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. 1979 Feb 1;177(2):521–529. doi: 10.1042/bj1770521

Troponin C-like proteins (calmodulins) from mammalian smooth muscle and other tissues.

R J Grand, S V Perry, R A Weeks
PMCID: PMC1186402  PMID: 435249

Abstract

1. An acidic protein with properties similar to those of troponin C from rabbit skeletal muscle has been shown to be present in bovine and rabbit smooth muscles, chicken gizzard and rabbit liver, kidney and lung. 2. A simple new method involving the use of organic solvents is described for the purification of the troponin C-like proteins from various tissues. 3. The troponin C-like proteins can be distinguished from rabbit skeletal-muscle toponin C by their electrophoretic behaviour on polyacrylamide gels at pH 8.3 in the presence and absence of Ca2+. The troponin C-like proteins have been shown to form complexes with rabbit skeletal-muscle troponin I that migrate on electrophoresis in polyacrylamide gels. 4. Behaviour on electrophoresis, amino acid analysis and the patterns of CNBr digests on polyacrylamide gels indicate that the troponin C-like proteins from bovine uterus and aorta, rabbit uterus, and liver and chicken gizzard are very similar to, if not identical with, bovine brain modulator protein. 5. With bovine cardiac muscle the organic-solvent method yields a preparation consisting of roughly similar amounts of troponin C and troponin C-like protein. 6. By the isotope-dilution technique, troponin C-like protein has been shown to represent 0.42% of the total protein in rabbit uterus. 7. In homogenates of smooth muscle, rabbit lung, kidney and brain, the troponin C-like proteins form a complex with other protein (or proteins) that requires Ca2+ for its formation and that is not dissociated in 9M-urea.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aksoy M. O., Williams D., Sharkey E. M., Hartshorne D. J. A relationship between Ca2+ sensitivity and phosphorylation of gizzard actomyosin. Biochem Biophys Res Commun. 1976 Mar 8;69(1):35–41. doi: 10.1016/s0006-291x(76)80268-9. [DOI] [PubMed] [Google Scholar]
  2. Amphlett G. W., Vanaman T. C., Perry S. V. Effect of the troponin C-like protein from bovine brain (brain modulator protein) on the Mg2+-stimulated ATPase of skeletal muscle actinomyosin. FEBS Lett. 1976 Dec 15;72(1):163–168. doi: 10.1016/0014-5793(76)80836-8. [DOI] [PubMed] [Google Scholar]
  3. Bremel R. D. Myosin linked calcium regulation in vertebrate smooth muscle. Nature. 1974 Nov 29;252(5482):405–407. doi: 10.1038/252405a0. [DOI] [PubMed] [Google Scholar]
  4. Carsten M. E. Uterine smooth muscle: troponin. Arch Biochem Biophys. 1971 Nov;147(1):353–357. doi: 10.1016/0003-9861(71)90346-8. [DOI] [PubMed] [Google Scholar]
  5. Collins J. H. Homology of myosin light chains, troponin-C and parvalbumins deduced from comparison of their amino acid sequences. Biochem Biophys Res Commun. 1974 May 7;58(1):301–308. doi: 10.1016/0006-291x(74)90927-9. [DOI] [PubMed] [Google Scholar]
  6. Dabrowska R., Sherry J. M., Aromatorio D. K., Hartshorne D. J. Modulator protein as a component of the myosin light chain kinase from chicken gizzard. Biochemistry. 1978 Jan 24;17(2):253–258. doi: 10.1021/bi00595a010. [DOI] [PubMed] [Google Scholar]
  7. Ebashi S., Toyo-Oka T., Nonmura Y. Gizzard Troponin. J Biochem. 1975 Oct;78(4):859–861. doi: 10.1093/oxfordjournals.jbchem.a130976. [DOI] [PubMed] [Google Scholar]
  8. Ebashi S., Wakabayashi T., Ebashi F. Troponin and its components. J Biochem. 1971 Feb;69(2):441–445. doi: 10.1093/oxfordjournals.jbchem.a129486. [DOI] [PubMed] [Google Scholar]
  9. Fine R., Lehman W., Head J., Blitz A. Troponin C in brain. Nature. 1975 Nov 20;258(5532):260–267. doi: 10.1038/258260a0. [DOI] [PubMed] [Google Scholar]
  10. Head J. F., Perry S. V. The interaction of the calcium-binding protein (troponin C) with bivalent cations and the inhibitory protein (troponin I). Biochem J. 1974 Feb;137(2):145–154. doi: 10.1042/bj1370145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Head J. F., Weeks R. A., Perry S. V. Affinity-chromatographic isolation and some properties of troponin C from different muscle types. Biochem J. 1977 Mar 1;161(3):465–471. doi: 10.1042/bj1610465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kuehl W. M., Adelstein R. S. Identification of epsilon-N-monomethyllysine and epsilon-N-trimethyllysine in rabbit skeletal myosin. Biochem Biophys Res Commun. 1969 Sep 24;37(1):59–65. doi: 10.1016/0006-291x(69)90880-8. [DOI] [PubMed] [Google Scholar]
  13. March S. C., Parikh I., Cuatrecasas P. A simplified method for cyanogen bromide activation of agarose for affinity chromatography. Anal Biochem. 1974 Jul;60(1):149–152. doi: 10.1016/0003-2697(74)90139-0. [DOI] [PubMed] [Google Scholar]
  14. Mikawa T., Toyo-oka T., Nonomura Y., Ebashi S. Essential factor of gizzard "troponin" fraction. A new type of regulatory protein. J Biochem. 1977 Jan;81(1):273–275. doi: 10.1093/oxfordjournals.jbchem.a131447. [DOI] [PubMed] [Google Scholar]
  15. Sobieszek A., Bremel R. D. Preparation and properties of vertebrate smooth-muscle myofibrils and actomyosin. Eur J Biochem. 1975 Jun 16;55(1):49–60. doi: 10.1111/j.1432-1033.1975.tb02137.x. [DOI] [PubMed] [Google Scholar]
  16. Sparrow M. P., van Bockxmeer F. M. Arterial tropomyosin and a relaxing protein fraction from vascular smooth muscle. Comparison with skeletal tropomyosin and troponin. J Biochem. 1972 Nov;72(5):1075–1080. doi: 10.1093/oxfordjournals.jbchem.a129993. [DOI] [PubMed] [Google Scholar]
  17. Stevens F. C., Walsh M., Ho H. C., Teo T. S., Wang J. H. Comparison of calcium-binding proteins. Bovine heart and brain protein activators of cyclic nucleotide phosphodiesterase and rabbit skeletal muscle troponin C. J Biol Chem. 1976 Aug 10;251(15):4495–4500. [PubMed] [Google Scholar]
  18. Teo T. S., Wang T. H., Wang J. H. Purification and properties of the protein activator of bovine heart cyclic adenosine 3',5'-monophosphate phosphodiesterase. J Biol Chem. 1973 Jan 25;248(2):588–595. [PubMed] [Google Scholar]
  19. Wang J. H., Desai R. Modulator binding protein. Bovine brain protein exhibiting the Ca2+-dependent association with the protein modulator of cyclic nucleotide phosphodiesterase. J Biol Chem. 1977 Jun 25;252(12):4175–4184. [PubMed] [Google Scholar]
  20. Watterson D. M., Harrelson W. G., Jr, Keller P. M., Sharief F., Vanaman T. C. Structural similarities between the Ca2+-dependent regulatory proteins of 3':5'-cyclic nucleotide phosphodiesterase and actomyosin ATPase. J Biol Chem. 1976 Aug 10;251(15):4501–4513. [PubMed] [Google Scholar]
  21. Watterson D. M., Vanaman T. C. Affinity chromatography purification of a cyclic nucleotide phosphodiesterase using immobilized modulator protein, a troponin C-like protein from brain. Biochem Biophys Res Commun. 1976 Nov 8;73(1):40–46. doi: 10.1016/0006-291x(76)90494-0. [DOI] [PubMed] [Google Scholar]
  22. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  23. Wilkinson J. M., Perry S. V., Cole H. A., Trayer I. P. The regulatory proteins of the myofibril. Separation and biological activity of the components of inhibitory-factor preparations. Biochem J. 1972 Mar;127(1):215–228. doi: 10.1042/bj1270215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Yagi K., Yazawa M., Kakiuchi S., Ohshima M., Uenishi K. Identification of an activator protein for myosin light chain kinase as the Ca2+-dependent modulator protein. J Biol Chem. 1978 Mar 10;253(5):1338–1340. [PubMed] [Google Scholar]

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