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Modulation of Cellular Transglutaminase: Protease-Induced Activation

  • Soo I. Chung
  • Sung Keun Chang
  • Enzo T. Cocuzzi
  • J. E. Folk
  • Hee Chul Kim
  • Soo Young Lee
  • Nadine Martinet
  • T. Nigra
  • Hee Sik Sun
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)

Summary

Multiple molecular forms of transglutaminase are found in cells and each form is widely distributed. We find a 95 K dalton enzyme associated with membrane fractions. A 50 K dalton enzyme occurs primarily in epidermis and hair follicles. Cells after treatment with proteases show greater transglutaminase activity. The activated enzyme in rat chondrosarcoma cells is one of 95 K daltons, whereas mouse epidermal cells and rabbit endometrium cells after protease activation display enzymes of both 95 K daltons and 50 K daltons. The 95 K dalton enzyme, but not that of 80 K daltons, can be activated by proteases or sulfhydryl compounds after cell lysis. In cells that undergo terminal differentiation, e.g., reticulocytes, megakaryocytes, monocytes, chondrocytes, and epidermal cells, the forms of transglutaminase are modulated. Our findings suggest that these modulations in differentiating cells are the results of transglutaminase post-translational modifications that cause pronounced changes in catalytic activity.

Keywords

Hair Follicle Factor Xiii Chondrosarcoma Cell Protease Treatment Mouse Epidermis 
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.

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References

  1. Anfinson, C.B. (1973) Principles that govern the folding of protein chains, Science 181, 223–230.CrossRefGoogle Scholar
  2. Birckbichler, P.J., Orr, G.R., Conway, E., and Patterson, M.K. Jr. (1977) Transglutaminase activity in normal and transformed cells, Cancer Res. 37, 1340–1344.PubMedGoogle Scholar
  3. Buluk, K., Januszko, T., and Olbromski, J. (1961) Conversion of fibrin to desmofibrin, Nature 191, 1093–1094.CrossRefGoogle Scholar
  4. Bures, D.M., and Goldsmith, L.A. (1978) Localization of transglutaminase in adult chicken epidermis, Arch. Dermatol. Res. 262, 329–332.PubMedCrossRefGoogle Scholar
  5. Buxman, M.M., and Wuepper, K.D. (1975) Isolation, purification and characterization of bovine epidermal transglutaminase, Biochin. Biophys. Acta 452, 356–359.CrossRefGoogle Scholar
  6. Chang, S.K., and Chung, S.I. (1986) Cellular Transglutaminase. The particulate-associated transglutaminase from chondrosarcoma and liver: partial purification and characterization, J. Biol. Chem. 261, 8112–8127.PubMedGoogle Scholar
  7. Chung, S.I., and Folk, J.E. (1972) Transglutaminase from hair follicle of guinea pig, Proc. Natl. Acad. Sci. USA 69, 303–307.PubMedCrossRefGoogle Scholar
  8. Chung, S.I. (1972) Comparative studies on tissue transglutaminase and factor XIII, Ann. N.Y. Acad. Sci. 202, 240–255.PubMedCrossRefGoogle Scholar
  9. Chung, S.I. (1975) Multiple molecular forms of transglutaminases in human and guinea pig, in Isozymes (Market, C.L. ed.) Vol. I, Molecular Structure, pp. 259–274, Academic Press NY.CrossRefGoogle Scholar
  10. Clark, D.D., Mycek, M.J., Neidle, A., and Waelsh, H. (1959) The incorporation of amines into proteins, Arch. Biochem. Biophys. 79, 338–354.CrossRefGoogle Scholar
  11. Cocuzzi, E.T., and Chung, S.I. (1986) Cellular Transglutaminase. Lung matrix-associated transglutaminase: characterization and activation with sulfhydryls, J. Biol. Chem. 261, 8122–8127.PubMedGoogle Scholar
  12. Folk, J.E., and Cole, P.W. (1966) Identification of a functional cysteine essential for the activity of guinea pig liver transglutaminase, J. Biol. Chem. 241, 3238–3240.PubMedGoogle Scholar
  13. Folk, J.E., and Chung, S.I. (1973) Molecular and catalytic properties of transglutaminases, Advances in Enzymol. 38 109–191.Google Scholar
  14. Folk, J.E., and Finlayson, J.S. (1979) The ε-(γ-glutamyl)lysine cross-link and the catalytic role of transglutaminase, Adv. Protein Chem. 31, 1–133.Google Scholar
  15. Folk, J.E., Park, M.H., Chung, S.I., Schrode, J., Lester, E.P., and Cooper, H.L. (1980) Polyamines as physiological substrates for transglutaminases, J. Biol. Chem. 255, 3695–3700.PubMedGoogle Scholar
  16. Folk, J.E. (1980) Transglutaminase, Ann. Rev. Biochem. 49, 517–531.PubMedCrossRefGoogle Scholar
  17. Folk, J.E. (1983) Mechanism and basis for specificity of transglutaminase-catalyzed ε-(γ-glutamyl)lysine bond formation, Adv. Enzymol. 54, 1–54.PubMedGoogle Scholar
  18. Goldknopf, I.L., and Busch, H. (1977) Isopeptide-linkage between non-histone and histone 2A polypeptides of chromosomal conjugateprotein A24, Proc. Natl. Acad. Sci. USA 74, 864–868.PubMedCrossRefGoogle Scholar
  19. Gross, A.J., and Sizer, I.W. (1959) The oxidation of tyramine, tyrosine, and related compounds by peroxidase, J. Biol. Chem. 234, 1611–1614.PubMedGoogle Scholar
  20. Lichiti, U., Ben, T., and Yuspa, S.H. (1985) Retinoic acid-induced transglutaminase in mouse epidermal cells is distinct from epidermal transglutaminase, J. Biol. Chem. 260, 1422–1426.Google Scholar
  21. Loewy, A.G. (1984) The Nε -(-γ-glutamic)lysine cross-link: methods of analysis, occurrence in extracellular and cellular proteins, Methods in Enzymol. 107, 241–257.Google Scholar
  22. Lorand, L., Downey, J., Gotoh, T., Jacobson, A., and Tokura, S. (1968) The transpeptidase system which cross-links fibrin by γ-glutamyl-ε-lysine bonds, Biochem. Biophys. Res. Comm. 31, 222–230.PubMedCrossRefGoogle Scholar
  23. Lou, M.F. (1975) Isolation and identification of L-β-aspartyl-L-lysine and L-γ-glutamyl-L-ornithine from normal human urine, Biochemistry, 14, 3503–3508.PubMedCrossRefGoogle Scholar
  24. Matacic, S.S., and Loewy, A.G. (1968) Identification of isopeptide cross-links in insoluble fibrin, Biochem. Biophys. Res. Commun. 30, 356–362.PubMedCrossRefGoogle Scholar
  25. Neurath, H., and Walsh, K.A. (1976) Role of proteolytic enzymes in biological regulation (a review), Proc. Natl. Acad. Sci. USA 73, 3825–3832.PubMedCrossRefGoogle Scholar
  26. Ogawa, H., and Goldsmith, L.A. (1976) Human epidermal transglutaminase; preparation and properties, J. Biol. Chem, 251, 7281–7288.PubMedGoogle Scholar
  27. Pisano, J.J., Finlayson, J.S., and Peyton, M.P. (1968) Cross-link in fibrin polymerized by factor XIII: ε(γ-glutamyl)lysine, Science 160, 892–893.PubMedCrossRefGoogle Scholar
  28. Reich, E., Rifkin, D.B., and Shaw, E. ed. (1975) Proteases and biological control, in Cold Spring Harbor Conferences on Cell Proliferation, Vol. 2, Cold Spring Harbor Laboratory.Google Scholar
  29. Rogers, G., Martinet, N., Steinert, P., Wynn, P., Roop, D., Kilkenney, M.S., Morgan, D., and Yuspa, H. (1987) Cultivation of murine hair follicles as organoids in collagen matrix, J. Invest. Dermat. in press.Google Scholar
  30. Takagi, T., and Doolittle, R.F. (1974) Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin, Biochemistry 13, 750–756.PubMedCrossRefGoogle Scholar
  31. Tanzer, M.L. (1976) Cross-linking, in Biochemistry of Collagen, Ramanchandran, G.N. and Reddi, A.H. eds. Plenum, NY, pp. 137.CrossRefGoogle Scholar
  32. Thacher, S.M., and Rice, R.H. (1985) Keratinocyte-specific transglutaminase of cultured human epidermal cells: relation to cross-linked envelope formation and terminal differentiation, Cell 40, 685–695.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Soo I. Chung
    • 1
    • 2
  • Sung Keun Chang
    • 1
    • 2
  • Enzo T. Cocuzzi
    • 1
    • 2
  • J. E. Folk
    • 1
    • 2
  • Hee Chul Kim
    • 1
    • 2
  • Soo Young Lee
    • 1
    • 2
  • Nadine Martinet
    • 1
    • 2
  • T. Nigra
    • 1
    • 2
  • Hee Sik Sun
    • 1
    • 2
  1. 1.National Institute of Dental ResearchNIHBethesdaUSA
  2. 2.Washington Hospital CenterUSA

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