Skip to main content

Advertisement

SpringerLink
Log in

Afterword (Editorial)

  • Comprehensive Review Article
  • Published:
Glycoconjugate Journal Aims and scope Submit manuscript

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

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

References

  1. Hakomori, S.: A rapid permethylation of glycolipid, and polysaccharide catalyzed by methylsulfinyl carbanion in dimethyl sulfoxide. J. Biochem. 55, 205–208 (1964)

    CAS  PubMed  Google Scholar 

  2. Hakomori, S., Murakami, W.T.: Glycolipids of hamster fibroblasts and derived malignant-transformed cell lines. Proc. Natl. Acad. Sci. USA 59(1), 254–261 (1968). https://doi.org/10.1073/pnas.59.1.254

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  3. Hakomori, S., Teather, C., Andrews, H.: Organizational difference of cell surface “hematoside” in normal and virally transformed cells. Biochem. Biophys. Res. Commun. 33(4), 563–568 (1968). https://doi.org/10.1016/0006-291x(68)90332-x

    Article  CAS  PubMed  Google Scholar 

  4. Hakomori, S.: Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res. 56(23), 5309–5318 (1996)

    CAS  PubMed  Google Scholar 

  5. Yamamoto, F., Clausen, H., White, T., Marken, J., Hakomori, S.: Molecular genetic basis of the histo-blood group ABO system. Nature. 345(6272), 229–233 (1990). https://doi.org/10.1038/345229a0

    Article  CAS  PubMed  Google Scholar 

  6. Degroote, S., Wolthoorn, J., van Meer, G.: The cell biology of glycosphingolipids. Semin. Cell. Dev. Biol. 15(4), 375–387 (2004)

    Article  CAS  PubMed  Google Scholar 

  7. Murate, M., Hayakawa, T., Ishii, K., Inadome, H., Greimel, P., Watanabe, M., Nagatsuka, Y., Ito, K., Ito, Y., Takahashi, H., Hirabayashi, Y., Kobayashi, T.: Phosphatidylglucoside forms specific lipid domains on the outer leaflet of the plasma membrane. Biochemistry 49(23), 4732–4739 (2010). https://doi.org/10.1021/bi100007u

    Article  CAS  PubMed  Google Scholar 

  8. Murate, M., Abe, M., Kasahara, K., Iwabuchi, K., Umeda, M., Kobayashi, T.: Transbilayer distribution of lipids at nano scale. J. Cell. Sci. 128(8), 1627–1638 (2015). https://doi.org/10.1242/jcs.163105

    Article  CAS  PubMed  Google Scholar 

  9. Hakomori, S.: Structure, organization, and function of glycosphingolipids in membrane. Curr. Opin. Hematol. 10(1), 16–24 (2003). https://doi.org/10.1097/00062752-200301000-00004

    Article  CAS  PubMed  Google Scholar 

  10. Kaga, N., Kazuno, S., Taka, H., Iwabuchi, K., Murayama, K.: Isolation and mass spectrometry characterization of molecular species of lactosylceramides using liquid chromatography-electrospray ion trap mass spectrometry. Anal. Biochem. 337(2), 316–324 (2005). https://doi.org/10.1016/j.ab.2004.11.003

    Article  CAS  PubMed  Google Scholar 

  11. Hakomori, S.: Glycosphingolipids in cellular interaction, differentiation, and oncogenesis. Annu. Rev. Biochem. 50, 733–764 (1981). https://doi.org/10.1146/annurev.bi.50.070181.003505

    Article  CAS  PubMed  Google Scholar 

  12. Hakomori, S.: The glycosynapse. Proc. Natl. Acad. Sci. USA. 99(1), 225–232 (2002). https://doi.org/10.1073/pnas.012540899

    Article  CAS  PubMed Central  Google Scholar 

  13. Laine, R.A., Hakomori, S.: Incorporation of exogenous glycosphingolipids in plasma membranes of cultured hamster cells and concurrent change of growth behavior. Biochem. Biophys. Res. Commun. 54(3), 1039–1045 (1973). https://doi.org/10.1016/0006-291x(73)90798-5

    Article  CAS  PubMed  Google Scholar 

  14. Bremer, E.G., Hakomori, S., Bowen-Pope, D.F., Raines, E., Ross, R.: Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation. J. Biol. Chem. 259(11), 6818–6825 (1984)

    Article  CAS  PubMed  Google Scholar 

  15. Bremer, E.G., Schlessinger, J., Hakomori, S.: Ganglioside-mediated modulation of cell growth. Specific effects of GM3 on tyrosine phosphorylation of the epidermal growth factor receptor. J. Biol. Chem. 261(5), 2434–2440 (1986)

  16. Hanai, N., Nores, G.A., MacLeod, C., Torres-Mendez, C.R., Hakomori, S.: Ganglioside-mediated modulation of cell growth. Specific effects of GM3 and lyso-GM3 in tyrosine phosphorylation of the epidermal growth factor receptor. J. Biol. Chem. 263(22), 10915–10921 (1988)

  17. Song, W.X., Vacca, M.F., Welti, R., Rintoul, D.A.: Effects of gangliosides GM3 and De-N-acetyl GM3 on epidermal growth factor receptor kinase activity and cell growth. J. Biol. Chem. 266(16), 10174–10181 (1991)

    Article  CAS  PubMed  Google Scholar 

  18. Zhou, Q., Hakomori, S., Kitamura, K., Igarashi, Y.: GM3 directly inhibits tyrosine phosphorylation and de-N-acetyl-GM3 directly enhances serine phosphorylation of epidermal growth factor receptor, independently of receptor-receptor interaction. J. Biol. Chem. 269(3), 1959–1965 (1994)

    Article  CAS  PubMed  Google Scholar 

  19. Miljan, E.A., Meuillet, E.J., Mania-Farnell, B., George, D., Yamamoto, H., Simon, H.G., Bremer, E.G.: Interaction of the extracellular domain of the epidermal growth factor receptor with gangliosides. J. Biol. Chem. 277(12), 10108–10113 (2002)

    Article  CAS  PubMed  Google Scholar 

  20. Yoon, S.J., Nakayama, K., Hikita, T., Handa, K., Hakomori, S.: Epidermal growth factor receptor tyrosine kinase is modulated by GM3 interaction with N-linked GlcNAc termini of the receptor. Proc. Natl. Acad. Sci. USA. 103(50), 18987–18991 (2006)

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  21. Yoon, S.J., Nakayama, K., Takahashi, N., Yagi, H., Utkina, N., Wang, H.Y., Kato, K., Sadilek, M., Hakomori, S.: Interaction of N-linked glycans, having multivalent GlcNAc termini, with GM3 ganglioside. Glycoconj. J. 23(9), 639–649 (2006)

    Article  CAS  PubMed  Google Scholar 

  22. Hanai, N., Dohi, T., Nores, G.A., Hakomori, S.: A novel ganglioside, de-N-acetyl-GM3 (II3NeuNH2LacCer), acting as a strong promoter for epidermal growth factor receptor kinase and as a stimulator for cell growth. J. Biol. Chem. 263(13), 6296–6301 (1988)

    Article  CAS  PubMed  Google Scholar 

  23. Inokuchi, J., Radin, N.S.: Preparation of the active isomer of 1-phenyl-2-decanoylamino-3-morpholino-1-propanol, inhibitor of murine glucocerebroside synthetase. J. Lipid. Res. 28(5), 565–571 (1987)

    Article  CAS  PubMed  Google Scholar 

  24. Barbour, S., Edidin, M., Felding-Habermann, B., Taylor-Norton, J., Radin, N.S., Fenderson, B.A.: Glycolipid depletion using a ceramide analogue (PDMP) alters growth, adhesion, and membrane lipid organization in human A431 cells. J. Cell. Physiol. 150(3), 610–619 (1992). https://doi.org/10.1002/jcp.1041500322

    Article  CAS  PubMed  Google Scholar 

  25. Ringerike, T., Blystad, F.D., Levy, F.O., Madshus, I.H., Stang, E.: Cholesterol is important in control of EGF receptor kinase activity but EGF receptors are not concentrated in caveolae. J. Cell. Sci. 115(6), 1331–1340 (2002)

    Article  CAS  PubMed  Google Scholar 

  26. Roepstorff, K., Thomsen, P., Sandvig, K., van Deurs, B.: Sequestration of epidermal growth factor receptors in non-caveolar lipid rafts inhibits ligand binding. J. Biol. Chem. 277(21), 18954–18960 (2002)

    Article  CAS  PubMed  Google Scholar 

  27. Pike, L.J.: Growth factor receptors, lipid rafts and caveolae: an evolving story. Biochim. Biophys. Acta. 1746(3), 260–273 (2005)

    Article  CAS  PubMed  Google Scholar 

  28. Pike, L.J., Han, X., Gross, R.W.: Epidermal growth factor receptors are localized to lipid rafts that contain a balance of inner and outer leaflet lipids: a shotgun lipidomics study. J. Biol. Chem. 280(29), 26796–26804 (2005)

    Article  CAS  PubMed  Google Scholar 

  29. Waugh, M.G., Lawson, D., Hsuan, J.J.: Epidermal growth factor receptor activation is localized within low-buoyant density, non-caveolar membrane domains. Biochem. J. 337(Pt 3), 591–597 (1999)

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  30. Waugh, M.G., Minogue, S., Anderson, J.S., dos Santos, M., Hsuan, J.J.: Signalling and non-caveolar rafts. Biochem. Soc. Trans. 29(Pt 4), 509–511 (2001)

  31. Wang, X.-Q., Sun, P., Paller, A.S.: Ganglioside Induces Caveolin-1 Redistribution and Interaction with the Epidermal Growth Factor Receptor. J. Biol. Chem. 277(49), 47028–47034 (2002)

    Article  CAS  PubMed  Google Scholar 

  32. Wang, X.Q., Sun, P., Paller, A.S.: Ganglioside GM3 blocks the activation of epidermal growth factor receptor induced by integrin at specific tyrosine sites. J. Biol. Chem. 278(49), 48770–48778 (2003)

    Article  CAS  PubMed  Google Scholar 

  33. Kabayama, K., Sato, T., Saito, K., Loberto, N., Prinetti, A., Sonnino, S., Kinjo, M., Igarashi, Y., Inokuchi, J.: Dissociation of the insulin receptor and caveolin-1 complex by ganglioside GM3 in the state of insulin resistance. Proc. Natl. Acad. Sci. USA. 104(34), 13678–13683 (2007). https://doi.org/10.1073/pnas.0703650104

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  34. Coskun, Ü., Grzybek, M., Drechsel, D., Simons, K.: Regulation of human EGF receptor by lipids. Proc. Natl. Acad. Sci. USA. 108(22), 9044–9048 (2011). https://doi.org/10.1073/pnas.1105666108

    Article  PubMed Central  PubMed  Google Scholar 

  35. Nakano, M., Hanashima, S., Hara, T., Kabayama, K., Asahina, Y., Hojo, H., Komura, N., Ando, H., Nyholm, T.K.M., Slotte, J.P., Murata, M.: FRET detects lateral interaction between transmembrane domain of EGF receptor and ganglioside GM3 in lipid bilayers. Biochim. Biophys. Acta. Biomembr. 1863(8), 183623 (2021). https://doi.org/10.1016/j.bbamem.2021.183623

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgements

We thank Dr. Steve Anderson for editing this Afterword. We would also like to express our gratitude to Dr. Anderson for his invaluable help in organizing some practical aspects of this Special issue. As administrator/scientific editor in Dr. Hakomori's lab. for 24 years, Dr. Anderson has been a fellow and companion for many Hakomori’s scholars.

Author information

Author notes

  1. Kazuhisa Iwabuchi and Alessandro Prinetti contributed equally in this work.

Authors and Affiliations

  1. Institute for Environmental and Gender-Specific Medicine, Juntendo University Graduate School of Medicine, 2-1-1 Tomioka Urayasu-shi, Chiba, 279-0021, Japan

    Kazuhisa Iwabuchi

  2. Infection Control Nursing, Juntendo University Graduate School of Health Care and Nursing, Urayasu, Chiba, 279-0023, Japan

    Kazuhisa Iwabuchi

  3. Department of Medical Biotechnology and Translational Medicine, University of Milano, Segrate, Milano, Italy

    Alessandro Prinetti

Authors
  1. Kazuhisa Iwabuchi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Alessandro Prinetti
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Kazuhisa Iwabuchi.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Iwabuchi, K., Prinetti, A. Afterword (Editorial). Glycoconj J 40, 119–122 (2023). https://doi.org/10.1007/s10719-022-10090-8

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10719-022-10090-8

Keywords

Search

Navigation