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Transglutaminase, Donor Age, and in Vitro Cellular Senescence

  • P. J. Birckbichler
  • L. E. Anderson
  • R. T. Dell’Orco
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)

Abstract

Human diploid fibroblast-like cells (HDF) exhibit a limited lifespan when maintained in culture, a property which has led to their use as a model system for the study of cellular senescence1. The lifespan is characteristic for each cell strain and is inversely related to the age of the donor from which the cells were obtained2. Upon continuous subcultivation, HDF gradually lose their ability to traverse the cell cycle and divide. This loss of proliferative potential results in a viable, post-mitotic population which is still metabolically active3. Although the mechanisms responsible for the loss of proliferative potential have not been defined, they appear to be regulated by a timing system that is based on the number of previous cellular divisions4. This biological clock has been postulated to be the result of a series of programmed and/or stochastic events which lead to alterations in genetic expression3. A primary focus for such alterations would appear to involve one or more of the many biochemical processes which are necessary for cells to proceed through Gl and enter the S phase of the division cycle5.

Keywords

Human Diploid Fibroblast Human Diploid Cell Isopeptide Bond Cornified Envelope Transglutaminase Activity 
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. 1.
    L. Hayflick, The Limited In Vitro Lifetime of Human Diploid Cell Strains, Exptl. Cell Res. 37:614 (1965).PubMedCrossRefGoogle Scholar
  2. 2.
    G.M. Martin, C.A. Sprague, and C.J. Epstein, Replicative Life-Span of Human Cells, Lab. Invest. 23:86 (1970).Google Scholar
  3. 3.
    L. Hayflick, Recent Advance in the Cell Biology of Aging, Mech. Ageing Develop. 14:59 (1980).CrossRefGoogle Scholar
  4. 4.
    R.T. Dell’Orco, J.G. Mertens, and P.F. Kruse Jr., Doubling Potential, Calendar Time, and Donor Age of Human Diploid Cells in Culture, Exptl. Cell Res. 84:363 (1974).PubMedCrossRefGoogle Scholar
  5. 5.
    A. Macieira-Coelho, Kinetics of the Proliferation of Human Fibroblasts During their Lifespan In Vitro, Mech. Ageing Develop. 6:341 (1977).CrossRefGoogle Scholar
  6. 6.
    A. Macieira-Coelho, Changes in Membrane Properties Associated with Cellular Aging, Inter. Rev. Cytol. 83:183 (1983).Google Scholar
  7. 7.
    P.J. Birckbichler and M.K. Patterson Jr., Cellular Transglutaminase, Growth, and Transformation, Ann. N.Y. Acad. Sci. 312:354 (1978).PubMedCrossRefGoogle Scholar
  8. 8.
    R.T. Dell’Orco, L.E. Anderson, E. Conway, and P.J. Birckbichler, Variable Transglutaminase Activity in Human Diploid Fibroblasts During In Vitro Senescence, Cell. Biol. Inter. Rep. 9:945 (1985).CrossRefGoogle Scholar
  9. 9.
    D.D. Clarke, M.J. Mycek, A. Neidle, and H. Waelsch, The Incorporation of Amines into Protein, Arch. Biochem. Biophys. 79:338 (1959).CrossRefGoogle Scholar
  10. 10.
    J.E. Folk and J.S. Finlayson, The ε-(γ-Glutamyl)Lysine Crosslink and the Catalytic Role of Transglutaminase, Adv. Protein Chem. 31:1 (1977).PubMedGoogle Scholar
  11. 11.
    J.E. Folk, Transglutaminases, Ann. Rev. Biochem. 49:517 (1980).PubMedCrossRefGoogle Scholar
  12. 12.
    J.E. Folk, Mechanism and Basis for Specificity of Transglutaminase-catalyzed ε-(γ-Glutamyl)Lysine Bond Formation, Adv. Enzymol. 54:1 (1983).PubMedGoogle Scholar
  13. 13.
    L. Lorand and S.M. Conrad, Transglutaminases, Mol. and Cell. Biochem. 58:9 (1984).CrossRefGoogle Scholar
  14. 14.
    P.J. Birckbichler, G.R. Orr, E. Conway, and M.K. Patterson Jr., Transglutaminase Activity in Normal and Transformed Cells, Cancer Res. 37:1340 (1977).PubMedGoogle Scholar
  15. 15.
    P.J. Birckbichler and M.K. Patterson Jr., Transglutaminase and ε-(γ-Glutamyl)Lysine Isopeptide Bonds in Eukaryotic Cells, Prog. Clin. Biol. Res. 41:845 (1980).PubMedGoogle Scholar
  16. 16.
    P.J. Birckbichler, G.R. Orr, M.K. Patterson Jr., E. Conway, H.A. Carter, Increase in Proliferative Markers After Inhibition of Transglutaminase, Proc. Natl. Acad. Sci. USA, 78:5005 (1981).PubMedCrossRefGoogle Scholar
  17. 17.
    P.J. Birckbichler, G.R. Orr, M.K. Patterson Jr., E. Conway, H.A. Carter, and M.D. Maxwell, Enhanced Transglutaminase Activity in Transformed Human Lung Fibroblast Cells After Exposure to Sodium Butyrate, Biochim. Biophys. Acta 723:27 (1983).CrossRefGoogle Scholar
  18. 18.
    M.K. Patterson Jr., M.D. Maxwell, P.J. Birckbichler, E. Conway, and H.A. Carter, Putrescine as a Regulator of ε-(γ-Glutamyl)lysine Isopeptide Production and the Proliferative State, Cell Biol. Inter. Rep. 6:461 (1982).CrossRefGoogle Scholar
  19. 19.
    E.L. Schneider and J.R. Smith, The Relationship of In Vitro Studies to In Vivo Human Aging, Inter. Rev. Cytol. 69:261 (1981).Google Scholar
  20. 20.
    E.L. Schneider, Y. Mitsui, K.S. Au, and S. Stuart Shorr, Tissue-Specific Differences in Cultured Human Diploid Fibroblasts, Exptl. Cell Res. 108:1 (1977).PubMedGoogle Scholar
  21. 21.
    U.K. Laemmli, Cleavage of Structural Proteins During the Assembly of the Head of Bacteriophage T4, Nature, 227:680 (1970).PubMedCrossRefGoogle Scholar
  22. 22.
    H. Towbin, T. Staehelin, and J. Gordon, Electrophoretic Transfer of Proteins from Polyacrylamide Gels to Nitrocellulose Sheets: Procedure and Some Applications, Proc. Natl. Acad. Sci. USA 76:4350 (1979).PubMedCrossRefGoogle Scholar
  23. 23.
    E.L. Schneider and Y. Mitsui, The Relationship Between In Vitro Cellular Aging and In Vivo Human Age, Proc. Natl. Acad. Sci. USA 73:3584 (1976).PubMedCrossRefGoogle Scholar
  24. 24.
    M.R. Duncan, R.T. Dell’Orco, and K.D. Kirk, Superoxide Dismutase Specific Activities in Cultured Human Diploid Cells of Various Donor Ages, J. Cell. Physiol. 98:437 (1979).PubMedCrossRefGoogle Scholar
  25. 25.
    Y. Courtois and R.C. Hughes, Surface Labelling of Senescent Chick Fibroblasts by Lactoperoxidase-catalyzed Iodination, Gerontology, 22:371 (1976).PubMedCrossRefGoogle Scholar
  26. 26.
    S. Aizawa, Y. Mitsui, F. Kurimoto, and K. Nomura, Cell Surface Changes Accompanying Aging in Human Diploid Fibroblasts, Exp. Cell Res. 127:143 (1980).PubMedCrossRefGoogle Scholar
  27. 27.
    K.G. Vogel, R.O. Kelley, and C. Stewart, Loss of Organized Fibronectin Matrix from the Surface of Aging Diploid Fibroblasts (IMR-90), Mech. Ageing Develop. 16:295 (1981).CrossRefGoogle Scholar
  28. 28.
    S. Chandrasekhar, J.A. Sorrentino, and A.J.T. Millis, Interaction of Fibronectin with Collagen: Age-specific Defect in the Biological Activity of Human Fibroblast Fibronectin, Proc. Natl. Acad. USA 80:4747 (1983).CrossRefGoogle Scholar
  29. 29.
    A.J.T. Millis, M. Hoyle, D.M. Dunn, and M.J. Brennan, Incorporation of Cellular and Plasma Fibronectins into the Smooth Muscle Cell Extracellular Matrix, in vitro, Proc. Natl. Acad. Sci. USA 82:2746 (1985).PubMedCrossRefGoogle Scholar
  30. 30.
    J. Shevitz, C.S.P. Jenkins, and V.B. Hatcher, Fibronectin Synthesis and Degradation in Human Fibroblasts with Aging, Mech. Ageing Develop. 35:221 (1986).CrossRefGoogle Scholar
  31. 31.
    M.K. Patterson Jr., M.D. Maxwell, P.J. Birckbichler, E. Conway, and H.A. Carter, Cytoskeletal Elements as Substrates for Transglutaminase Catalyzed Bonds, In Vitro, 20:251 (1984) abstract.Google Scholar
  32. 32.
    H.F. Upchurch, E. Conway, M.K. Patterson Jr., P.J. Birckbichler, and M.D. Maxwell, An Immunofluorescence Study of Cellular Transglutaminase and Its Affinity for Extracellular Matrix, submitted for publication (1987).Google Scholar
  33. 33.
    M.K. Patterson Jr., M.D. Maxwell, P.J. Birckbichler, and H.F. Upchurch, Is Fibronectin a Physiological Substrate of Transglutaminase? In Vitro 21:34A (1985) abstract.Google Scholar
  34. 34.
    M.K. Patterson, M. Maxwell, P.J. Birckbichler, H. Upchurch, and E. Conway, Cellular Relationship of Transglutaminase to Its Substrate, Fed. Proc. 45:1685 (1986) abstract.Google Scholar
  35. 35.
    U. Lichti, T. Ben, and S.H. Yuspa, Retinoic Acid-Induced Transglutaminase in Mouse Epidermal Cells is Distinct from Epidermal Transglutaminase, J. Biol. Chem. 260:1422 (1985).PubMedGoogle Scholar
  36. 36.
    S.M. Thacher and R.H. Rice, Keratinocyte-Specific Transglutaminase of Cultured Human Epidermal Cells: Relation to Cross-Linked Envelope Formation and Terminal Differentiation, Cell 40:685 (1985).PubMedCrossRefGoogle Scholar
  37. 37.
    R.H. Rice and H. Green, The Cornified Envelope of Terminally Differentiated Human Epidermal Keratinocytes Consists of Cross-Linked Protein, Cell 11:417 (1978).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • P. J. Birckbichler
    • 1
  • L. E. Anderson
    • 1
  • R. T. Dell’Orco
    • 1
  1. 1.Biomedical DivisionThe Samuel Roberts Noble Foundation, Inc.ArdmoreUSA

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