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2002 | 49 | 2 | 471-479
Article title

Insight into the kinetics and the mode of the interaction between smooth muscle calponin and F-actin.

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EN
Abstracts
EN
Kinetics of the smooth muscle calponin-F-actin interaction was studied by stopped- flow measurements of light scattering and fluorescence intensity of pyrene-labelled F-actin. The intensity and character of the changes in light scattering, and thus the mode of calponin binding to actin filaments leading to changes in their shape and bundling, depend on the molar ratio of the two proteins. Parallel measurements of pyrene-fluorescence quenching upon calponin binding revealed that intrinsic conformational changes in actin filaments are delayed relative to the binding process and are not markedly influenced by the mode of calponin binding. Bundling of actin filaments by calponin was not correlated with fluorescence changes and thus with alterations in the structure of actin filaments.
Publisher

Year
Volume
49
Issue
2
Pages
471-479
Physical description
Dates
published
2002
received
2002-03-12
accepted
2002-03-27
Contributors
  • Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warszawa, Poland
  • Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warszawa, Poland
References
  • Barshop BA, Wren RF, Frieden C. (1983) Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM-a flexible, portable system. Anal Biochem.; 130: 134-45.
  • Bartegi A, Roustan C, Kassab R, Fattoum A. (1999) Fluorescence studies of the carboxyl- terminal domain of smooth muscle calponin effects of F-actin and salts. Eur J Biochem.; 262: 335-41.
  • Borovikov YuS, Horiuchi KY, Avrova SV, Chacko S. (1996) Modulation of actin conformation and inhibition of actin filament velocity by calponin. Biochemistry.; 35: 13849-57.
  • Cantor CR, Schimmel PR. (1980) Biophysical chemistry. Part III. In The behaviour of biological macromolecules. Freeman WH, Company, pp 887-937, San Francisco.
  • Cooper JA, Walker SB, Pollard TP. (1983) Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J Muscle Res Cell Motil.; 4: 253-62.
  • El-Mezgueldi M, Marston SB. (1996) The effect of smooth muscle calponin on the strong and weak myosin-binding sites of F-actin. J Biol Chem.; 271: 28161-7.
  • El-Mezgueldi M, Fattoum A, Derancourt J, Kassab R. (1992) Mapping of the functional domains in the amino-terminal region of calponin. J Biol Chem.; 267: 15943-51.
  • El-Mezgueldi M, Mendre C, Calas B, Kassab R, Fattoum A. (1995) Characterization of the regulatory domain of gizzard calponin. Interactions of the 145-163 region with F-actin, calcium-binding proteins, and tropomyosin. J Biol Chem.; 270: 8867-76.
  • El-Mezgueldi M, Strasser P, Fattoum A, Gimona M. (1996) Expressing functional domains of mouse calponin: involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin. Biochemistry.; 35: 3654-61.
  • Hodgkinson JL, El-Mezgueldi M, Craig R, Vibert P, Marston SB, Lehman W. (1997) 3-D image reconstruction of reconstituted smooth muscle thin filaments containing calponin: visualization of interactions between F-actin and calponin. J Mol Biol.; 273:150-9.
  • Houk T, Ue K. (1974) The measurement of actin concentration in solution: a comparison of methods. Anal Biochem.; 62: 66-74.
  • Itoh T, Suzuki A, Watanabe Y, Mino T, Naka M, Tanaka T. (1995) A calponin peptide enhances Ca2+ sensitivity of smooth muscle contraction without affecting myosin light chain phosphorylation. J Biol Chem.; 270: 20400-3.
  • Kołakowski J, Karkucińska A, Dąbrowska R. (1997) Calponin inhibits actin-activated MgATPase of myosin subfragment 1 (S1) without displacing S1 from its binding site on actin. Eur J Biochem.; 243: 624-9.
  • Kołakowski J, Makuch R, Stępkowski D, Dąbrowska R. (1995) Interaction of calponin with actin and its functional implications. Biochem J.; 306: 199-204.
  • Kouyama T, Mihashi K. (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem.; 114: 33-8.
  • Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
  • Leinweber B, Tang JX, Stafford WF, Chalovich JM. (1999) Calponin interaction with alpha- actinin-actin: evidence for a structural role for calponin. Biophys J.; 77: 3208-17.
  • Lu FW, Freedman MV, Chalovich JM. (1995) Characterization of calponin binding to actin. Biochemistry.; 34: 11864-71.
  • Mabuchi KLiY, Tao T, Wang CL. (1996) Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle. J Muscle Res Cell Motil.; 17: 243-60.
  • Mino T, Yuasa U, Nakamura F, Naka M, Tanaka T. (1998) Two distinct actin-binding sites of smooth muscle calponin. Eur J Biochem.; 251: 262-8.
  • Noda S, Ito M, Watanabe S, Takahashi K, Maruyama K. (1992) Conformational changes of actin induced by calponin. Biochem Biophys Res Commun.; 185: 481-7.
  • North AJ, Gimona M, Cross RA, Small JV. (1994) Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells. J Cell Sci.; 107: 437-44.
  • Spudich JA, Watt S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem.; 246: 4866-71.
  • Stafford WF, Mabuchi K, Takahashi K, Tao, T. (1995) Physical characterization of calponin. A circular dichroism, analytical ultracentrifuge, and electron microscopy study. J Biol Chem.; 270: 10576-9.
  • Szymanski PT, Grabarek Z, Tao T. (1997) Correlation between calponin and myosin subfragment 1 binding to F-actin and ATPase inhibition. Biochem J.; 321: 519-23.
  • Takahashi K, Hiwada K, Kokubu T. (1986) Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle. Biochem Biophys Res Commun.; 141: 20-6.
  • Tang JX, Szymanski PT, Janmey PA, Tao T. (1997) Electrostatic effects of smooth muscle calponin on actin assembly. Eur J Biochem.; 247: 432-40.
  • Walsh MP, Carmichael JD, Kargacin, G J. (1993) Characterization and confocal imaging of calponin in gastrointestinal smooth muscle. Am J Physiol.; 265: C1371-8.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv49i2p471kz
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