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Review
. 2020 May 31;12(6):1421.
doi: 10.3390/cancers12061421.

Galectins and Ovarian Cancer

Chisa Shimada  1   2 , Rui Xu  1   2 , Linah Al-Alem  1   2 , Marina Stasenko  3 , David R Spriggs  1   4 , Bo R Rueda  1   2   5
Affiliations
Review

Galectins and Ovarian Cancer

Chisa Shimada et al. Cancers (Basel). .

Abstract

Ovarian cancer is known for its aggressive pathological features, including the capacity to undergo epithelial to mesenchymal transition, promoting angiogenesis, metastatic potential, chemoresistance, inhibiting apoptosis, immunosuppression and promoting stem-like features. Galectins, a family of glycan-binding proteins defined by a conserved carbohydrate recognition domain, can modulate many of these processes, enabling them to contribute to the pathology of ovarian cancer. Our goal herein was to review specific galectin members identified in the context of ovarian cancer, with emphasis on their association with clinical and pathological features, implied functions, diagnostic or prognostic potential and strategies being developed to disrupt their negative actions.

Keywords: chemoresistance; galectins; immune suppression; invasion; metastasis; ovarian cancer.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
A schematic showing the different galectin structures and members of each (A). Galectins have been shown to play a role in altering many functions in cancer, including angiogenesis, apoptosis, tumor growth, immune escape, immune cell adhesion, cell transformation and metastasis/invasion (B).
Figure 2
Figure 2
Oncogenic H-Ras plays a major role in tumor transformation via two major pathways, PI3K/AKT and MEK/ERK [73,74]. H-Ras recruits intracellular Gal-1 from the cytosol. This interaction enhances H-Ras-mediated cell transformation. Since Gal-1 has no effect on the membrane localization of inactive H-Ras, Ras activation, via GTP binding is needed for the H-Ras/Gal-1 interaction. Gal-1 is then able to enhance H-Ras-GTP, leading to an increase in Raf-1 recruitment, which culminates in a sustained activation of the MEK-ERK pathway and enhanced cell transformation [63].
Figure 3
Figure 3
Gal-3 is involved in cell adhesion regulation, migration, invasion, angiogenesis, and metastasis. The specific extracellular Gal-3 function depends on the polymerization of Gal-3 into pentameric complexes. The action of Galectin 3 depends on glycan binding partners. These complexes link to glycans of high complexity (e.g., N-glycosylation lactosamine tetra-antennary forms and the Thomsen–Fredenreich antigen on O-glycans, especially in cancer. Through carbohydrate binding and polymerization to pentamers, Gal-3 forms a lattice and regulates the position of growth factor receptors, including EGFR, integrins and proteins like MUC16.
Figure 4
Figure 4
Galectin-3 as an inhibitor of the apoptotic response. Gal-3 can translocate from the cytosol and/or the nucleus to the mitochondria, inhibiting stressors of the mitochondrial membrane potential and subsequent release of Cyt C. In response to apoptotic stimuli, Gal-3 can translocate to the mitochondria and interact with Bax and prevent its function, as well as other pro-apoptotic Bcl-2 family members, subsequently preventing the formation of pro-death promoting homodimers.
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