Calmodulin-like Ca2+-Binding Proteins of Smooth Muscle

  • Gwyneth De Vries
  • John R. McDonald
  • Michael P. Walsh
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)


Ca2+ ions serve as intracellular messengers mediating the effects of a variety of extracellular signals (hormones, neurotransmitters, growth factors, etc.) in eliciting appropriate physio logical responses (Carafoli and Penniston, 1985). For example, the neurotransmitter acetylcholine causes an elevation of cytosolic [Ca2+ ] in smooth muscle leading to contraction. The effects of Ca2+ ions are mediated by a number of Ca2+ -binding proteins (Kretsinger, 1980). Calmodulin is one such Ca2+ -binding protein which responds to physiological [Ca2+ ] transients by binding Ca2+ and undergoing a conformational change (Klee, 1977) which includes exposure of a hydrophobic site(s) (LaPorteet al., 1980; Tanaka and Hidaka, 1980). In this altered conformation, calmodulin can interact with a target enzyme, e.g., myosin light-chain kinase of smooth muscle (Walsh, 1985). Usually, such interaction converts the target enzyme from an inactive to an active state, triggering a cascade of biochemical reactions (often protein phosphorylations) and leading ultimately to the desired physiological response.


Bovine Brain Smooth Muscle Myosin cAMP Phosphodiesterase Chicken Gizzard Muscle Myosin Light Chain Kinase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Burgess, W. H., Jemiolo, D. K., and Kretsinger, R. H., 1980, Interaction of calcium and calmodulin in the presence of sodium dodecyl sulfate, Biochim. Biophys. Acta 623:257–270.PubMedGoogle Scholar
  2. Carafoli, E., and Penniston, J. T., 1985, The calcium signal, Sci. Am. 253(5):70–78.PubMedCrossRefGoogle Scholar
  3. Cheung, W. Y., 1971, Cyclic 3’, 5’-nucleotide phosphodiesterase. Evidence for and properties of a protein activator, J. Biol. Chem. 246:2859–2869.PubMedGoogle Scholar
  4. Geisow, M. J., and Walker, J. H., 1986, New proteins involved in cell regulation by Ca2+ and phospholipids, Trends Biochem. Sci. 11:420–424.CrossRefGoogle Scholar
  5. Gopalakrishna, R., and Anderson, W. B., 1982, Ca2+ -induced hydrophobic site on calmodulin: Ap plication for purification of calmodulin by phenyl-Sepharose affinity chromatography, Biochem. Biophys. Res. Commun. 104:830–836.PubMedCrossRefGoogle Scholar
  6. Klee, C. B., 1977, Conformational transition accompanying the binding of Ca2+ to the protein activator of 3’, 5’-cyclic adenosine monophosphate phosphodiesterase, Biochemistry 16:1017–1024.PubMedCrossRefGoogle Scholar
  7. Kretsinger, R. H., 1980, Structure and evolution of calcium-modulated proteins, CRC Crit. Rev. Biochem. 8:119–174.PubMedCrossRefGoogle Scholar
  8. LaPorte, D. C., Wierman, B. M., and Storm, D. R., 1980, Calcium-induced exposure of hydrophobic surface on calmodulin, Biochemistry 19:3814–3819.PubMedCrossRefGoogle Scholar
  9. Manalan, A. S., and Klee, C. B., 1984, Purification and characterization of a novel Ca2+ -binding protein (CBP-18) from bovine brain, J. Biol. Chem. 259:2047–2050.PubMedGoogle Scholar
  10. Maruyama, K., Mikawa, T., and Ebashi, S., 1984, Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis, J. Biochem. 95:511–519.PubMedGoogle Scholar
  11. McDonald, J. R., and Walsh, M. P., 1985a, Ca2+ -binding proteins from bovine brain including a potent inhibitor of protein kinase C., Biochem. J. 232:559–567.PubMedGoogle Scholar
  12. McDonald, J. R., and Walsh, M. P., 1985b, Inhibition of the Ca2+ -and phospholipid-dependent protein kinase by a novel Mr 17,000 Ca2+ -binding protein, Biochem. Biophys. Res. Commun. 129:603–610.CrossRefGoogle Scholar
  13. McDonald, J. R., Walsh, M. P., McCubbin, W. D., Oikawa, K., and Kay, C. M., 1985, Ca2+ -binding proteins from bovine brain including a potent inhibitor of protein kinase C., Biochem. J. 232: 569–575.PubMedGoogle Scholar
  14. McDonald, J. R., Walsh, M. P., McCubbin, W. D., and Kay, C. M., 1987a, Isolation and characterization of novel 21 kDa Ca2 + -binding protein from bovine brain, Methods Enzymol. 139:88–105.PubMedCrossRefGoogle Scholar
  15. McDonald, J. R., Gröschel-Stewart, U., and Walsh, M. P., 1987b, Properties and distribution of the protein inhibitor (Mr 17000) of protein kinase C., Biochem. J. 242:695–705.PubMedGoogle Scholar
  16. Ngai, P. K., Carruthers, C. A., and Walsh, M. P., 1984, Isolation of the native form of chicken gizzard myosin light-chain kinase, Biochem. J. 218:863–870.PubMedGoogle Scholar
  17. Ngai, P. K., Scott-Woo, G. C., Lim, M. S., Sutherland, C., and Walsh, M. P., 1987, Activation of smooth muscle myosin Mg24-ATPase by native thin filaments and actin/tropomyosin, J. Biol. Chem. 262:5352–5359.PubMedGoogle Scholar
  18. Sharma, R. K., Taylor, W. A., and Wang, J. H., 1983, Use of calmodulin affinity chromatography for purification of specific calmodulin-dependent enzymes, Methods Enzymol. 102:210–219.PubMedCrossRefGoogle Scholar
  19. Tanaka, T., and Hidaka, H., 1980, Hydrophobic regions function in calmodulin-enzyme(s) interactions, J. Biol. Chem. 255:11078–11080.PubMedGoogle Scholar
  20. Teo, T. S., Wang, T. H., and Wang, J. H., 1973, Purification and properties of the protein activator of bovine heart cyclic adenosine 3’,5’-monophosphate phosphodiesterase, J. Biol. Chem. 248: 588–595.PubMedGoogle Scholar
  21. Walsh, M. P., 1985, Calcium regulation of smooth muscle contraction, in Calcium and Cell Physiology (D. Marmé, ed.), Springer-Verlag, Berlin, pp. 170–203.CrossRefGoogle Scholar
  22. Walsh, M. P., Hinkins, S., Dabrowska, R., and Hartshorne, D. J., 1983, Smooth muscle myosin light chain kinase, Methods Enzymol. 99:279–288.PubMedCrossRefGoogle Scholar
  23. Walsh, M. P., Valentine, K. A., Ngai, P. K., Carruthers, C. A., and Hollenberg, M. D., 1984, Ca2+ -dependent hydrophobic-interaction chromatography. Isolation of a novel Ca2+ -binding protein and protein kinase C from bovine brain, Biochem. J. 224:117–127.PubMedGoogle Scholar
  24. Watterson, D. M., Harrelson, W. G., Jr., Keller, P. M., Sharief, F., and Vanaman, T. C., 1976, Structural similarities between the Ca2+ -dependent regulatory proteins of 3’:5’-cyclic nucleotide phosphodiesterase and actomyosin ATPase, J. Biol. Chem. 251:4501–4513.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Gwyneth De Vries
    • 1
  • John R. McDonald
    • 1
  • Michael P. Walsh
    • 1
  1. 1.Department of Medical BiochemistryUniversity of CalgaryCalgaryCanada

Personalised recommendations