Skip to main content
SpringerLink
Log in

Glycosylation defining cancer cell motility and invasiveness

  • Published:
Glycoconjugate Journal Aims and scope Submit manuscript

Abstract

Published in 2004.

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

Similar content being viewed by others

References

  1. Hakomori S, Aberrant glycosylation in tumors and tumorassociated carbohydrate antigens, Adv Cancer Res 52, 257–331 (1989).

    Article  PubMed  CAS  Google Scholar 

  2. Hakomori S, Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism, Cancer Res 56, 5309–18 (1996).

    PubMed  CAS  Google Scholar 

  3. Kojima N, Shiota M, Sadahira Y, Handa K, Hakomori S, Cell adhesion in a dynamic flow system as compared to static system: Glycosphingolipid-glycosphingolipid interaction in the dynamic system predominates over lectin-or integrin-based mechanisms in adhesion of B16 melanoma cells to non-activated endothelial cells, J Biol Chem 267, 17264–70 (1992).

    PubMed  CAS  Google Scholar 

  4. Hakomori S, Carbohydrate-carbohydrate interaction as an initial step in cell recognition, Pure & Appl Chem 63, 473–82 (1991).

    CAS  Google Scholar 

  5. Bovin NV, Carbohydrate-carbohydrate interactions:Areview, Biochemistry (Moscow) 61(6), 694–704 (1996).

    Google Scholar 

  6. Rojo J, Morales JC, Penades S, Carbohydrate-carbohydrate interactions in biological and model systems, Topics Curr Chem 218, 45–92 (2002).

    CAS  Google Scholar 

  7. Varki A, Selectin ligands, Proc Natl Acad Sci USA 91, 7390–7 (1994).

    Article  PubMed  CAS  Google Scholar 

  8. Ito A, Handa K, Withers DA, Satoh M, Hakomori S, Binding specificity of siglec7 to disialogangliosides of renal cell carcinoma: Possible role of disialogangliosides in tumor progression, FEBS Lett 498, 116–20 (2001).

    Article  PubMed  CAS  Google Scholar 

  9. Kopitz J, von Reitzenstein C, Andre S, Kaltner H, Uhl J, Ehemann V, Cantz M, Gabius H-J, Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3, J Biol Chem 276(38), 35917–23 (2001).

    Article  PubMed  CAS  Google Scholar 

  10. Crocker PR, Varki A, Siglecs in the immune system, Immunology 103(2), 137–45 (2001).

    Article  PubMed  CAS  Google Scholar 

  11. Hoff SD, Matsushita Y, Ota DM, Cleary KR, Yamori T, Hakomori S, Irimura T, Increased expression of sialyl-dimeric Lex antigen in liver metastases of human colorectal carcinoma, Cancer Res 49, 6883–8 (1989).

    PubMed  CAS  Google Scholar 

  12. Nakamori S, Kameyama M, Imaoka S, Furukawa H, Ishikawa O, Sasaki Y, Kabuto T, Iwanaga T, Matsushita Y, Irimura T, Increased expression of sialyl Lewisx antigen correlates with poor survival in patients with colorectal carcinoma: Clinicopathological and immunohistochemical study, Cancer Res 53, 3632–7 (1993).

    PubMed  CAS  Google Scholar 

  13. Kannagi R, Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer, Glycoconj J 14, 577–84 (1997).

    Article  PubMed  CAS  Google Scholar 

  14. Basu S, Das K, Basu M, Glycosyltransferase in glycosphingolipid biosynthesis. In Oligosaccharides in Chemistry and Biology: Comprehensive Handbook, edited by Ernst B, Sinay PHart G (Wiley-VCH, Weinheim, Germany, 2000), pp. 329–47.

    Google Scholar 

  15. Ono M, Sakamoto M, Ino Y, Moriya Y, Sugihara K, Muto T, Hirohashi S, Cancer cell morphology at the invasive front and expression of cell adhesion-related carbohydrate in the primary lesion of patients with colorectal carcinoma with liver metastasis, Cancer 78(6), 1179–86 (1996).

    Article  PubMed  CAS  Google Scholar 

  16. Ono M, Handa K, Withers DA, Hakomori S, Motility inhibition and apoptosis are induced by metastasis-suppressing gene product CD82 and its analogue CD9, with concurrent glycosylation, Cancer Res 59, 2335–9 (1999).

    PubMed  CAS  Google Scholar 

  17. Ono M, Handa K, Withers DA, Hakomori S, Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: A preliminary note on functional α3, α5-CD82 glycosylation complex in ldlD 14 cells, Biochem Biophys Res Commun 279, 744–50 (2000).

    Article  PubMed  CAS  Google Scholar 

  18. Ono M, Handa K, Sonnino S, Withers DA, Nagai H, Hakomori S, GM3ganglioside inhibits CD9-facilitated haptotactic cell motility: Co-expression of GM3 and CD9 is essential in down-regulation of tumor cell motility and malignancy, Biochemistry 40(21), 6414–21 (2001).

    Article  PubMed  CAS  Google Scholar 

  19. Phillips ML, Nudelman ED, Gaeta FCA, Perez M, Singhal AK, Hakomori S, Paulson JC, ELAM-1 mediates cell adhesion by recognition of a carbohydrate ligand, sialyl-Lex, Science 250, 1130–2 (1990).

    PubMed  CAS  Google Scholar 

  20. Shitara K, Hanai N, Yoshida H, Distribution of lung adenocarcinomaassociated antigens in human tissues and sera defined by monoclonal antibodies: KM-52 and KM-93, Cancer Res 47, 1267–72 (1987).

    PubMed  CAS  Google Scholar 

  21. Dong J-T, Lamb PW, Rinker-Schaeffer CW, Vukanovic J, Ichikawa T, Isaacs JT, Barrett JC, KAI1, a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2, Science 268, 884–6 (1995).

    PubMed  Google Scholar 

  22. Dong JT, Suzuki H, Pin SS, Bova S, Schalken JA, Isaacs WB, Barrett JC, Isaacs JT, Down-regulation of the KAI1 metastasis suppressor gene during the progression of human prostatic cancer infrequently involves gene mutation or allelic loss, Cancer Res 56, 4387–90 (1996).

    PubMed  CAS  Google Scholar 

  23. Miyake M, Koyama M, Seno M, Ikeyama S, Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility, J Exp Med 174, 1347–54 (1991).

    Article  PubMed  CAS  Google Scholar 

  24. Cajot J-F, Sordat I, Silvestre T, Sordat B, Differential display cloning identifies motility-related protein (MRP1/CD9) as highly expressed in primary compared to metastatic human colon carcinoma cells, Cancer Res 57, 2593–7 (1997).

    PubMed  Google Scholar 

  25. Maecker HT, Todd SC, Levy S, The tetraspanin superfamily: Molecular facilitators, FASEB J 11, 428–42 (1997).

    PubMed  CAS  Google Scholar 

  26. Mannion BA, Berditchevski F, Kraeft S-K, Chen LB, Hemler ME, Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associate with integrin β1 (CD94d/CD29), J Immunol 157, 2039–47 (1996).

    PubMed  CAS  Google Scholar 

  27. Rubinstein E, Le Naour F, Lagaudri`ere-Gesbert C, Billard M, Conjeaud H, Boucheix C, CD9, CD63, CD81, and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins, Eur J Immunol 26(11), 2657–65 (1996).

    PubMed  CAS  Google Scholar 

  28. Berditchevski F, Tolias KF, Wong K, Carpenter CL, Hemler ME,A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase, J Biol Chem 272, 2595–8 (1997).

    Article  PubMed  CAS  Google Scholar 

  29. Serru V, LeNaour F, Billard M, Azorsa D O, Lanza F, Boucheix C, Rubinstein E, Selective tetraspan-integrin complexes (CD81/α4β1, CD151/α3β1, CD151/α6β1) under conditions disrupting tetraspan interactions, Biochem J 340(1), 103–11 (1999).

    Article  PubMed  CAS  Google Scholar 

  30. Charrin S, Le Naour F, Oualid M, Billard M, Faure G, Hanash SM, Boucheix C, Rubinstein E, The major CD9 and CD81 molecular partner. Identification and characterization of the complexes, J Biol Chem 276(17), 14329–37 (2001).

    PubMed  CAS  Google Scholar 

  31. Zheng M, Fang H, Hakomori S, Functional role of N-glycosylation in α5β1 integrin receptor: De-N-glycosylation induces dissociation or altered association of α5 and β1 subunits and concomitant loss of fibronectin binding activity, J Biol Chem 269, 12325–31 (1994).

    PubMed  CAS  Google Scholar 

  32. Zheng M, Fang H, Tsuruoka T, Tsuji T, Sasaki T, Hakomori S, Regulatory role of GM3 ganglioside in α5β1 integrin receptor for fibronectin-mediated adhesion of FUA169 cells, J Biol Chem 268, 2217–22 (1993).

    PubMed  CAS  Google Scholar 

  33. Kingsley DM, Kozarsky KF, Hobbie L, Krieger M, Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDPGalNAc 4-epimerase deficient mutant, Cell 44, 749–59 (1986).

    Article  PubMed  CAS  Google Scholar 

  34. Krieger M, Reddy P, Kozarsky K, Kingsley D, Hobbie L, Penman M, Analysis of the synthesis, intracellular sorting, and function of glycoproteins using a mammalian cell mutant with reversible glycosylation defects, Meth Cell Biol 32, 57–84 (1989).

    Article  CAS  Google Scholar 

  35. Sonnino S, Nicolini M, Chigorno V, Preparation of radiolabeled gangliosides, Glycobiology 6(5), 479–87 (1996).

    PubMed  CAS  Google Scholar 

  36. Kawakami Y, Kawakami K, Steelant WFA, Ono M, Baek RC, Handa K, Withers DA, Hakomori S, Tetraspanin CD9 is a “proteolipid”, and its interaction with α3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility, J Biol Chem 277(37), 34349–58 (2002).

    Article  PubMed  CAS  Google Scholar 

  37. Inufusa H, Kojima N, Yasutomi M, Hakomori S, Human lung adenocarcinoma cell lines with different lung colonization potential (LCP), and a correlation between expression of sialosyl dimeric Lex (defined by MAb FH6) and LCP, Clin Expl Metastasis 9, 245–57 (1991).

    Article  CAS  Google Scholar 

  38. Kazui A, Ono M, Handa K, Hakomori S, Glycosylation affects translocation of integrin, Src, and caveolin into or out of GEM, Biochem Biophys Res Commun 273, 159–63 (2000).

    Article  PubMed  CAS  Google Scholar 

  39. Kojima N, Hakomori S, Cell adhesion, spreading, and motility of GM3-expressing cells based on glycolipid-glycolipid interaction, J Biol Chem 266, 17552–8 (1991).

    PubMed  CAS  Google Scholar 

  40. Iwabuchi K, Yamamura S, Prinetti A, Handa K, Hakomori S,GM3-enriched microdomain involved in cell adhesion and signal transduction through carbohydrate-carbohydrate interaction in mouse melanoma B16 cells, J Biol Chem 273, 9130–8 (1998).

    Article  PubMed  CAS  Google Scholar 

  41. Iwabuchi K, Handa K, Hakomori S, Separation of “Glycosphingolipid signaling domain” from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling, J Biol Chem 273, 33766–73 (1998).

    Article  PubMed  CAS  Google Scholar 

  42. Yamamura S, Handa K, Hakomori S, A close association of GM3 with c-Src and Rho in GM3-enriched microdomains at the B16 melanoma cell surface membrane: A preliminary note, Biochem Biophys Res Commun 236, 218–22 (1997).

    Article  PubMed  CAS  Google Scholar 

  43. Hakomori S, Handa K, Glycosphingolipid microdomains in signal transduction, cancer, and development. In Oligosaccharides in Chemistry and Biology: A Comprehensive Handbook, edited by Ernst B, Sinay P, Hart G (Wiley-VCH, Weinheim, Germany, 2000), pp. 771–81.

    Google Scholar 

  44. Handa K, Jacobs F, Longenecker BM, Hakomori S, Association of MUC-1 and PSGL-1 with low-density microdomain in T-lymphocytes: A preliminary note, Biochem Biophys Res Commun 285, 788–94 (2001).

    Article  PubMed  CAS  Google Scholar 

  45. Hakomori S, The glycosynapse, Proc Natl Acad Sci USA 99(1), 225–32 (2002).

    Article  CAS  Google Scholar 

  46. Fenderson BA, Eddy EM, Hakomori S, Glycoconjugate expression during embryogenesis and its biological significance, BioEssays 12(4), 173–9 (1990).

    Article  PubMed  CAS  Google Scholar 

  47. Hakomori S, Handa K, Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: Essential basis to define tumor malignancy, FEBS Lett 531(1), 88–92 (2002).

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Pacific Northwest Research Institute, 720 Broadway, Seattle, WA, 98122-4302, USA

    Masaya Ono & Senitiroh Hakomori

  2. Departments of Pathobiology and Microbiology, University of Washington, Seattle, WA, USA

    Masaya Ono

Authors
  1. Masaya Ono
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Senitiroh Hakomori
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Senitiroh Hakomori.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ono, M., Hakomori, S. Glycosylation defining cancer cell motility and invasiveness. Glycoconj J 20, 71–78 (2003). https://doi.org/10.1023/B:GLYC.0000018019.22070.7d

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/B:GLYC.0000018019.22070.7d

Search

Navigation