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Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein

  • Published:
Bioscience Reports

Abstract

The sensitivity of tissue transglutaminase to activation by Ca2+ and other cellular factors was investigated using the enzyme purified from rat liver. The inclusion of Mg2+ in the assay system appeared to reduce the Ca2+-requirement of the enzyme when native N,N′-dimethylcasein was used as the protein acceptor substrate. However, when this protein was dephosphorylated, the Ca2+-requirement was unaffected by Mg2+. In addition, using this modified assay, a Km for Ca2+ was calculated to be in the range of 3–4 μM, at least an order of magnitude lower than that obtained with native acceptor substrate. Membrane phospholipids, 1,2-diolein and calmodufin were found not to affect the activation oftransglutaminase by Ca2+. The sensitivity of transglutaminase to Ca2+ which we have now demonstrated suggests that this enzyme may directly act as a receptor protein for Ca2+ during stimulusresponse coupling mediated by this cation.

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References

  • Barnes RN, Bungay PJ, Elliott BM, Walton PL & Griffin M (1985a) Carcinogenesis6, 459–463.

    PubMed  Google Scholar 

  • Barnes RN, Walton PL & Griffin M (1985b) Biochem. Soc. Transact.13, 227–228.

    Google Scholar 

  • Beaven MA, Rogers J, Moore JP, Hesketh TR, Smith GA & Metcalfe JC (1984) J. Biol. Chem.259, 7129–7136.

    PubMed  Google Scholar 

  • Birckbichler PJ, Orr GR & Patterson MK (1976) Cancer Res.36, 2911–2914.

    PubMed  Google Scholar 

  • Brocklehurst KW & Hutton JC (1984) Biochem. J.220, 283–290.

    PubMed  Google Scholar 

  • Bruce SE, Shah T & Peters TJ (1983) Biochem. Soc. Transact.11, 777.

    Google Scholar 

  • Bungay PJ, Potter JM & Griffin M (1984a) Biochem. J.219, 819–827.

    PubMed  Google Scholar 

  • Bungay PJ, Potter JM & Griffin M (1984b) Biosci. Rep.4, 869–877.

    PubMed  Google Scholar 

  • Cheung WY (1980) Science207, 19–27.

    PubMed  Google Scholar 

  • Cooke RD & Holbrook JJ (1974) Biochem. J.141, 71–78.

    PubMed  Google Scholar 

  • Davies PJA, Davies DR, Levitzki A, Maxfield FR, Milhaud P, Willingham MC & Pastan IH (1980) Nature283, 162–167.

    PubMed  Google Scholar 

  • Folk JE & Finlayson JS (1977) Adv. Prot. Chem.31, 1–133.

    Google Scholar 

  • Gomis R, Sener A, Malaisse-Lagae F & Malaisse WJ (1983) Biochim. Biophys. Acta760, 384–388.

    PubMed  Google Scholar 

  • Griffin M, Barnes RN, Wynne J & Williams C (1978) Biochem. Pharmacol.27, 1211–1219.

    PubMed  Google Scholar 

  • Griffin M, Smith LL & Wynne J (1979) Br. J. Exp. Path.60, 653–661.

    Google Scholar 

  • Julian C, Speck NA & Pierce SK (1983) J. Immunol.130, 91–96.

    PubMed  Google Scholar 

  • Klee CB, Crouch TH & Richman PG (1980) Ann. Rev. Biochem.49, 489–515.

    PubMed  Google Scholar 

  • Koenig H, Goldstone A & Lu CY (1983) Nature (London)305, 530–534.

    Google Scholar 

  • Lorand L & Conrad SM (1984) Mol. Cell Biochem.58, 9–36

    PubMed  Google Scholar 

  • Lorand L, Campbell-Wilkes LK and Cooperstein L (1972) Anal. Biochem.50, 623–631.

    PubMed  Google Scholar 

  • LaPort DE, Wierman BN & Storm DR (1980) Biochemistry19, 3814–3819.

    PubMed  Google Scholar 

  • Rasmussen H & Barret PQ (1984) Physiol. Rev.64, 938–984.

    PubMed  Google Scholar 

  • Schatzmann JH (1973) J. Physiol. (London)235, 551–569.

    Google Scholar 

  • Takai Y, Kishimoto A, Kawahara Y, Minakuchi R, Sano K, Kikkawa U, Mori T, Yu B, Kaibuchi K & Nishizuka Y (1981) Adv. Cyclic Nucleotide Res.14, 301–313.

    PubMed  Google Scholar 

  • Veloso D, Guynn RW, Oskarsson M & Veech RL (1973) J. Biol. Chem.248, 4811–4819.

    PubMed  Google Scholar 

  • Wise BC, Raynor RL & Kuo JF (1982) J. Biol. Chem.257, 8481–8488.

    PubMed  Google Scholar 

Download references

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Authors and Affiliations

  1. Department of Life Sciences, Trent Polytechnic, Clifton Lane, NG11 8NS, Nottingham, UK

    D. Hand, P. J. Bungay & M. Griffin

  2. Central Toxicology Laboratory, Imperial Chemical Industries PLC, Alderley Park, SK10 4TJ, Macclesfield, UK

    B. M. Elliott

Authors
  1. D. Hand
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  2. P. J. Bungay
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  3. B. M. Elliott
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  4. M. Griffin
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Hand, D., Bungay, P.J., Elliott, B.M. et al. Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein. Biosci Rep 5, 1079–1086 (1985). https://doi.org/10.1007/BF01119629

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  • DOI: https://doi.org/10.1007/BF01119629

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