Advertisement

Glycoconjugate Journal

, Volume 14, Issue 2, pp 267–274 | Cite as

Macrophage surface glycoproteins binding to galectin-3 (Mac-2-antigen)

  • Sucai Dong
  • R Colin Hughes
Article

Abstract

Galectin-3 (formerly called Mac-2 antigen) is a ∼30 kDa carbohydrate-binding protein expressed on the surface of inflammatory macrophages and several macrophage cell lines. We have purified from lysates of the murine macrophage cell line WEHI-3 glycoproteins that bind to a galectin-3 affinity column. Several of these receptors are labelled after biotinylation of intact cells showing their location at the cell surface. N-terminal aminoacid sequencing of intact galectin-3-binding glycoproteins isolated from preparative SDS-gels or of chemically derived fragments showed several homologies with known proteins and identification was confirmed by immunoprecipitation with specific antibodies. The glycoproteins were shown to be: the α-subunit(CD11b) of the CD11b/CD18 integrin(Mac-1 antigen); the lysosomal membrane glycoproteins LAMPs 1 and 2 which are known in part to be expressed at cell surfaces; the Mac-3 antigen, a mouse macrophage differentiation antigen defined by the M3/84 monoclonal antibody and related immunochemically to LAMP-2; the heavy chain of CD98, a 125 kDa heterodimeric glycoprotein identified by the 4F2/RL388 monoclonal antibodies respectively on human and mouse monocytes/macrophages and on activated T cells. Further studies showed that CD11b/CD18, CD98 and Mac-3 are major surface receptors for galectin-3 on murine peritoneal macrophages elicited by thioglycollate. Abbreviations: PBS, phosphate buffered saline; CNBR, cyanogen bromide; PMSF, phenyl methyl sulphonyl fluoride

galectin-3 macrophages receptors 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Barondes SH, Cooper DNW, Gitt MA, Leffer H (1994) J Biol Chem 269: 20807-10.PubMedGoogle Scholar
  2. 2.
    Hughes RC (1994) Glycobiol. 4: 5-12.Google Scholar
  3. 3.
    Sato S, Burdett IDJ, Hughes RC (1993) Exp Cell Res 207: 8-18.PubMedCrossRefGoogle Scholar
  4. 4.
    Springer TA (1981) J Biol Chem 256: 3833-8.PubMedGoogle Scholar
  5. 5.
    Ho M-K, Springer T (1982) J Immunol 128: 1221-8.PubMedGoogle Scholar
  6. 6.
    Leenen PJM, de Bruijn FTR, Voerman JSA, Campbell PA, van Ewijk W (1994) J Immunol Methods 174: 5-19.PubMedCrossRefGoogle Scholar
  7. 7.
    Ralph P, Ho M-K, Litcofsky PB, Springer TA (1983) J Immunol 130: 108-14.PubMedGoogle Scholar
  8. 8.
    Leenen PJM, Jansen AMAC, van Ewijk W (1986) Differentiation 32 157-64.PubMedCrossRefGoogle Scholar
  9. 9.
    Sato S, Hughes RC (1994) Eur J Immunol 24: 216-21.PubMedGoogle Scholar
  10. 10.
    Sato S, Hughes RC (1994) J Biol Chem 269: 4424-30.PubMedGoogle Scholar
  11. 11.
    Sato S, Hughes RC (1992) J Biol Chem 267: 6983-90.PubMedGoogle Scholar
  12. 12.
    Jeng KC, Frigeri LG, Liu F-T (1994) Immunol Letters 42: 113-16.CrossRefGoogle Scholar
  13. 13.
    Yamaoka A, Kuwabara I, Frogeri LG, Liu F-T (1995) J Immunol 154: 3479-87.PubMedGoogle Scholar
  14. 14.
    Zuberi RI, Frigeri LG, Liu F-T (1994) Cell Immunol 156: 1-12.PubMedCrossRefGoogle Scholar
  15. 15.
    Frigeri LG, Zuberi RI, Liu F-T (1993) Biochemistry 32: 7644-9.PubMedCrossRefGoogle Scholar
  16. 16.
    Truong M-T, Gruart JP, Kusnierz J-P, Papin S, Loiseau S, Capron A, Capron M (1993) J Exp Med 177: 243-8.PubMedCrossRefGoogle Scholar
  17. 17.
    Probstmeier R, Montag D, Schachner M (1995) J Neurochem 64: 2465-72.PubMedCrossRefGoogle Scholar
  18. 18.
    Rosenberg I, Cherayil BJ, Isselbacher KJ, Pillai S, (1991) J Biol Chem 266: 18731-6.PubMedGoogle Scholar
  19. 19.
    Inohara H, Raz A (1994) Biochem Biophys Res Commun 201: 1366-75.PubMedCrossRefGoogle Scholar
  20. 20.
    Koths K, Taylor E, Haenbeck R, Casipit C, Wang A (1993) J Biol Chem 268: 14245-9.PubMedGoogle Scholar
  21. 21.
    Chicheportiche Y, Vassalli P (1994) J Biol Chem 269: 5512-17.Google Scholar
  22. 22.
    Vlassara H, Li YM, Imani F, Wojciechowicz D, Yang Z, Liu F-T, Cerami A (1995) Nature Molec Med 1: 634-46.Google Scholar
  23. 23.
    Ho M-K, Springer T (1983) J Biol Chem 258: 636-42.PubMedGoogle Scholar
  24. 24.
    Mehul B, Bawumia S, Martin SR, Hughes RC (1994) J Biol Chem 269: 18250-8.PubMedGoogle Scholar
  25. 25.
    Schagger H, VonJagow G (1987) Anal Biochem 166: 368-79.PubMedCrossRefGoogle Scholar
  26. 26.
    Springer TA, Galfre G, Secher DS, Milstein C (1979) Eur J Immunol 9: 301-6.PubMedGoogle Scholar
  27. 27.
    Arnaout MA (1990) Blood 75: 1037-50.PubMedGoogle Scholar
  28. 28.
    Diamond MS, Staunton DE, Marlin SD, Springer TA (1991) Cell 65: 961-71.PubMedCrossRefGoogle Scholar
  29. 29.
    Altieri DC, Stamnes SF, Gahmberg CG, (1992) Biochem J 288: 465-73.PubMedGoogle Scholar
  30. 30.
    Asada M, Furukawa K, Kantor C, Gahmberg C, Kobata A (1991) Biochemistry 30: 1561-71.PubMedCrossRefGoogle Scholar
  31. 31.
    Chen JW, Murphy TL, Willingham MC, Pastan I, August JT, (1985) J Cell Biol 101: 85-95PubMedCrossRefGoogle Scholar
  32. 32.
    Hemler ME, Strominger JL (1982) J Immunol 129: 623-8.PubMedGoogle Scholar
  33. 33.
    MacDonald HR, Lees RK, Bron C (1985) J Immunol 135: 3944-50PubMedGoogle Scholar
  34. 34.
    Luscher B, Pousseaux M, Lees R, MacDonald HR, Bron C (1986) J Immunol 135, 3951-7.Google Scholar
  35. 35.
    Bron C, Rousseaux M, Spiazzi A-L, Macdonald HR (1986) J Immunol 137, 397-9.PubMedGoogle Scholar
  36. 36.
    Parmacek MS, Karpinski BR, Gottesdiener KM, Thompson CB, Leiden JM (1989) Nucleic Acids Res 17: 1915-32.PubMedGoogle Scholar
  37. 37.
    Michalak M, Quackenbush EJ, Letarte M (1986) J Biol Chem 261, 92-5.PubMedGoogle Scholar
  38. 38.
    Messika EJ, Avni O, Gallily R, Yefenof E, Baniyash M (1995) J Immunol 154: 6563-70.PubMedGoogle Scholar

Copyright information

© Chapman and Hall 1997

Authors and Affiliations

  • Sucai Dong
    • 1
  • R Colin Hughes
  1. 1.National Institute for Medical ResearchLondonUK

Personalised recommendations