Abstract
Galectin-3 is a member of a family of carbohydrate-binding proteins. It is present in the nucleus, the cytoplasm, and also the extracellular matrix (ECM) of many normal and neoplastic cell types. Reports show an upregulation of this protein in transformed and metastatic cell lines (Raz and Lotan Cancer Metastasis Rev 6: 433–452, 1987; Raz et al. Int J Cancer 46: 871–877, 1990). Moreover, in many human carcinomas, an increased expression of galectin-3 correlates with progressive tumor stages (Lotan et al. Int J Cancer 56: 474–480, 1994; Bresalier et al. Gastroenterology 115: 287–296, 1998; Nangia-Makker et al. Int J Oncol 7: 1079–1087, 1995; Xu et al. Am J Pathol 147: 815–822, 1995).
Several lines of analysis have demonstrated that the galectins participate in cell–cell and cell–matrix interactions by recognizing and binding complementary glycoconjugates and thereby play a crucial role in normal and pathological processes. Elevated expression of the protein is associated with an increased capacity for anchorage-independent growth, homotypic aggregation, and tumor cell lung colonization (Lotan et al. Cancer Res 45: 4349–4353, 1985; Lotan and Raz J Cell Biochem 37: 107–117, 1988; Meromsky et al. Cancer Res 46: 5270–5275, 1986). In this chapter we describe the methods of purification of galectin-3 from transformed Escherichia coli and some of the commonly used functional assays for analyzing galectin-3 binding.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Raz A, Lotan R (1987) Endogenous galactoside-binding lectins: a new class of functional tumor cell surface molecules related to metastasis. Cancer Metastasis Rev 6:433–452
Raz A, Zhu DG, Hogan V, Shah N, Raz T, Karkash R, Pazerini G, Carmi P (1990) Evidence for the role of 34-kDa galactoside-binding lectin in transformation and metastasis. Int J Cancer 46:871–877
Lotan R, Ito H, Yasui W, Yokozaki H, Lotan D, Tahara E (1994) Expression of a 31-kDa lactoside-binding lectin in normal human gastric mucosa and in primary and metastatic gastric carcinomas. Int J Cancer 56:474–480
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
Nangia-Makker P, Thompson E, Hogan V, Ochieng J, Raz A (1995) Induction of tumorigenicity by galectin-3 in a non-tumorigenic human breast carcinoma cell line. Int J Oncol 7:1079–1087
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
Lotan R, Lotan D, Raz A (1985) Inhibition of tumor cell colony formation in culture by a monoclonal antibody to endogenous lectins. Cancer Res 45:4349–4353
Lotan R, Raz A (1988) Endogenous lectins as mediators of tumor cell adhesion. J Cell Biochem 37:107–117
Meromsky L, Lotan R, Raz A (1986) Implications of endogenous tumor cell surface lectins as mediators of cellular interactions and lung colonization. Cancer Res 46:5270–5275
Barondes SH, Castronovo V, Cooper DN, Cummings RD, Drickamer K, Feizi T, Gitt MA, Hirabayashi J, Hughes C, Kasai K et al (1994) Galectins: a family of animal beta-galactoside-binding lectins. Cell 76:597–598
Dumic J, Dabelic S, Flögel M (2006) Galectin-3: an open-ended story. Biochim Biophys Acta 1760:616–635
Gong HC, Honjo Y, Nangia-Makker P, Hogan V, Mazurak N, Bresalier RS, Raz A (1999) The NH2 terminus of galectin-3 governs cellular compartmentalization and functions in cancer cells. Cancer Res 59:6239–6245
Ochieng J, Fridman R, Nangia-Makker P, Kleiner DE, Liotta LA, Stetler-Stevenson WG, Raz A (1994) Galectin-3 is a novel substrate for human matrix metalloproteinases-2 and -9. Biochemistry 33:14109–14114
Akahani S, Nangia-Makker P, Inohara H, Kim HR, Raz A (1997) Galectin-3: a novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family. Cancer Res 57:5272–5276
Davidson PJ, Li SY, Lohse AG, Vandergaast R, Verde E, Pearson A, Patterson RJ, Wang JL, Arnoys EJ (2006) Transport of galectin-3 between the nucleus and cytoplasm. I. Conditions and signals for nuclear import. Glycobiology 16:602–611
Li SY, Davidson PJ, Lin NY, Patterson RJ, Wang JL, Arnoys EJ (2006) Transport of galectin-3 between the nucleus and cytoplasm. II. Identification of the signal for nuclear export. Glycobiology 16:612–622
van den Brule FA, Waltregny D, Liu FT, Castronovo V (2000) Alteration of the cytoplasmic/nuclear expression pattern of galectin-3 correlates with prostate carcinoma progression. Int J Cancer 89:361–367
Hughes RC (1999) Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta 1473:172–185
Nickel W (2005) Unconventional secretory routes: direct protein export across the plasma membrane of mammalian cells. Traffic 6:607–614
Nangia-Makker P, Balan V, Raz A (2008) Regulation of tumor progression by extracellular galectin-3. Cancer Microenviron 1: 43–51
Ochieng J, Furtak V, Lukyanov P (2004) Extracellular functions of galectin-3. Glycoconj J 19:527–535
Dong S, Hughes RC (1997) Macrophage surface glycoproteins binding to galectin-3 (Mac-2-antigen). Glycoconj J 14:267–274
Raz A, Meromsky L, Zvibel I, Lotan R (1987) Transformation-related changes in the expression of endogenous cell lectins. Int J Cancer 39:353–360
Warfield PR, Makker PN, Raz A, Ochieng J (1997) Adhesion of human breast carcinoma to extracellular matrix proteins is modulated by galectin-3. Invasion Metastasis 17:101–112
Lotan R, Raz A (1983) Low colony formation in vivo and in culture as exhibited by metastatic melanoma cells selected for reduced homotypic aggregation. Cancer Res 43:2088–2093
Inohara H, Raz A (1994) Effects of natural complex carbohydrate (citrus pectin) on murine melanoma cell properties related to galectin-3 functions. Glycoconj J 11:527–532
Nangia-Makker P, Wang Y, Raz T, Tait L, Balan V, Hogan V, Raz A (2010) Cleavage of galectin-3 by matrix metalloproteases induces angiogenesis in breast cancer. Int J Cancer 127:2530–2541
Cifone MA, Fidler IJ (1980) Correlation of patterns of anchorage-independent growth with in vivo behavior of cells from a murine fibrosarcoma. Proc Natl Acad Sci USA 77:1039–1043
Acknowledgements
This work was supported by NIH R37CA46120-19 (A. Raz).
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2012 Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Nangia-Makker, P., Balan, V., Raz, A. (2012). Galectin-3 Binding and Metastasis. In: Dwek, M., Brooks, S., Schumacher, U. (eds) Metastasis Research Protocols. Methods in Molecular Biology, vol 878. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-854-2_17
Download citation
DOI: https://doi.org/10.1007/978-1-61779-854-2_17
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-61779-853-5
Online ISBN: 978-1-61779-854-2
eBook Packages: Springer Protocols