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. 1979 Nov 1;183(2):285–295. doi: 10.1042/bj1830285

Calmodulin-binding proteins from brain and other tissues.

R J Grand, S V Perry
PMCID: PMC1161557  PMID: 534497

Abstract

The calmodulin contents of rabbit brain, lung, kidney and liver, of bovine aorta and uterus, and of chicken gizzard have been determined. 2. The calmodulin in all of these tissues has been shown to be present in the form of very stable complexes with several other proteins. 3. A calmodulin-binding protein of mol.wt. 22 000 has been purified in high yield from bovine brain. It has been shown to interact with calmodulin and rabbit skeletal-muscle troponin C in a Ca2+-dependent manner. 4. The 22 000-mol.wt. protein inhibits the activation of bovine brain phosphodiesterase by calmodulin, but has very little affect on the activation of myosin light-chain kinase. 5. Calmodulin-binding proteins of mol.wts. 140000, 77000 and 61000 have also been partially purified from rabbit brain by affinity chromatography and have been shown to interact in a Ca2+-dependent manner with calmodulin. 6. The apparent molecular weights of the calmodulin-calmodulin-binding protein complexes, determined by gel filtration in the presence of 6M-urea, have been shown to be similar for most of the mammalian tissues examined. 7. By using 125I-labelled calmodulin, similar complexes have been demonstrated in rabbit skeletal muscle, although they are present at much lower concentrations.

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Selected References

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

  1. Baryłko B., Kuźnicki J., Drabikowski W. Identification of Ca2+-binding subunit of myosin light chain kinase from skeletal muscle with modulator protein. FEBS Lett. 1978 Jun 15;90(2):301–304. doi: 10.1016/0014-5793(78)80391-3. [DOI] [PubMed] [Google Scholar]
  2. Bolton A. E., Hunter W. M. The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Biochem J. 1973 Jul;133(3):529–539. doi: 10.1042/bj1330529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brostrom C. O., Huang Y. C., Breckenridge B. M., Wolff D. J. Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase. Proc Natl Acad Sci U S A. 1975 Jan;72(1):64–68. doi: 10.1073/pnas.72.1.64. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. CRUMPTON M. J., WILKINSON J. M. AMINO ACID COMPOSITIONS OF HUMAN AND RABBIT GAMMA-GLOBULINS AND OF THE FRAGMENTS PRODUCED BY REDUCTION. Biochem J. 1963 Aug;88:228–234. doi: 10.1042/bj0880228. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cheung W. Y. Cyclic 3',5'-nucleotide phosphodiesterase. Demonstration of an activator. Biochem Biophys Res Commun. 1970 Feb 6;38(3):533–538. doi: 10.1016/0006-291x(70)90747-3. [DOI] [PubMed] [Google Scholar]
  6. Cohen P., Burchell A., Foulkes J. G., Cohen P. T., Vanaman T. C., Nairn C. Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett. 1978 Aug 15;92(2):287–293. doi: 10.1016/0014-5793(78)80772-8. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Dedman J. R., Jackson R. L., Schreiber W. E., Means A. R. Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins. J Biol Chem. 1978 Jan 25;253(2):343–346. [PubMed] [Google Scholar]
  9. 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]
  10. Gopinath R. M., Vincenzi F. F. Phosphodiesterase protein activator mimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase. Biochem Biophys Res Commun. 1977 Aug 22;77(4):1203–1209. doi: 10.1016/s0006-291x(77)80107-1. [DOI] [PubMed] [Google Scholar]
  11. Grand R. J., Perry S. V., Weeks R. A. Troponin C-like proteins (calmodulins) from mammalian smooth muscle and other tissues. Biochem J. 1979 Feb 1;177(2):521–529. doi: 10.1042/bj1770521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. 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]
  14. Holroyde M. J., Chesher J. M., Trayer I. P., Walker D. G. Studies on the use of sepharose-N-(6-aminohexanoyl)-2-amino-2-deoxy-D-glucopyranose for the large-scale purification of hepatic glucokinase. Biochem J. 1976 Feb 1;153(2):351–361. doi: 10.1042/bj1530351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kakiuchi S., Yamazaki R. Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain studies on cyclic 3',5'-nucleotide phosphodiesterase (3). Biochem Biophys Res Commun. 1970 Dec 9;41(5):1104–1110. doi: 10.1016/0006-291x(70)90199-3. [DOI] [PubMed] [Google Scholar]
  16. Kato T., Kato Y., Kasai H., Okuyama T. Highly acidic proteins in bovine liver. J Biochem. 1977 Nov;82(5):1297–1305. doi: 10.1093/oxfordjournals.jbchem.a131817. [DOI] [PubMed] [Google Scholar]
  17. Klee C. B. Conformational transition accompanying the binding of Ca2+ to the protein activator of 3',5'-cyclic adenosine monophosphate phosphodiesterase. Biochemistry. 1977 Mar 8;16(5):1017–1024. doi: 10.1021/bi00624a033. [DOI] [PubMed] [Google Scholar]
  18. Klee C. B., Krinks M. H. Purification of cyclic 3',5'-nucleotide phosphodiesterase inhibitory protein by affinity chromatography on activator protein coupled to Sepharose. Biochemistry. 1978 Jan 10;17(1):120–126. doi: 10.1021/bi00594a017. [DOI] [PubMed] [Google Scholar]
  19. Lin Y. M., Liu Y. P., Cheung W. Y. Cyclic 3':5'-nucleotide phosphodiesterase. Purification, characterization, and active form of the protein activator from bovine brain. J Biol Chem. 1974 Aug 10;249(15):4943–4954. [PubMed] [Google Scholar]
  20. Mann K. G., Fish W. W. Protein polypeptide chain molecular weights by gel chromatography in guanidinium chloride. Methods Enzymol. 1972;26:28–42. doi: 10.1016/s0076-6879(72)26004-9. [DOI] [PubMed] [Google Scholar]
  21. Nairn A. C., Perry S. V. Calmodulin and myosin light-chain kinase of rabbit fast skeletal muscle. Biochem J. 1979 Apr 1;179(1):89–97. doi: 10.1042/bj1790089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Perry S. V., Cole H. A. Phosphorylation of troponin and the effects of interactions between the components of the complex. Biochem J. 1974 Sep;141(3):733–743. doi: 10.1042/bj1410733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Pires E. M., Perry S. V. Purification and properties of myosin light-chain kinase from fast skeletal muscle. Biochem J. 1977 Oct 1;167(1):137–146. doi: 10.1042/bj1670137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Sanui H. Measurement of inorganic orthophosphate in biological materials: extraction properties of butyl acetate. Anal Biochem. 1974 Aug;60(2):489–504. doi: 10.1016/0003-2697(74)90259-0. [DOI] [PubMed] [Google Scholar]
  25. Syska H., Perry S. V., Trayer I. P. A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle. FEBS Lett. 1974 Apr 1;40(2):253–257. doi: 10.1016/0014-5793(74)80238-3. [DOI] [PubMed] [Google Scholar]
  26. Tanford C. Protein denaturation. Adv Protein Chem. 1968;23:121–282. doi: 10.1016/s0065-3233(08)60401-5. [DOI] [PubMed] [Google Scholar]
  27. Teo T. S., Wang J. H. Mechanism of activation of a cyclic adenosine 3':5'-monophosphate phosphodiesterase from bovine heart by calcium ions. Identification of the protein activator as a Ca2+ binding protein. J Biol Chem. 1973 Sep 10;248(17):5950–5955. [PubMed] [Google Scholar]
  28. Waisman D. M., Stevens F. C., Wang J. H. Purification and characterization of a Ca2+-binding protein in Lumbricus terrestris. J Biol Chem. 1978 Feb 25;253(4):1106–1113. [PubMed] [Google Scholar]
  29. Waisman D., Stevens F. C., Wang J. H. The distribution of the Ca++-dependent protein activator of cyclic nucleotide phosphodiesterase in invertebrates. Biochem Biophys Res Commun. 1975 Aug 4;65(3):975–982. doi: 10.1016/s0006-291x(75)80481-5. [DOI] [PubMed] [Google Scholar]
  30. Wallace R. W., Lynch T. J., Tallant E. A., Cheung W. Y. An endogenous inhibitor protein of brain adenylate cyclase and cyclic nucleotide phosphodiesterase. Arch Biochem Biophys. 1978 Apr 30;187(2):328–334. doi: 10.1016/0003-9861(78)90042-5. [DOI] [PubMed] [Google Scholar]
  31. 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]
  32. 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]
  33. 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]
  34. 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]
  35. Wilkinson J. M. The preparation and properties of the components of troponin B. Biochim Biophys Acta. 1974 Aug 8;359(2):379–388. doi: 10.1016/0005-2795(74)90238-4. [DOI] [PubMed] [Google Scholar]
  36. 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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