Galectins and Gliomas

Mercier, Marie Le; Fortin, Shannon P.; Mathieu, VÃ©ronique; Kiss, Róbert; Lefranc, Florence

doi:10.1111/j.1750-3639.2009.00270.x

Cited by 98 publications

(75 citation statements)

References 131 publications

(233 reference statements)

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“…Both Galectins 1 and 3 are prominently expressed in adult NSCs and reactive astrocytes (Beckervordersandforth et al, 2010; Di Lella et al, 2011; Kajitani et al, 2009; Sakaguchi et al, 2006; Yan et al, 2009), and their expression levels also increase after other injuries, including middle cerebral artery occlusion (MCAo) (Qu et al, 2011; Young et al, 2014; Zamanian et al, 2012) and cancer (for review, see Camby et al, 2006; Griffioen and Thijssen, 2014; LeMercier et al, 2010; Newlaczyl and Yu, 2011). Interestingly, Lgals3 expression is not increased upon LPS stimulation, an injury condition with limited proliferative response of reactive astrocytes (Zamanian et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Astrocyte reactivity after brain injury—: The role of galectins 1 and 3

Sirko

Irmler

Gascón

et al. 2015

Glia

109

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Astrocytes react to brain injury in a heterogeneous manner with only a subset resuming proliferation and acquiring stem cell properties in vitro. In order to identify novel regulators of this subset, we performed genomewide expression analysis of reactive astrocytes isolated 5 days after stab wound injury from the gray matter of adult mouse cerebral cortex. The expression pattern was compared with astrocytes from intact cortex and adult neural stem cells (NSCs) isolated from the subependymal zone (SEZ). These comparisons revealed a set of genes expressed at higher levels in both endogenous NSCs and reactive astrocytes, including two lectins—Galectins 1 and 3. These results and the pattern of Galectin expression in the lesioned brain led us to examine the functional significance of these lectins in brains of mice lacking Galectins 1 and 3. Following stab wound injury, astrocyte reactivity including glial fibrillary acidic protein expression, proliferation and neurosphere‐forming capacity were found significantly reduced in mutant animals. This phenotype could be recapitulated in vitro and was fully rescued by addition of Galectin 3, but not of Galectin 1. Thus, Galectins 1 and 3 play key roles in regulating the proliferative and NSC potential of a subset of reactive astrocytes. GLIA 2015;63:2340–2361

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Section: Discussionmentioning

confidence: 99%

Astrocyte reactivity after brain injury—: The role of galectins 1 and 3

Sirko

Irmler

Gascón

et al. 2015

Glia

109

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“…Accumulating experimental and clinical evidence has revealed that galectin-3 has distinctive expression patterns and plays critical roles in various pathological conditions, including cancer (6,(37)(38)(39)(40). Galectin-3 appears to function through both intracellular and extracellular actions, thereby modulating health and disease (1).…”

Section: Discussionmentioning

confidence: 99%

Galectin-3 Exerts Cytokine-Like Regulatory Actions through the JAK–STAT Pathway

Jeon

Yoon

Chang

et al. 2010

The Journal of Immunology

158

105

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Galectin-3, a β-galactoside–binding lectin, has been proposed to have multifaceted functions in various pathophysiological conditions. However, the characteristics of galectin-3 and its molecular mechanisms of action are still largely unknown. In this study, we show that galectin-3 exerts cytokine-like regulatory actions in rat and mouse brain-resident immune cells. Both the expression of galectin-3 and its secretion into the extracellular compartment were significantly enhanced in glia under IFN-γ–stimulated, inflamed conditions. After exposure to galectin-3, glial cells produced high levels of proinflammatory mediators and exhibited activated properties. Notably, within minutes after exposure to galectin-3, JAK2 and STAT1, STAT3, and STAT5 showed considerable enhancement of tyrosine phosphorylation; thereafter, downstream events of STAT signaling were also significantly enhanced. Treatment of the cells with pharmacological inhibitors of JAK2 reduced the galectin-3–stimulated increases of inflammatory mediators. Using IFN-γ receptor 1–deficient mice, we further found that IFN-γR 1 might be required for galectin-3–dependent activation of the JAK–STAT cascade. However, galectin-3 significantly induced phosphorylation of STATs in glial cells from IFN-γ–deficient mice, suggesting that IFN-γ does not mediate activation of STATs. Collectively, our findings suggest that galectin-3 acts as an endogenous danger signaling molecule under pathological conditions in the brain, providing a potential explanation for the molecular basis of galectin-3–associated pathological events.

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“…Gal-1 also modulates the expression of six other hypoxia-related genes that are implicated in angiogenesis (i.e., CTGF, ATF3 (activating transcription factor 3), PPP1R15A (protein phosphate 1 regulatory subunity 15A), HSPA5 (heat shock protein family A member 5), TRA1 (transcription-associated protein 1) and CYR61 (cysteine rich angiogenic inducer 61) [200]. Clausse et al have also previously shown that galectin-1 was upregulated in capillaries associated with carcinoma cells, and could mediate interactions between tumors and endothelial cells in vitro , suggesting a potential role for Gal-1 in modulating angiogenesis [201, 202]. …”

Section: Hypoxia Alters Cell Location Of Galectins and Interaction Wimentioning

confidence: 99%

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Silva-filho¹,

Sena²,

Lima

et al. 2017

Cell Physiol Biochem

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Post-translational and co-translational enzymatic addition of glycans (glycosylation) to proteins, lipids, and other carbohydrates, is a powerful regulator of the molecular machinery involved in cell cycle, adhesion, invasion, and signal transduction, and is usually seen in both in vivo and in vitro cancer models. Glycosyltransferases can alter the glycosylation pattern of normal cells, subsequently leading to the establishment and progression of several diseases, including cancer. Furthermore, a growing amount of research has shown that different oxygen tensions, mainly hypoxia, leads to a markedly altered glycosylation, resulting in altered glycan-receptor interactions. Alteration of intracellular glucose metabolism, from aerobic cellular respiration to anaerobic glycolysis, inhibition of integrin 3α1β translocation to the plasma membrane, decreased 1,2-fucosylation of cell-surface glycans, and galectin overexpression are some consequences of the hypoxic tumor microenvironment. Additionally, increased expression of gangliosides carrying N-glycolyl sialic acid can also be significantly affected by hypoxia. For all these reasons, it is possible to realize that hypoxia strongly alters glycobiologic events within tumors, leading to changes in their behavior. This review aims to analyze the complexity and importance of glycoconjugates and their molecular interaction network in the hypoxic context of many solid tumors.

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Galectins and Gliomas

Cited by 98 publications

References 131 publications

Astrocyte reactivity after brain injury—: The role of galectins 1 and 3

Astrocyte reactivity after brain injury—: The role of galectins 1 and 3

Galectin-3 Exerts Cytokine-Like Regulatory Actions through the JAK–STAT Pathway

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

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