Monocyte Migration Driven by Galectin-3 Occurs through Distinct Mechanisms Involving Selective Interactions with the Extracellular Matrix

Polli, Claudia; Toledo, Karina Alves; Franco, Luis H.; Mariano, Vânia Sammartino; Oliveira, Leandro Licursi de; Bernardes, Emerson Soares; Roque‐Barreira, Maria Cristina; Pereira-da-Silva, Gabriela

doi:10.1155/2013/259256

Cited by 24 publications

(16 citation statements)

References 31 publications

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“…Several lines of evidence have pointed to the relevance of galectin-3 in cell adhesion and motility 27,28 . This possibility was tested in HTR-8/SVneo cells using cell adhesion and migration assays (Fig.…”

Section: Resultsmentioning

confidence: 99%

Human trophoblast requires galectin-3 for cell migration and invasion

Bojić‐Trbojević

Krivokuća

Vilotić

et al. 2019

Sci Rep

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Invasive extravillous cytotrophoblast of the human placenta expresses galectins-1, -3, and -8 in vivo and in vitro. This study aimed to investigate the potential role of galectin-3 in cell migration and invasion, using recombinant human galectin-3 (rhgalectin-3), small molecule galectin inhibitor I47, and galectin-3 silencing. HTR-8/SVneo cell migration was stimulated by rhgalectin-3 and reduced by I47, which could be neutralised by rhgalectin-3. Inhibitor specificity and selectivity for the galectins expressed in extravillous trophoblast were validated in solid phase assays using recombinant galectin-1, -3, -8, confirming selectivity for galectin-3. HTR-8/SVneo cell migration and invasion, and invasion by isolated trophoblast cells in primary culture were significantly reduced in the presence of I47, which could be restored by rhgalectin-3. Upon HTR-8/SVneo cell treatment with galectin-3 siRNA both LGALS3 and galectin-3 protein were dramatically decreased. Silencing of galectin-3 induced significant reduction in cell migration and invasion, which was restored by rhgalectin-3. The influence on known mediators of cell invasion, MMP2 and -9, and integrins α1, α5, and β1 was followed in silenced cells, showing lower levels of MMPs and a large reduction in integrin subunit β1. These results show that galectin-3 acts as a pro-invasive autocrine/paracrine factor in trophoblast in vitro.

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Section: Resultsmentioning

confidence: 99%

Human trophoblast requires galectin-3 for cell migration and invasion

Bojić‐Trbojević

Krivokuća

Vilotić

et al. 2019

Sci Rep

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“…Galectin‐3 has been implicated in a variety of physiological and pathological processes. In inflammation, galectin‐3 has evolved as an important regulatory mediator, shown by its capacity to promote cell adhesion, enhance phagocytosis, and induce production of NADPH‐oxidase‐derived ROS in human neutrophils …”

Section: Introductionmentioning

confidence: 99%

Galectin-3 type-C self-association on neutrophil surfaces; The carbohydrate recognition domain regulates cell function

Sundqvist

Welin

Elmwall

et al. 2018

Journal of Leukocyte Biology

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Summary sentence: Galectin-3 is cleaved by both neutrophils and bacteria and the residual galectin-3C inhibits galectin-3-induced neutrophil activity but potentiates galectin-3 cell-surface binding. AbstractGalectin-3 is an endogenous -galactoside-binding lectin comprising a carbohydrate recognition domain (CRD) linked to a collagen-like N-domain. Both domains are required for galectin-3 to induce cellular effects; a C-terminal fragment of galectin-3, galectin-3C, containing the CRD but lacking the N-domain, binds cell surface glycoconjugates but does not induce cellular effects since cross-linking promoted by the N-domain is thought to be required. Instead, galectin-3C is proposed to antagonize the effects of galectin-3 by competing for binding sites. The aim of this study was to investigate the effects of galectin-3C on galectin-3 interactions with human neutrophils.Recombinant galectin-3C inhibited galectin-3-induced production of reactive oxygen species in primed neutrophils. Surprisingly, this inhibition was not due to competitive inhibition of galectin-3 binding to the cells. In contrast, galectin-3C potentiated galectin-3 binding, in line with emerging evidence that galectin-3 can aggregate not only through the N-domain but also through the CRD. The cell surface interaction between galectin-3C and galectin-3 was corroborated by colocalization of fluorescently labeled galectin-3 and galectin-3C. Galectin-3C can be generated in vivo through cleavage of galectin-3 by proteases. Indeed, in circulation, galectin-3 and galectin-3C were both attached to the cell surface of neutrophils, which displayed great capacity to bind additional galectin-3 and galectin-3C. In conclusion, galectin-3C enhances galectin-3 binding to neutrophils by nonactivating type-C self-association, in parallel to inhibiting neutrophil activation by galectin-3 (induced by type-N self-association). This implicates type-C self-association as a termination system for galectin-3-induced cell activation, with the purpose of avoiding oxidantdependent tissue damage.

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“…In vitro, galectin-3 induces the expression of L-selectin and IL-8 by neutrophils, suggesting that it can modulate neutrophil migration and activation (Nieminen et al, 2005). Galectin-3 is also involved in the recruitment of monocytes/macrophages from the blood stream to the inflamed tissue through interactions with laminin and fibronectin, but the underlying mechanisms are not fully understood (Danella Polli et al, 2013). Studies with different inflammation models have revealed that the lack of galectin-3 decreases the mobilization and activation of neutrophils and macrophages in tissues, with consequent reduction in the expression of pro-inflammatory cytokines and chemokines (Alves et al, 2010(Alves et al, , 2012Brand et al, 2012;Nieminen et al, 2005;Rotshenker et al, 2008;Sano et al, 2003).…”

Section: Introductionmentioning

confidence: 99%