Regulation of smooth muscle contractile elements by second messengers.

In smooth muscle cells, development of force results from MgA TP-dependent cyclic interactions of myosin in thick filaments with actin in thin filaments. The force of contraction, in turn, is regulated by the concentration of free Ca2+ surrounding these myofilaments. The purposes of the present chapter are to discuss (a) Ca2+ -dependent mechanisms other than myosin light chain phosphorylation by which contractile force in smooth muscle may be reg­ ulated, and (b) other second messenger mechanisms that regulate contractile elements or the myosin kinase/phosphatase system . Since the discovery that phosphorylation of the 20-kDa light chains of myosin by Ca2+ /calmodulin-dependent myosin light chain kinase allows smooth muscle myosin MgATPase to be activated by actin, many in­ vestigators have studied the relationship between light chain phosphorylation and active force in smooth muscle (reviewed in 42; Hai & Murphy, this volume). It is generally accepted that myosin phosphorylation and de­ phosphorylation are sufficient to regulate contraction. While myosin phos­ phorylatiOn/dephosphorylation may be the dominant regulatory pathway, the coexistence of thin-filament linked regulation is not ruled out (51).

[1]  H. Itoh,et al.  Contraction of rat thoracic aorta strips induced by phorbol 12-myristate 13-acetate. , 1987, The American journal of physiology.

[2]  P F Dillon,et al.  Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle. , 1981, Science.

[3]  R. Deth,et al.  Phorbol ester-induced contraction of arterial smooth muscle and inhibition of α-adrenergic response , 1984 .

[4]  J. Stull,et al.  Myosin phosphorylation, force, and maximal shortening velocity in neurally stimulated tracheal smooth muscle. , 1985, The American journal of physiology.

[5]  J. Wagner,et al.  Caldesmon‐induced inhibition of ATPase activity of actomyosin and contraction of skinned fibres of chicken gizzard smooth muscle , 1985, FEBS letters.

[6]  C. Cohen,et al.  Rod phosphorylation favors folding in a catch muscle myosin. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[7]  Ca2+ can control vascular smooth-muscle thin filaments without caldesmon phosphorylation. , 1986, The Biochemical journal.

[8]  W. Gerthoffer.  Dissociation of myosin phosphorylation and active tension during muscarinic stimulation of tracheal smooth muscle. , 1987, The Journal of pharmacology and experimental therapeutics.

[9]  H. Rasmussen,et al.  TPA-induced contraction of isolated rabbit vascular smooth muscle. , 1984, Biochemical and biophysical research communications.

[10]  J. Sellers,et al.  The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin. , 1986, The Journal of biological chemistry.

[11]  T. Itoh,et al.  Purified rabbit brain protein kinase C relaxes skinned vascular smooth muscle and phosphorylates myosin light chain. , 1987, Archives of biochemistry and biophysics.

[12]  C. Cohen,et al.  Myosin rod phosphorylation and the catch state of molluscan muscles. , 1987, Science.

[13]  H. Hidaka,et al.  Conformational studies of myosin phosphorylated by protein kinase C. , 1985, The Journal of biological chemistry.

[14]  H. Rasmussen,et al.  Plasma membrane calcium flux, protein kinase C activation and smooth muscle contraction. , 1985, The Journal of pharmacology and experimental therapeutics.

[15]  W. Lehman,et al.  Caldesmon is a Ca2+-regulatory component of native smooth-muscle thin filaments. , 1985, The Biochemical journal.

[16]  J. D. De Mey,et al.  Localization of filamin in smooth muscle , 1986, The Journal of cell biology.

[17]  R. A. Murphy,et al.  Cross-bridge phosphorylation and regulation of latch state in smooth muscle. , 1988, The American journal of physiology.

[18]  T. Lincoln,et al.  Phosphorylation of mammalian myosin light chain kinases by the catalytic subunit of cyclic AMP-dependent protein kinase and by cyclic GMP-dependent protein kinase. , 1984, The Journal of biological chemistry.

[19]  M. Walsh,et al.  The effects of phosphorylation of smooth-muscle caldesmon. , 1987, The Biochemical journal.

[20]  J. D. De Mey,et al.  Caldesmon is an elongated, flexible molecule localized in the actomyosin domains of smooth muscle. , 1986, The EMBO journal.

[21]  M. Ikebe,et al.  Binding of caldesmon to smooth muscle myosin. , 1988, The Journal of biological chemistry.

[22]  R. Adelstein,et al.  Increased phosphorylation of myosin light chain kinase after an increase in cyclic AMP in intact smooth muscle. , 1984, Science.

[23]  Steven B Marston,et al.  Ca2+ regulation of the thin filaments: biochemical mechanism and physiological role. , 1988, Biochemical Society transactions.

[24]  M. Bárány,et al.  Characterization of the phosphorylatable myosin light chain in rat uterus. , 1986, Biochimica et biophysica acta.

[25]  J. Small.  Geometry of actin‐membrane attachments in the smooth muscle cell: the localisations of vinculin and alpha‐actinin. , 1985, The EMBO journal.

[26]  H. Hidaka,et al.  Phosphorylation of smooth muscle myosin light chain kinase by Ca2+-activated, phospholipid-dependent protein kinase. , 1985, The Journal of biological chemistry.

[27]  C. Smith,et al.  The mechanism of Ca2+ regulation of vascular smooth muscle thin filaments by caldesmon and calmodulin. , 1987, The Journal of biological chemistry.

[28]  K. Morgan,et al.  Intracellular calcium levels in phorbol ester-induced contractions of vascular muscle. , 1987, The American journal of physiology.

[29]  K. Horiuchi,et al.  Modulation of smooth muscle actomyosin ATPase by thin filament associated proteins. , 1986, Biochemical and biophysical research communications.

[30]  K. Sobue,et al.  Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[31]  J. Stull,et al.  Different phosphorylated forms of myosin in contracting tracheal smooth muscle. , 1986, The Journal of biological chemistry.

[32]  R. Pearson,et al.  Spatial requirements for location of basic residues in peptide substrates for smooth muscle myosin light chain kinase. , 1985, The Journal of biological chemistry.

[33]  C. Michnoff,et al.  Phosphorylation of synthetic peptides by skeletal muscle myosin light chain kinases. , 1986, The Journal of biological chemistry.

[34]  C. Slaughter,et al.  Sites phosphorylated in myosin light chain in contracting smooth muscle. , 1988, The Journal of biological chemistry.

[35]  T. Hada,et al.  Expression of high and low molecular weight caldesmons during phenotypic modulation of smooth muscle cells. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[36]  Steven B Marston.  The regulation of smooth muscle contractile proteins. , 1983, Progress in biophysics and molecular biology.

[37]  M. Bárány,et al.  Myosin light chain phosphorylation in frog heart. , 1982, Biochimica et biophysica acta.

[38]  R. Adelstein,et al.  Phosphorylation of smooth muscle myosin light chain kinase by protein kinase C. Comparative study of the phosphorylated sites. , 1985, The Journal of biological chemistry.

[39]  M. De Brabander,et al.  The molecular organization of myosin in stress fibers of cultured cells , 1986, The Journal of cell biology.

[40]  H. Osińska,et al.  The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments. , 1985, Biochimica et biophysica acta.

[41]  Effects of Ca2+, Mg2+, and myosin phosphorylation on skinned smooth muscle fibers. , 1987, The American journal of physiology.

[42]  J. Stull,et al.  The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. , 1985, Annual review of pharmacology and toxicology.

[43]  E. Appella,et al.  Sequence of the sites phosphorylated by protein kinase C in the smooth muscle myosin light chain. , 1987, The Journal of biological chemistry.

[44]  R. A. Murphy,et al.  Ca2+, myosin phosphorylation, and relaxation of arterial smooth muscle. , 1983, The American journal of physiology.

[45]  K. Sobue,et al.  CONTROL OF ACTIN-MYOSIN INTERACTION OF GIZZARD SMOOTH MUSCLE BY CALMODULIN- AND CALDESMONLINKED FLIP-FLOP MECHANISM , 1982 .

[46]  W. Lehman,et al.  Diversity in smooth muscle thin filament composition. , 1987, Biochimica et biophysica acta.

[47]  D. Hartshorne,et al.  Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase. , 1985, The Journal of biological chemistry.

[48]  S. Kawamoto,et al.  The heavy chain of smooth muscle myosin is phosphorylated in aorta cells. , 1988, The Journal of biological chemistry.

[49]  J. N. Wells,et al.  Phorbol diesters alter the contractile responses of porcine coronary artery. , 1986, The Journal of pharmacology and experimental therapeutics.

[50]  A. Hakura,et al.  Occurrence of caldesmon (a calmodulin-binding protein) in cultured cells: comparison of normal and transformed cells. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[51]  M. Bárány,et al.  Myosin Light Chain Isoforms and Their Phosphorylation in Arterial Smooth Muscle , 1987, Circulation research.