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. 2008 Dec;1(1):43-51.
doi: 10.1007/s12307-008-0003-6. Epub 2008 Feb 20.

Regulation of Tumor Progression by Extracellular galectin-3

Free PMC article

Regulation of Tumor Progression by Extracellular galectin-3

Pratima Nangia-Makker et al. Cancer Microenviron. .
Free PMC article


The relationship between a tumor cell and its microenvironment is bi-directional. The proteins expressed by the tumor cells alter the signatures on the seemingly normal stromal cells within the microenvironment, while the tumor cell signatures reflect the changes that occur as these cells interact with the host microenvironment. Galectin-3 is a carbohydrate-binding protein that is over-expressed in a variety of tumors and immune cells in response to various stimuli. Ever since its discovery, it has been associated with cell and extracellular matrix interactions. However, in the last decade, an extensive accumulation of data has changed the perspective of this multifunctional protein. The unique structure of this protein, consisting of a carbohydrate-binding domain and a matrix metalloproteinase cleavable domain, enables it to interact with a plethora of ligands in a carbohydrate-dependent or independent manner. It is now becoming evident that galectin-3 is involved with a variety of extracellular functions like cell adhesion, migration, invasion, angiogenesis, immune functions, apoptosis and endocytosis. Galectin-3 is a substrate for matrix metalloproteinases and its cleavage plays an important role in tumor progression and can be used as a surrogate diagnostic marker for in vivo MMP activity.


Fig. 1
Fig. 1
Extracellular functions mediated by galectin-3. The secreted galectin-3 potentiates angiogenesis by facilitating migration, chemotaxis and morphogenesis of endothelial cells. It also induces T cell apoptosis. The cell surface protein is involved with homotypic and heterotypic cell aggregation and invasion leading to metastasis. Extracellular galectin-3 cross-links cell surface glycol-conjugates, form dimers and multimers, and delivers signals inside the cell. The ∼22 kDa fragment of MMP cleaved galectin-3 binds to the glycan receptors more efficiently than the intact protein, the functions of smaller fragments are as yet unknown

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