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. 2020 Apr;53(4):173-180.
doi: 10.5483/BMBRep.2020.53.4.020.

Non-classical Role of Galectin-3 in Cancer Progression: Translocation to Nucleus by Carbohydrate-Recognition Independent Manner

Free PMC article

Non-classical Role of Galectin-3 in Cancer Progression: Translocation to Nucleus by Carbohydrate-Recognition Independent Manner

Seok-Jun Kim et al. BMB Rep. .
Free PMC article


Galectin-3 is a carbohydrate-binding protein and regulates diverse functions, including cell proliferation and differentiation, mRNA splicing, apoptosis induction, immune surveillance and inflammation, cell adhesion, angiogenesis, and cancer-cell metastasis. Galectin-3 is also recommended as a diagnostic or prognostic biomarker of various diseases, including heart disease, kidney disease, and cancer. Galectin-3 exists as a cytosol, is secreted in extracellular spaces on cells, and is also detected in nuclei. It has been found that galectin-3 has different functions in cellular localization: (i) Extracellular galectin-3 mediates cell attachment and detachment. (ii) cytosolic galectin-3 regulates cell survival by blocking the intrinsic apoptotic pathway, and (iii) nuclear galectin-3 supports the ability of the transcriptional factor for target gene expression. In this review, we focused on the role of galectin-3 on translocation from cytosol to nucleus, because it happens in a way independent of carbohydrate recognition and accelerates cancer progression. We also suggested here that intracellular galecin-3 could be a potent therapeutic target in cancer therapy. [BMB Reports 2020; 53(4): 173-180].

Conflict of interest statement


The authors have no conflicting interests.


Fig. 1
Fig. 1
Structure of galectin-3. Galectin-3 consists of an N-terminal Domain (NTD), which has an N-terminal Region of 12 amino acids (aa) and a PGAY repeat motif (12-115aa). The carbohydrate-recognition domain (CRD) 130 aa comprises the C-terminal. Each domain describes a binding motif and signaling pathway.
Fig. 2
Fig. 2
Schematic model of mechanism of galectin-3 in cancer progression and metastasis. Galectin-3 bound various transcription factors, such as AP-1, HSF-1, C/EBPβ, and TCF4/LEF1, and regulates cancer progression and cell motility.

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    1. Dumic J, Dabelic S, Flogel M. Galectin-3: an open-ended story. Biochim Biophys Acta. 2006;1760:616–635. doi: 10.1016/j.bbagen.2005.12.020. - DOI - PubMed
    1. Leffler H, Carlsson S, Hedlund M, Qian Y, Poirier F. Introduction to galectins. Glycoconj J. 2002;19:433–440. doi: 10.1023/B:GLYC.0000014072.34840.04. - DOI - PubMed
    1. Drickamer K, Fadden AJ. Genomic analysis of C-type lectins. Biochem Soc Symp. 2002;69:59–72. doi: 10.1042/bss0690059. - DOI - PubMed
    1. Liu FT, Rabinovich GA. Galectins as modulators of tumour progression. Nat Rev Cancer. 2005;5:29–41. doi: 10.1038/nrc1527. - DOI - PubMed
    1. Fortuna-Costa A, Gomes AM, Kozlowski EO, Stelling MP, Pavao MS. Extracellular galectin-3 in tumor progression and metastasis. Front Oncol. 2014;4:138. doi: 10.3389/fonc.2014.00138. - DOI - PMC - PubMed