Skip to main content

Advertisement

Log in

Expression of galectin-3 in primary and metastatic melanoma: immunohistochemical studies on human lesions and nude mice xenograft tumors

  • Original Paper
  • Published:
Archives of Dermatological Research Aims and scope Submit manuscript

Abstract

Galectins are a large family of proteins which bind galactoside-containing glycans. Their role in cancer seems to be important since members of the family may mediate cell adhesion and modulate cell growth. Galectin-3 (Gal-3) is expressed in the nucleus, in the cytoplasm and on the cell surface, and can also be secreted into the extracellular matrix. A series of experimental and clinical data have been reported which indicate that Gal-3 may play a putative role in carcinogenesis, cancer progression and the process of metastasis. To study the possible correlation between Gal-3 expression and malignant potential in primary melanoma lesions, we conducted an immunohistochemical study with monoclonal anti-Gal-3 antibody in a series of primary and metastatic melanoma lesions as well as benign skin pigmented lesions. We also developed a xenograft melanoma model in nude mice with two melanoma cell lines (ATCC G-361 and ATCC HT-144) and assessed staining with the Gal-3 antibody in the xenografts and the metastases. The expression of anti-Gal-3 staining was determined semiquantitatively. The expression of Gal-3 was higher in thin primary melanoma lesions than in benign pigmented skin lesions or metastases and seemed to correlate inversely with the aggressiveness as estimated by the Breslow index which is recognized as the main prognostic factor in melanoma. We propose Gal-3 expression in melanoma as a diagnostic and/or a prognostic parameter and suggest that further studies of such a role for Gal-3 are warranted.

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

Access this article

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

Instant access to the full article PDF.

Fig. 1
Fig. 2

Similar content being viewed by others

References

  1. Barondes SH, Castronovo V, Cooper DN, Cummings RD, Drickamer K, Feizi T, Gitt MA, Hirabayashi J, Hugues C, Kasai K (1994) Galectins: a family of animal beta-galactoside-binding lectins. Cell 76:597–598

    Article  Google Scholar 

  2. Loris R (2002) Principles of structures of animal and plant lectins. Biochim Biophys Acta 1572:198–208

    Google Scholar 

  3. Yang RY, Liu FT (2003) Galectins in cell growth and apoptosis. Cell Mol Life Sci 60(2):267–276

    Article  Google Scholar 

  4. Barondes SH (1997) Galectins: a personal overview. Trends Glycosci Glycotechnol 9(45):1–7

    Google Scholar 

  5. Barondes SH, Cooper DNW, Gitt MA, Leffler H (1994) Galectins: structure and function of a large family of animal lectins. J Biol Chem 269(33):20807–20810

    CAS  PubMed  Google Scholar 

  6. Hughes RC (1999) Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta 1473:172–185

    Google Scholar 

  7. Hughes RC (2001) Galectins as modulators of cell adhesion. Biochimie 83:667–676

    Article  Google Scholar 

  8. Ochieng J, Green B, Evans S, James O, Warfield P (1998) Modulation of the biological functions of galectin-3 by matrix metalloproteinases. Biochim Biophys Acta 1379:97–106

    Google Scholar 

  9. Perillo NL, Marcus ME, Baum LG (1998) Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death. J Mol Med 76:402–412

    Article  CAS  PubMed  Google Scholar 

  10. Liu FT, Patterson RJ, Wang JL (2002) Intracellular functions of galectins. Biochim Biophys Acta 1572:263–273

    Google Scholar 

  11. Akahani S, Inohara H, Nangia-Makker P, Raz A (1997) Galectin-3 in tumor metastasis. Trends Glycosci Glycotechnol 9(45):69–75

    Google Scholar 

  12. Danguy A, Camby I, Kiss R (2002) Galectins and cancer. Biochim Biophys Acta 1572:285–293

    Google Scholar 

  13. Xu XC, El-Naggar AK, Lotan R (1995) Differential expression of galectin-1 and galectin-3 in thyroid tumors: potential diagnostic implications. Am J Pathol 147:815–822

    CAS  PubMed  Google Scholar 

  14. Bresalier RS, Mazurek N, Sternberg LR, Byrd JC, Yunker CK, Nangia Makker P, Raz A (1998) Metastasis of human colon cancer is altered by modifying expression of the beta-galactoside-binding protein galectin-3. Gastroenterology 115:287–296

    Google Scholar 

  15. Lotz MM, Andrews CW Jr, Korzelius CA, Lee EC, Steele GD Jr, Clarke A, Mercurio AM (1993) Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma. Proc Natl Acad Sci U S A 90:3466–3470

    Google Scholar 

  16. Schoeppner HL, Raz A, Ho SB, Bresalier RS (1995) Expression of an endogenous galactose-binding lectin correlates with neoplastic progression in the colon. Cancer 75:2818–2826

    Google Scholar 

  17. Inohara H, Raz A (1994) Effects of natural complex carbohydrate (citrus pectin) on melanoma cell properties related to galectin-3 functions. Glycoconj J 11(6):527–532

    Article  Google Scholar 

  18. Seidal T, Balaton AJ, Battifora H (2001) Interpretation and quantification of immunostains. Am J Surg Pathol 25(9):1204–1207

    Article  Google Scholar 

  19. Wick MR, Mills SE (2001) Consensual interpretive guidelines for diagnostic immunochemistry. Am J Surg Pathol 25(9):1208–1210

    Article  Google Scholar 

  20. Price JE (2001) Xenograft models in immunodeficient animals. In: Brooks SA, Schumacher U (eds) Metastasis research protocols, vol II, Analysis of cell behaviour in vitro and in vivo. Humana Press, Totowa, pp 205–213

  21. Balch CM, Buzaid AC, Soong SJ, Atkins MB, Cascinelli M, Coit DG, Fleming ID, Gershenwald JE, Houghton A Jr, Kirkwood JM, McMasters KM, Mihm MF, Morton DL, Reintgen DS, Ross MI, Sober A, Thompson JA, Thompson JF (2001) Final version of the American-Joint Committee on cancer staging system for cutaneous melanoma. J Clin Oncol 19(16):3622–3634

    CAS  PubMed  Google Scholar 

  22. Breslow A (1989) Prognosis in cutaneous melanoma: tumor thickness as a guide to treatment. Pathol Annu 24:383–407

    Google Scholar 

  23. Mey A, Berthier-Vergnes O, Apoil PA, Doré JF, Revillard JP (1994) Expression of the galactose binding protein Mac-2 by human melanoma cell lines. Cancer Lett 81:155–163

    Article  Google Scholar 

  24. Santa Lucia P, Wilson BD, Allen HJ (1991) Localization of endogenous beta-galactoside-binding lectin as means to distinguish malignant from benign skin tissue. J Dermatol Surg Oncol 17(8):653–655

    Google Scholar 

  25. Kageshita T, Kashio Y, Yamauchi A, Seki M, Abedin MJ, Nishi N, Shoji H, Nakamura T, Ono T, Hirashima M (2002) Possible role of galectin-9 in cell aggregation and apoptosis of human melanoma cell lines and its clinical significance. Int J Cancer 99(6):806–816

    Article  Google Scholar 

  26. Legendre H, Decaestecker C, Nagy N, Hendlisz A, Schüring MP, Salmon I, Gabius HJ, Pector JC, Kiss R (2003) Prognostic values of galectin-3 and the macrophage inhibitory factor (MIF) in human colorectal cancers. Mod Pathol 16(5):491–504

    Article  Google Scholar 

  27. Castronovo V, Van Den Brûle FA, Jackers P, Clausse N, Liu FT, Gillet C, Sobel ME (1996) Decreased expression of galectin-3 is associated with progression of human breast cancer. J Pathol 179:43–48

    Article  Google Scholar 

  28. Matarrese P, Fusco O, Tinari N, Natoli C, Liu FT, Semeraro ML, Malorni W, Iacobelli S (2000) Galectin-3 overexpression protects from apoptosis by improving cell adhesion properties. Int J Cancer 85(4):545–554

    Article  Google Scholar 

  29. Woo HJ, Shaw LM, Messier JM, Mercurio AM (1990) The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2). J Biol Chem 265:7097–7099

    Google Scholar 

  30. Johnson JP (1999) Cell adhesion molecules in the development and progression of malignant melanoma. Cancer Metastasis Rev 18:345–357

    Article  Google Scholar 

  31. Warfield PR, Makker PN, Raz A, Ochieng J (1997) Adhesion of human breast carcinoma to extracellular matrix proteins is modulated by galectin-3. Invas Metast 17:101–112

    Google Scholar 

  32. Debray C, Vereecken P, Belot N, Teillard P, Brion JP, Pandolfo M, Pochet R (2004) Multifaceted role of galectin-3 on human glioblastoma cell motility. Biochem Biophys Res Commun 325:1393–1398

    Article  Google Scholar 

  33. Ochieng J, Leite-Browning ML, Warfield P (1998) Regulation of cellular adhesion to extracellular matrix proteins by galectin-3. Biochem Biophys Res Commun 246:788–791

    Article  Google Scholar 

Download references

Acknowledgements

This work was supported by an Erasmus Foundation grant (P.V.) and by a grant from the Fonds pour la Formation à la Recherche dans l’Industrie et dans l’Agriculture (F.R.I.A.) (C.D.).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Pierre Vereecken.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Vereecken, P., Debray, C., Petein, M. et al. Expression of galectin-3 in primary and metastatic melanoma: immunohistochemical studies on human lesions and nude mice xenograft tumors. Arch Dermatol Res 296, 353–358 (2005). https://doi.org/10.1007/s00403-004-0536-6

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00403-004-0536-6

Keywords

Navigation