in this decade has it been recognized that phosphorylation of a small subunit in the head part of the myosin molecule plays a key role in uterine contractility.2–5

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References

  1. Needham, D. M., 1971, Machina Carnis, Cambridge University Press, London.

    Book  Google Scholar 

  2. Huszar, G., and Bailey, P., 1979, Relationship between actin-myosin interaction and myosin light- chain phosphorylation in human placental smooth muscle, Am. J. Obstet. Gynecol 135:718–726.

    PubMed  CAS  Google Scholar 

  3. Lebowitz, E. A., and Cooke, R., 1979, Phosphorylation of uterine smooth muscle myosin permits actin-activation, J. Biochem 85:1489–1494.

    PubMed  CAS  Google Scholar 

  4. Janis, R. A., Moats-Staats, B. M., and Gualtieri, R. T., 1980, Protein phosphorylation during spontaneous contraction of smooth muscle, Biochem. Biophys. Res. Commun 96:265–270.

    Article  PubMed  CAS  Google Scholar 

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

    CAS  Google Scholar 

  6. Kühne, W., 1859, Untersuchungen über Bewegungen und Veränderungen der contractilen Substanzen, Arch. Anat. Physiol. Wiss. Medp. 748. Quoted from Needham, D. M., 1971, Machina Carnis, Cambridge University Press, London, p. 674.

    Google Scholar 

  7. Kühne, W., 1864, Untersuchungen über das Protoplasma und die Contractilität, W. Engelmann, Leipzig. Quoted from Needham, D. M., 1971, Machina Carnis, Cambridge University Press, London, p. 674.

    Google Scholar 

  8. Mehl, J. W., 1938, Studies on the proteins of smooth muscle, I, J. Biol. Chem 123:1xxxiii

    Google Scholar 

  9. Csapo, A., 1948, Actomyosin content of the uterus, Nature 162:218–219.

    Article  PubMed  CAS  Google Scholar 

  10. Needham, D. M., and Williams, J. M., 1959, Some properties of uterus actomyosin and myofilaments, Biochem. J 73:171–181.

    PubMed  CAS  Google Scholar 

  11. Needham, D. M., and Williams, J. M., 1963, Proteins of the uterine contractile mechanism, Biochem. J 89:552–561.

    PubMed  CAS  Google Scholar 

  12. Bárány, M., Bárány, K., Gaetjens, E., and Bailin, G., 1966, Chicken gizzard myosin, Arch. Biochem. Biophys 113:205–221.

    Article  PubMed  Google Scholar 

  13. Tsao, T. C., 1953, Fragmentation of myosin molecule, Biochim. Biophys. Acta 11:368–382.

    Article  PubMed  CAS  Google Scholar 

  14. Locker, R. H., 1956, The dissociation of myosin by heat coagulation, Biochim. Biophys. Acta 20:514–521.

    Article  PubMed  CAS  Google Scholar 

  15. Kominz, D. R., Carroll, W. R., Smith, E. N., and Mitchell, E. R., 1959, A subunit of myosin, Arch. Biochem. Biophys 79:191–199.

    Article  CAS  Google Scholar 

  16. Wetlaufer, D. B., and Edsall, J. T., 1960, Sedimentation of myosin in urea solutions, Biochim. Biophys. Acta 43:132–134.

    Article  PubMed  CAS  Google Scholar 

  17. Dreizen, P., Hartshorne, D. J., and Stracher, A., 1966, The subunit structure of myosin, I. Poly- dispersity in 5 M guanidine, J. Biol. Chem 241:443–448.

    PubMed  CAS  Google Scholar 

  18. Gershman, L. C., Dreizen, P., and Stracher, A., 1966, Subunit structure of myosin. II. Heavy and light alkali components, Proc. Natl. Acad. Sci. USA 56:966–973.

    Article  PubMed  CAS  Google Scholar 

  19. Oppenheimer, H., Bárány, K., Hamoir, G., and Fenton, J., 1967, Succinylation of myosin, Arch. Biochem. Biophys 120:108–118.

    Article  PubMed  CAS  Google Scholar 

  20. Bárány, K., and Oppenheimer H., 1967, Succinylated meromyosins, Nature 213:626–627.

    Article  PubMed  Google Scholar 

  21. Perry, S. V., 1979, The regulation of contractile activity in muscle, Biochem. Soc. Trans 7:596– 617.

    Google Scholar 

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

    Google Scholar 

  23. Gorecka, A., Aksoy, M. O, and Hartshorne, D. J., 1976, The effect of phosphorylation of gizzard myosin on actin activation, Biochem. Biophys. Res. Commun 71:325–331.

    Article  PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  25. Barron, J. T., Bárány, M., and Bárány, K., 1979, Phosphorylation of the 20,000-dalton light chain of myosin of intact arterial smooth muscle in rest and in contraction, J. Biol. Chem 254:4954– 4956.

    Google Scholar 

  26. 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.

    Article  PubMed  CAS  Google Scholar 

  27. Ashton, F. T., Somlyo, A. V., and Somlyo, A. P., 1975, The contractile apparatus of vascular smooth muscle: Intermediate high voltage stereo electron microscopy, J. Mol. Biol 98:17–29.

    Article  PubMed  CAS  Google Scholar 

  28. Trybus, K. M., Huiatt, T. W., and Lowey, S., 1982, A bent monomelic conformation of myosin from smooth muscle, Proc. Natl. Acad. Sci. USA 79:6151–6155.

    Article  PubMed  CAS  Google Scholar 

  29. Ikebe, M., Hinkins, S., and Hartshorne, D. J., 1983, Correlation of enzymatic properties and conformation of smooth muscle myosin, Biochemistry 22:4580–4587.

    Article  PubMed  CAS  Google Scholar 

  30. Bailin, G., 1986, Structure and function of smooth muscle myosin, Biochem. Arch 2:229–236.

    CAS  Google Scholar 

  31. Sobieszek, A., and Bremel, R. D., 1975, Preparation and properties of vertebrate smooth-muscle myofibrils and actomyosin, Eur. J. Biochem 55:49–60.

    Article  PubMed  CAS  Google Scholar 

  32. Cavaille, F., Janmot, C., Ropert, S., and d’Albis, A., 1986, Isoforms of myosin and actin in human, monkey, and rat myometrium. Comparison of pregnant and non-pregnant uterus proteins, Eur. J. Biochem 160:507–513.

    Article  PubMed  CAS  Google Scholar 

  33. Bárány, M., 1967, ATPase activity of myosin correlated with speed of muscle shortening, J. Gen. Physiol 50:197–218.

    Article  PubMed  Google Scholar 

  34. Murphy, R. A., 1979, Filament organization and contractile function in vertebrate smooth muscle, Annu. Rev. Physiol 41:737–748.

    Article  PubMed  CAS  Google Scholar 

  35. Small, J. V., and Sobieszek, A., 1983, Contractile and structural proteins of smooth muscle, in: Biochemistry of Smooth Muscle, Volume I (N. L. Stephens, ed.), CRC Press, Boca Raton, pp. 85– 140

    Google Scholar 

  36. Marston, S. B., 1983, Myosin and actomyosin ATPase: Kinetics, in: Biochemistry of Smooth Muscle, Volume I ( N. L. Stephens, ed.), CRC Press, Boca Raton, pp. 167–191.

    Google Scholar 

  37. Horiuchi, K. Y., Miyata, H., and Chacko, S., 1986, Modulation of smooth muscle actomyosin ATPase by thin filament associated proteins, Biochem. Biophys. Res. Commun 136:962–968.

    Article  PubMed  CAS  Google Scholar 

  38. Aksoy, M. O., and Murphy, R. A., 1983, Regulation of the dynamic properties of smooth muscle: Ca++-stimulated cross-bridge phosphorylation, in: Biochemistry of Smooth Muscle, Volume I ( N. L. Stephens, ed.), CRC Press, Boca Raton, pp. 141–166.

    Google Scholar 

  39. Edelman, A. M., Blumenthal, D. K., and Krebs, E. G., 1987, Protein serine/threonine kinases, Annu. Rev. Biochem 56:567–613.

    Article  PubMed  CAS  Google Scholar 

  40. Higashi, K., Fukunaga, K., Matsui, K., Maeyama, M., and Miyamoto, E., 1983, Purification and characterization of myosin light-chain kinase from porcine myometrium and its phosphorylation and modulation by cyclic AMP-dependent protein kinase, Biochim. Biophys. Acta 747:232–240.

    Article  PubMed  CAS  Google Scholar 

  41. Cohen, D. M., and Murphy, R. A., 1978, Differences in cellular contractile protein contents among porcine smooth muscles, J. Gen. Physiol 72:369–380.

    Article  PubMed  CAS  Google Scholar 

  42. Adelstein, R. S., and Hathaway, D. R., 1979, Role of calcium and cyclic adenosine 3′: 5′ monophosphate in regulating smooth muscle contraction, Am. J. Cardiol 44:783–787.

    Article  PubMed  CAS  Google Scholar 

  43. Polacek, I., and Daniel, E. E., 1971, Effect of a- and p-adrenergic stimulation on the uterine motility and adenosine 3′,5′–monophosphate level, Can. J. Physiol. Pharmacol 49:988–998.

    Article  PubMed  CAS  Google Scholar 

  44. Richardson, M. R., Taylor, D. A., Casey, M. L., MacDonald, P. C., and Stull, J. T., 1987, Biochemical markers of contraction in human myometrial smooth muscle cells in culture, In Vitro Cell. Dev. Biol 23:21–28.

    Article  PubMed  CAS  Google Scholar 

  45. Endo, T., Naka, M., and Hidaka, H., 1982, Ca2+ -phospholipid dependent phosphorylation of smooth muscle myosin, Biochem. Biophys. Res. Commun 105:942–948.

    Article  PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  47. Baraban, J. M., Gould, R. J., Peroutka, S. J., and Snyder, S. H., 1985, Phorbol ester effects on neurotransmission: Interaction with neurotransmitters and calcium in smooth muscle, Proc. Natl. Acad. Sci. USA 82:604–607.

    Article  PubMed  CAS  Google Scholar 

  48. Sawamura, M., Kobayashi, Y., Nara, Y., Hattori, K., and Yamori, Y., 1987, Effect of extracellular calcium on vascular contraction induced by phorbol ester, Biochem. Biophys. Res. Commun 145:494–501.

    Article  PubMed  CAS  Google Scholar 

  49. Howe, P. H., and Abdel-Latif, A. A., 1987, Phorbol ester-induced protein-phosphorylation and contraction in sphincter smooth muscle of rabbit iris, FEBS Lett 215:279–284.

    Article  PubMed  CAS  Google Scholar 

  50. Kamm, K. E., and Stull, J. T., 1985, The function of myosin and myosin light chain kinase phosphorylation in smooth muscle, Annu. Rev. Pharmacol. Toxicol 25:593–620.

    Article  PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  52. Di Salvo, J., Gifford, D., Bialojan, C., and Rüegg, J. C., 1983, An aortic spontaneously active phosphatase dephosphorylates myosin and inhibits actin-myosin interaction, Biochem. Biophys. Res. Commun 111:906–911.

    Google Scholar 

  53. Pato, M. D., and Kerc, E., 1985, Purification and characterization of a smooth muscle myosin phosphatase from turkey gizzards, J. Biol. Chem 260:12359–12366.

    PubMed  CAS  Google Scholar 

  54. 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 

  55. Bárány, K., Ledvora, R. F., Mougios, V., and Bárány, M., 1985, Stretch-induced myosin light chain phosphorylation and stretch-release-induced tension development in arterial smooth muscle, J. Biol. Chem 260:7126 –7130.

    PubMed  Google Scholar 

  56. Bárány, K., Csabina, S., and Bárány, M., 1985, The phosphorylation of the 20,000 dalton myosin light chain in rat uterus, in: Advances in Protein Phosphatases, Volume II ( W. Merlevede and J. DiSalvo, eds.), Leuven University Press, Leuven, Belgium, pp. 37–58.

    Google Scholar 

  57. Csabina, S., Mougios, V., Bárány, M., and Bárány, K., 1986, Characterization of the phos- phorylatable myosin light chain in rat uterus, Biochim. Biophys. Acta 871:311–315.

    Article  PubMed  CAS  Google Scholar 

  58. Dokhac, L., D’Albis, A., Janmot, C., and Harborn, S., 1986, Myosin light chain phosphorylation in intact rat uterine smooth muscle. Role of calcium and cyclic AMP, J. Muscle Res. Cell Motil 7:259–268.

    Article  PubMed  CAS  Google Scholar 

  59. Haeberle, J. R., Hott, J. W., and Hathaway, D. R., 1984, Pseudophosphorylation of the smooth muscle 20,000 dalton myosin light chain. An artifact due to protein modification, Biochim. Biophys. Acta 790:78–86.

    Article  PubMed  CAS  Google Scholar 

  60. Gagelmann, M., Ruegg, J. C., and Di Salvo, J., 1984, Phosphorylation of the myosin light chains and satellite proteins in detergent-skinned arterial smooth muscle, Biochem. Biophys. Res. Commun 120:933–938.

    Article  PubMed  CAS  Google Scholar 

  61. Mougios, V., and Bárány, M., 1986, Isoforms of the phosphorylatable myosin light chain in arterial smooth muscle, Biochim. Biophys. Acta 872:305–308.

    Article  PubMed  CAS  Google Scholar 

  62. Bárány, K., Csabina, S., de Lanerolle, P., and Bárány, M., 1987, Evidence for isoforms of the phosphorylatable myosin light chain in rat uterus, Biochim. Biophys. Acta 911:369–371.

    Article  PubMed  Google Scholar 

  63. Pette, D., 1980, Plasticity of Muscle, de Gruyter, Berlin

    Google Scholar 

  64. Swynghedauw, B., 1986, Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles, Physiol. Rev 66:710–771.

    PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  66. Hathaway, D. R., and Haeberle, J. R., 1985, A radioimmunoblotting method for measuring myosin light chain phosphorylation levels in smooth muscle, Am. J. Physiol 249:C345–C351.

    PubMed  CAS  Google Scholar 

  67. Silver, P. J., and Stull, J. T., 1982, Quantitation of myosin light chain phosphorylation in small tissue samples, J. Biol. Chem 257:6137–6144.

    PubMed  CAS  Google Scholar 

  68. Csabina, S. Bárány, M., and Bárány, K., 1987, Comparison of myosin light chain phosphorylation in uterine and arterial smooth muscles, Comp. Biochem. Physiol 87B:271–277.

    CAS  Google Scholar 

  69. Bárány, K., Ledvora, R. F., and Bárány, M., 1985, The phosphorylation of the 20,000 dalton myosin light chain in intact arterial muscle, in: Calmodulin Antagonists and Cellular Physiology H. Hidaka and D. J. Hartshorne, eds.), Academic Press, New York, pp. 199–223.

    Google Scholar 

  70. 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 

  71. Silver, P. J., and Stull, J. T., 1982, Regulation of myosin light chain and phosphorylase phosphorylation in tracheal smooth muscle, J. Biol. Chem257: 6145–6150.

    PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  73. Weisbrodt, N. W., and Murphy, R. A., 1985, Myosin phosphorylation and contraction of feline esophageal smooth muscle, Am. J. Physiol 249:C9–C14.

    PubMed  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  75. Kroeger, E. A., Marshall, J. M., and Bianchi, C. P., 1975, Effect of isoproterenol and D600 on calcium movements in rat myometrium, J. Pharmacol. Exp. Ther 193:309–316.

    PubMed  CAS  Google Scholar 

  76. Huszar, G., 1981, Biology and biochemistry of myometrial contractility and cervical maturation, Semin. Perinatol 5:216–234.

    PubMed  CAS  Google Scholar 

  77. 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 

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

    PubMed  CAS  Google Scholar 

  79. van Breemen, C., Leijten, P., Yamamoto, H., Aaronson, P., and Cauvin, C., 1986, Calcium activation of vascular smooth muscle, Hypertension 8:II-89-I-95

    Google Scholar 

  80. Carsten, M. E., Miller, J. D., 1985, Ca2+ release by inositol trisphosphate from Ca2+ -transporting microsomes derived from uterine sarcoplasmic reticulum, Biochem. Biophys. Res. Commun 130:1027–1031.

    Article  PubMed  CAS  Google Scholar 

  81. Riemer, R. K., and Roberts, J. M., 1986, Activation of uterine smooth muscle contraction: Implications for eicosanoid action and interactions, Semin. Perinatol 10:276–287.

    PubMed  CAS  Google Scholar 

  82. Bárány, K., Bárány, M., Gillis, J. M., and Kushmerick, M. J., 1979, Phosphorylation-de- phosphorylation of the 18,000-dalton light chain of myosin during the contraction-relaxation cycle of frog muscle, J. Biol Chem 254:3617–3623.

    PubMed  Google Scholar 

  83. Gershman, L. C., Selden, L. A., and Estes, J. E., 1986, High affinity binding of divalent cation to actin monomer is much stronger than previously reported, Biochem. Biophys. Res. Commun 135:607–614.

    Article  PubMed  CAS  Google Scholar 

  84. Bond, M., Shuman, H., Somlyo, A. P., and Somlyo, A. V., 1984, Total cytoplasmic calcium in relaxed and maximally contracted rabbit portal vein smooth muscle, J. Physiol. (London 357:185– 201.

    Google Scholar 

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Bárány, K., Bárány, M. (1990). Myosin Light Chain Phosphorylation in Uterine Smooth Muscle. In: Carsten, M.E., Miller, J.D. (eds) Uterine Function. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0575-0_3

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  • DOI: https://doi.org/10.1007/978-1-4613-0575-0_3

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