Caldesmon and smooth-muscle regulation

Smooth muscles exist in the wall of hollow organs in our body and are responsible for controlling the flow of vital fluids that are essential for the normal function of the cardiovascular, respiratory, digestive, and reproductive systems. Many diseases, such as hypertension, asthma, indigestion, and premature birth, may attribute to malfunction of smooth-muscle contraction. It is therefore important to decipher how smooth-muscle contraction is regulated. This review attempts to give a brief overview of current understanding about the molecular mechanisms of smooth-muscle regulation and, in particular, to discuss possible roles of caldesmon in this regulatory process.

[1]  Z. Q. Yang,et al.  Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[2]  P. Wagner.  Unphosphorylated calf thymus and aorta myosins contract ghost myofibrils. , 1986, The Journal of biological chemistry.

[3]  G. Ellis‐Davies,et al.  Kinetics of Prephosphorylation Reactions and Myosin Light Chain Phosphorylation in Smooth Muscle , 1995, The Journal of Biological Chemistry.

[4]  W. Lehman,et al.  Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments , 1993, The Journal of cell biology.

[5]  B. Katzenellenbogen,et al.  Analysis of Mechanisms That Determine Dominant Negative Estrogen Receptor Effectiveness (*) , 1995, The Journal of Biological Chemistry.

[6]  J. Derancourt,et al.  Precise identification of the regulatory F-actin- and calmodulin-binding sequences in the 10-kDa carboxyl-terminal domain of caldesmon. , 1994, The Journal of biological chemistry.

[7]  J. Small.  Structure‐function relationships in smooth muscle: The missing links , 1995, BioEssays : news and reviews in molecular, cellular and developmental biology.

[8]  P. Graceffa,et al.  A long helix from the central region of smooth muscle caldesmon. , 1991, The Journal of biological chemistry.

[9]  P. Graceffa,et al.  Disulfide cross-linking of caldesmon to actin. , 1991, The Journal of biological chemistry.

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

[11]  K. Mabuchi,et al.  The Major Myosin-binding Site of Caldesmon Resides Near Its N-terminal Extreme* , 2000, The Journal of Biological Chemistry.

[12]  T. Tao,et al.  Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle , 1996, Journal of Muscle Research & Cell Motility.

[13]  F. Fay,et al.  Myosin filaments isolated from skinned amphibian smooth muscle cells are side-polar , 1989, Journal of Muscle Research & Cell Motility.

[14]  C. L. Wang.  Photocrosslinking of calmodulin and/or actin to chicken gizzard caldesmon. , 1988, Biochemical and biophysical research communications.

[15]  A. Bretscher,et al.  The calmodulin and F-actin binding sites of smooth muscle caldesmon lie in the carboxyl-terminal domain whereas the molecular weight heterogeneity lies in the middle of the molecule. , 1989, The Journal of biological chemistry.

[16]  C. L. Wang,et al.  Caldesmon has two calmodulin-binding domains. , 1989, Biochemical and biophysical research communications.

[17]  K. Morgan,et al.  Regulation of vascular smooth muscle tone by caldesmon. , 1992, The Journal of biological chemistry.

[18]  I. Fraser,et al.  Location of two contact sites between human smooth muscle caldesmon and Ca(2+)-calmodulin. , 1994, Journal of Biological Chemistry.

[19]  H. Huxley.  7 – MOLECULAR BASIS OF CONTRACTION IN CROSS-STRIATED MUSCLES , 1972 .

[20]  J. Bryan.  Caldesmon, acidic amino acids and molecular weight determinations , 1989, Journal of Muscle Research and Cell Motility.

[21]  S. Wong,et al.  A calmodulin-binding peptide of caldesmon. , 1991, Journal of Biological Chemistry.

[22]  J. Bryan,et al.  Sequence of an avian non-muscle caldesmon , 1991, Journal of Muscle Research & Cell Motility.

[23]  J. Bryan,et al.  Domain mapping of chicken gizzard caldesmon. , 1987, The Journal of biological chemistry.

[24]  P. Graceffa,et al.  Caldesmon exhibits a clustered distribution along individual chicken gizzard native thin filaments , 2004, Journal of Muscle Research & Cell Motility.

[25]  A. Gronenborn,et al.  Solution structure of a calmodulin-target peptide complex by multidimensional NMR. , 1994, Science.

[26]  K. Mabuchi,et al.  Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin , 1991, Journal of Muscle Research & Cell Motility.

[27]  K. Sobue,et al.  Primary structure and functional expression of h-caldesmon complementary DNA. , 1989, Biochemical and biophysical research communications.

[28]  K. Sobue,et al.  Isolation and characterization of a calmodulin binding fragment of chicken gizzard caldesmon. , 1987, Journal of biochemistry.

[29]  Shaobin Zhuang,et al.  Identification of the Functionally Relevant Calmodulin Binding Site in Smooth Muscle Caldesmon (*) , 1995, The Journal of Biological Chemistry.

[30]  R. Craig,et al.  Assembly of smooth muscle myosin into side-polar filaments , 1977, The Journal of cell biology.

[31]  P. Thibault,et al.  Phosphorylation of Caldesmon by p21-activated Kinase , 2000, The Journal of Biological Chemistry.

[32]  Steven B Marston,et al.  Caldesmon binds to smooth muscle myosin and myosin rod and crosslinks thick filaments to actin filaments , 1992, Journal of Muscle Research & Cell Motility.

[33]  A. Szpacenko,et al.  Functional domain of caldesmon , 1986, FEBS letters.

[34]  J. Bryan,et al.  A note on the caldesmon sequence , 1999, Journal of Muscle Research & Cell Motility.

[35]  S. Graether,et al.  Tryptophan residues in caldesmon are major determinants for calmodulin binding. , 1997, Biochemistry.

[36]  C. Dessy,et al.  Calmodulin levels are dynamically regulated in living vascular smooth muscle cells. , 2001, American journal of physiology. Heart and circulatory physiology.

[37]  V. Shirinsky,et al.  Caldesmon-calmodulin interaction. Study by the method of protein intrinsic tryptophan fluorescence. , 1988, The Biochemical journal.

[38]  K. Maruyama.  Birth of the sliding filament concept in muscle contraction. , 1995, Journal of biochemistry.

[39]  J. Trewhella,et al.  Calmodulin remains extended upon binding to smooth muscle caldesmon: a combined small-angle scattering and fourier transform infrared spectroscopy study. , 2000, Biochemistry.

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

[41]  S. Chacko,et al.  Mutagenesis Analysis of Functionally Important Domains within the C-terminal End of Smooth Muscle Caldesmon* , 1996, The Journal of Biological Chemistry.

[42]  F A Quiocho,et al.  Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. , 1992, Science.

[43]  A. Bretscher.  Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties. , 1984, The Journal of biological chemistry.

[44]  K. Mabuchi,et al.  Electron microscopic images suggest both ends of caldesmon interact with actin filaments , 1993, Journal of Muscle Research & Cell Motility.

[45]  Z. Grabarek,et al.  Calmodulin binds to caldesmon in an antiparallel manner. , 1997, Biochemistry.

[46]  Charles E. Bugg,et al.  Three-dimensional structure of calmodulin , 1985, Nature.

[47]  J. Derancourt,et al.  Characterization of the carboxyl-terminal 10-kDa cyanogen bromide fragment of caldesmon as an actin-calmodulin-binding region. , 1990, The Journal of biological chemistry.

[48]  R. Bagby,et al.  Ultrastructure, cytochemistry, and organization of myofilaments in vertebrate smooth muscle cells , 1990 .

[49]  C. Kay,et al.  Isolation and characterization of a novel molecular weight 11,000 Ca2(+)-binding protein from smooth muscle. , 1990, Biochemistry.

[50]  V. Dubowitz.  The Structure and Function of Muscle , 1974 .

[51]  J. Chalovich,et al.  Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin. , 1988, The Journal of biological chemistry.

[52]  D. Malencik,et al.  Calmodulin-linked equilibria in smooth muscle myosin light chain kinase. , 1986, Biochemistry.

[53]  K. Trybus,et al.  The effects of smooth muscle caldesmon on actin filament motility. , 1992, The Journal of biological chemistry.

[54]  M. Walsh,et al.  Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon. , 1984, The Journal of biological chemistry.

[55]  P. Graceffa,et al.  Caldesmon. Molecular weight and subunit composition by analytical ultracentrifugation. , 1988, The Journal of biological chemistry.

[56]  K. Morgan,et al.  Regulation of Vascular Smooth Muscle Tone by N-terminal Region of Caldesmon , 2000, The Journal of Biological Chemistry.

[57]  R. Moreland,et al.  Caldesmon inhibits active crossbridges in unstimulated vascular smooth muscle: an antisense oligodeoxynucleotide approach. , 1998, Circulation research.

[58]  J. Stull,et al.  Contractile elements and myosin light chain phosphorylation in myometrial tissue from nonpregnant and pregnant women. , 1993, The Journal of clinical investigation.

[59]  M. Dufau,et al.  Multiple and Tissue-specific Promoter Control of Gonadal and Non-gonadal Prolactin Receptor Gene Expression (*) , 1996, The Journal of Biological Chemistry.

[60]  K. Mabuchi,et al.  Heat Treatment Could Affect the Biochemical Properties of Caldesmon* , 1996, The Journal of Biological Chemistry.

[61]  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.