Skip to main content

Novel Endogenous ADP-Ribosylations of Proteins in Transformed Cells: Effects of Cellular Transformation and Differentiation

  • Chapter
Book cover Biology of Cellular Transducing Signals

Abstract

ADP-ribosylation is a post-translational modification of proteins that utilizes NAD1 as a donor for the modification grohp (Ueda and Hayaishi, 1985). The reaction involves enzymatic transfer of the ADP-ribose moiety of NAD to specific acceptor amino acids on the target protein; nicotinamide being the released product of this reaction. ADP-ribosylation reactions are broadly classified into mono- and poly(ADPribosyl) ation on the basis of ADP-ribose chain length. However, there are other differences between the two groups. Mono(ADPribosyl) ations generally occur on the side-chain nitrogen atom of the acceptor amino acid, and depending upon this acceptor, can be classified as types A (arginine), C (cysteine) and D (diphthamide) respectively (Moss et al., 1980; Tanuma et al., 1988; Sayhan et al., 1986). On the contrary, poly(ADP-ribosyl) ation starts on the carboxyl groups and forms oglycosidic linkages on glutamic acid residues within the target protein. In some cases (e.g. in histone H1), COOH-terminal lysine may also be the site for poly(ADP-ribosyl)ation (Ogata et al., 1980).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Agarwal, S., Drysdale, B. and Shin, H. S., 1988, Tumor necrosis factor-mediated cytotoxicity involves ADP- ribosylation, J. Immunol. 140:4187.

    PubMed  CAS  Google Scholar 

  • Aktories, K., Just, I. and Rosenthal, W., 1988, Different types of ADP-ribose protein bonds formed by botulinum C2 toxin, botulinum ADP-ribosyltransferase C3 and pertussis toxin. Biochem. Biophys. Res. Commun., 156:361.

    Article  PubMed  CAS  Google Scholar 

  • Alonso, T., Morgan, R. O., Marvizon, J. C., Zabrl, H. and Santos, E., 1988, Malignant transformation by ras and other oncogenes produces common alterations in inositol phospholipid signaling pathways, Proc. Natl. Acad. Sci. USA, 85:4271.

    Article  PubMed  CAS  Google Scholar 

  • Althaus, F. R., Hilz, H. and Shall, S., 1985, “ADP-ribosylation of proteins”, Springer Verlag, Berlin.

    Google Scholar 

  • Banga, H. S., Walker, R. K., Winberry, L. K. and Rittenhouse, S. E., 1988, Platelet adenylate cyclase and phospholipase C are affected differentially by ADP- ribosylation, Biochem. J., 252:297.

    PubMed  CAS  Google Scholar 

  • Breitman, T. R., Selonick, S. E. and Collins, S. J., 1980, Induction of differentiation of human promyelocytic leukemia cell line HL-60) by retinoic acid, Proc. Natl. Acad. Sci. USA, 77:2936.

    Article  PubMed  CAS  Google Scholar 

  • Brune, B. and Lapetina, E. G., 1989, Activation of cytosolic ADP-ribosyl transferase by nitric oxide-generating agents, J. Biol. Chem., 264:8455.

    PubMed  CAS  Google Scholar 

  • Burzio, L. O., Saez, L. and Cornejo, R., 1981, Poly(ADP- ribose) synthetase activity in rat testis mitochondria. Biochem. Biophys. Res. Commun., 103:369.

    Article  PubMed  CAS  Google Scholar 

  • Collins, S. J., Ruscetti, F. W., Gallagher, R. E. and Gallo, R. C., 1978, Terminal differentiation of human promyelocytic leukemia cells induced by dimethyl sulfoxide and other polar compounds, Proc. Natl. Acad. Sci. USA. 75:2458.

    Article  PubMed  CAS  Google Scholar 

  • Duhpan, M. R., Rankin, P. R., King, R. L., Jacobson, M. K. and Dell’Orco, R. T., 1988, Stimulation of mono (ADP- ribosyl) -ation by reduced extracellular calcium levels in human fibroblasts, J. Cell.Physiol., 134:161.

    Article  Google Scholar 

  • Fendrick, J. L. and Iglewski, W. J., 1989, Endogenous ADP- ribosylation of elongation factor-2 in polyoma virus- transformed baby hamster kidney cells, Proc. Natl. Acad. Sci. USA, 86:554.

    Article  PubMed  CAS  Google Scholar 

  • Hayaishi, O. and Ueda, K., 1982, “ADP-ribosylation reactions: biology and medicine”, Academic Press, New York.

    Google Scholar 

  • Hilz, H., 1981, ADP-ribosylation of proteins - a multifunctional process, Hoppe-Seyler’s Z. Physiol. Chem., 362:1415.

    Article  PubMed  CAS  Google Scholar 

  • Hisa, J. A., Tsai, S. C., Adamik, R., Yost, D. A., Hewlett, E. L. and Moss, J., 1985, Amino acid-specific ADP- ribosylation. Sensitivity to hydroxylamine of [cysteine(ADP-ribose) ] protein and [arginine(ADP- ribose)] protein linkages, J. Biol. Chem., 260:16187

    Google Scholar 

  • Iglewski, W.J., Lee, H. and Muller, P., 1984, ADP-ribosyl transferase from beef liver which ADP-ribosylates elongation factor-2, FEBS Lett., 173:113.

    Article  PubMed  CAS  Google Scholar 

  • Kanai, M., Miwa, M., Kondo, T., Tanaka, Y., Nakayasu, M. and Sugimura, T., 1982, Involvement of poly(ADP-ribose) metabolism in induction of differentiation of HL-60 promyelocytic leukemia cells, Biochem. Biophys. Res. Commun., 105:404.

    Article  PubMed  CAS  Google Scholar 

  • Katada, T. and Ui, M., 1982, Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein, Proc. Natl. Acad. Sci. USA, 79:3129.

    Article  PubMed  CAS  Google Scholar 

  • Kitamura, A., Tanigawa, Y., Yamamoto, T., Kawamura, M., Doi, S. and Shimoyama, Y., 1979, Glucocorticoid induced reduction of poly (ADP-ribose)synthetase in nuclei from chick embryo liver, Biochem. Biophys. Res. Commun., 87:725.

    Article  PubMed  CAS  Google Scholar 

  • Kun, E., Zimber, P. H., Chang, A. Y., Puschendorf, B. and Grunicke, H., 1975, Macromolecular enzymatic product of NAD+ in liver mitochondria, Proc. Natl. Acad. Sci. USA, 72:1436.

    Article  PubMed  CAS  Google Scholar 

  • Mangelsdorf, D. J., Koeffler, P. H., Donaldson, C. A., Pike, J. W. and Jaussler, M. R., 1984, 1, 25-Dihydroxyvitamin D3-induced differentiation in a human promyelocytic leukemia cell line (HL-60): receptor-mediated maturation to macrophage-1ike cells, J. Cell Biol., 98:391.

    Article  PubMed  CAS  Google Scholar 

  • Miwa, M., Oda, K., Segawa, K., Tanaka, M., Irie, S., Yamaguchi, N., Kuchino, T., Shiroki, K., Shimojo, H., Sakura, H., Matsushima, T. and Sugimura, T., 1977, Cell density dependent increase in chromatin-associated ADP- ribosyl transferase activity in simian virus 40- transformed cells, Arch. Biochem. Biophys., 181:313–321.

    Article  PubMed  CAS  Google Scholar 

  • Miwa, M., Saikawa, N., Yamaizumi, Z., Nishimura, S. and Sugimura, T., 1979, Structure of poly (adenosine diphosphate ribose) : Identification of 2′ - [1″-ribosy1-2″- (or 3″-) (1″′-ribosyl)]adenosine-5′,5′,5″′-tris (phosphate) as a branch linkage, Proc. Natl. Acad. Sci. USA, 76:595.

    Article  PubMed  CAS  Google Scholar 

  • Miyaura, C., Abe, E., Kuribayashi, T., Tanaka, H., Konno, K., Nishii, Y. and Suda, T., 1981, 1, 25-Dihydroxyvitamin D3 induces differentiation of human myeloid leukemia cells, Biochem. Biophys. Res. Commun., 102:937.

    Article  PubMed  CAS  Google Scholar 

  • Molina Y Vedia, L., Nolan, R. D. and Lapetina, E. G., 1988, Endogenous ADP-ribosylation in human platelets, Biochem. Biophys. Res. Commun., 157:1323.

    Article  Google Scholar 

  • Moss, J. and Vaughan, M., 1978, Isolation of an avian erythrocyte protein possessing ADP-ribosyltransferase activity and capable of activating adenylate cyclase, Proc.Natl. Acad. Sci. USA, 75:3621.

    Article  PubMed  CAS  Google Scholar 

  • Moss, J., Stanley, S. J. and Watkins, P. A., 1980, Isolation and properties of an NAD- and guanidine-dependent ADP- ribosyl transferase from turkey erythrocytes, J. Biol. Chem., 255:5838.

    PubMed  CAS  Google Scholar 

  • Muira, S., Burzio, L. and Koide, S. S., 1972, Studies on deoxyribosenucleic acid synthesis in uteri of immature mouse, Hormone Metab. Res., 4:273.

    Article  Google Scholar 

  • Nishizuka, Y., Ueda, K., Honjo, T. and Hayaishi, O., 1968, Enzymatic adenosine diphosphate ribosylation of histone and polyadenosine diphosphate ribose synthesis in rat liver nuclei, J. Biol. Chem., 243:3765.

    PubMed  CAS  Google Scholar 

  • Ogata, N., Ueda, K., Kagamiyama, H. and Hayaishi, O., 1980, ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14 and the carboxy terminal lysine residues as modification sites, J. Biol. Chem., 255:7616.

    PubMed  CAS  Google Scholar 

  • Pekala, P. H., Lane, M. D., Watkins, P. A. and Moss, J., 1981, On the mechanism of preadipocyte differentiation. Masking of poly(ADP-ribose)synthetase activity during differentiation of 3T3-L1 preadipocytes, J. Biol. Chem. 256:4871.

    PubMed  CAS  Google Scholar 

  • Rankin, P. W., Jacobson, E. L., Benjamin, R. C., Moss, J. and Jacobson, M. K., 1989, Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo, J. Biol. Chem., 264:4312.

    PubMed  CAS  Google Scholar 

  • Rastle, E. and Swetly, P., 1978, Expression of poly (adenosine diphosphate ribose) polymerase activity in erythroleukemic mouse cells during cell cycle and erythropoeitic differentiation, J. Biol. Chem., 253:4333.

    Google Scholar 

  • Roberts, J. H., Stark, P., Giri, C. P. and Smulson, M., 1975, Cytoplasmic poly (ADP-ribose) polymerase during the HeLa cell cycle, Arch. Biochem. Biophys., 171:305.

    Article  PubMed  CAS  Google Scholar 

  • Rovera, G., Santoli, D. and Damski, C. (1979) Human promyelocytic leukemia cells in culture differentiate into macrophage-like cells when treated with a phorbol diester, Proc. Natl. Acad. Sci. USA, 76:2779.

    Article  PubMed  CAS  Google Scholar 

  • Sariban, E., Mitchell, T. and Kufe, D., 1985, Expression of the c-fms pro-oncogene during human monocytic differentiation, Nature (Lond.), 316:64.

    Article  CAS  Google Scholar 

  • Sayhan, O., Ozdemirli, M., Nurten, R. and Bermek, E., 1986, On the nature of cellular ADP-ribosyltransferase from rat liver specific for elongation factor 2, Biochem. Biophys. Res. Commun., 139:1210.

    Article  PubMed  CAS  Google Scholar 

  • Shall, S., 1988, ADP-ribosylation of proteins: A ubiquitous cellular control mechanism, Adv. Exp. Med. Biol., 231:597.

    PubMed  CAS  Google Scholar 

  • Tanigawa, Y., Tsuchiya, M., Imai, Y. and Shimoyama, M., 1984, ADP-ribosyltransferase from hen liver nuclei, J. Biol. Chem., 259:2022.

    PubMed  CAS  Google Scholar 

  • Tanuma, S., Johnson, L. D. and Johnson, G. S., 1983, ADP- ribosylation of chromosomal proteins and mouse mammary tumor virus gene expression, J. Biol. Chem., 258:15371.

    PubMed  CAS  Google Scholar 

  • Tanuma, S., Kawashima, K. and Endo, H., 1988, Eukaryotic mono (ADP-ribosyl) transferase that ADP-ribosylates GTP- binding regulatory Gi protein, J. Biol. Chem.,263:5485.

    PubMed  CAS  Google Scholar 

  • Ueda, K. and Hayaishi, 0., 1985, ADP-ribosylation, Ann. Rev. Biochem., 54:73.

    Article  PubMed  CAS  Google Scholar 

  • Ueda, K. and Hayaishi, O., 1982, Leukemia and cancer, in: “ADP-ribosylation reactions: biology and medicine,” O. Hayaishi and K. Ueda, eds., Academic Press, New York.

    Google Scholar 

  • Van Ness, B. G., Howard, J. B. and Bodley, J. W., 1980, ADP- ribosylation of elongation factor 2 by diphtheria toxin, J. Biol. Chem., 255:10710.

    PubMed  Google Scholar 

  • Vaughan, M. and Moss, J., 1981, Mono(ADP-ribosyl)transferases and their effects on cellular metabolism, Curr. Top. Cell. Reαul., 20:205.

    CAS  Google Scholar 

  • Vitti, P., De Wolf, M. J. S., Acquaviva, A. M., Epstein, M. and Kohn, L. D., 1982, Thyrotropin stimulation of the ADP-ribosyltransferase activity of bovine thyroid membranes, Proc. Natl. Acad. Sci. USA, 79: 1525–1529.

    Article  PubMed  CAS  Google Scholar 

  • Wielckens, K., Bredehorst, R., Adamietz, P. and Hilz, H., 1981, Protein-bound polymeric and monomeric ADP-ribose residues in hepatic tissues, Eur. J. Biochem., 117:69.

    Article  PubMed  CAS  Google Scholar 

  • Yost, D. A. and Moss, J., 1983, Amino acid specific ADP- ribosylation. Evidence for two distinct NAD-arginine ADP -ribosyltransferases in turkey erythrocytes, J. Biol. Chem., 258:4926.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1990 Plenum Press, New York

About this chapter

Cite this chapter

Banga, H.S., Feinstein, M.B. (1990). Novel Endogenous ADP-Ribosylations of Proteins in Transformed Cells: Effects of Cellular Transformation and Differentiation. In: Vanderhoek, J.Y. (eds) Biology of Cellular Transducing Signals. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0559-0_21

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-0559-0_21

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-7866-5

  • Online ISBN: 978-1-4613-0559-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics