Homophilic Binding Properties of Galectin‐3: Involvement of the Carbohydrate Recognition Domain

Kuklinski, Stephan; Probstmeier, Rainer

doi:10.1046/j.1471-4159.1998.70020814.x

Cited by 47 publications

(34 citation statements)

References 16 publications

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Section: A Galectins Accumulate In the Cytosol: Distinct Segregationmentioning

confidence: 99%

“…1B) (6)(7)(8)(9)(10)(11)(12). In addition to N-terminal-mediated oligomerization, CRD of galectin-3 selfassociates upon binding to its ligands, thereby contributing to positive cooperativity in the formation of multivalency (8,11,(13)(14)(15). Galectins do not contain a signal sequence for transport to the secretory pathway and are synthesized by free ribosomes.…”

Section: A Galectins Accumulate In the Cytosol: Distinct Segregationmentioning

confidence: 99%

“…1B) (6-12). In addition to N-terminal-mediated oligomerization, CRD of galectin-3 selfassociates upon binding to its ligands, thereby contributing to positive cooperativity in the formation of multivalency (8,11,(13)(14)(15).Divalent or multivalent galectins cross-link membrane proteins via binding to their glycans and exert multifaceted effects, including modulation of signal transduction, membrane receptor dynamics, cell mobility and cell-cell adhesion (Figs. 1B and 2) (3,(16)(17)(18).…”

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confidence: 99%

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Cytosolic Galectins and Their Release and Roles as Carbohydrate-Binding Proteins in Host–Pathogen Interaction

Sato

2018

TIGG

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The glycocalyx is a layer of glycoconjugates found on the surface of both host cells and microorganisms. Information presented on some of the glycans on glycoconjugates is recognized by mammalian glycan-binding proteins, lectins, and these interactions modulate various physiological processes, including host innate immune responses. Lectins and host glycoconjugates are synthesized in the same secretory pathway. One notable exception is a family of soluble β-galactoside-binding lectins, galectins, which are synthesized and accumulated in the cytosol and thereby segregated from their glycan ligands. In cases where pathogenic infection persists and tissue injury occurs, galectins are passively released from injured cells. In addition, galectins are actively secreted through unconventional secretory pathways by inflammation-activated or differentiating cells. Thus, extracellular emergence of galectins is associated with the presence of pathogenic hazards. Evidence from a series of studies suggests that galectins exert multiple immunological effects. Extracellular galectin-3 acts as a damage-associated molecular pattern (DAMP) and adhesion molecule for neutrophils in lungs to initiate a proinflammatory response and to mediate rapid neutrophil migration in lungs infected with pathogenic microorganisms. In this review, the roles of galectin-3 in initial innate immune responses and resolution are discussed together with a historical overview of research on galectins in the secretory pathway and innate immunology. A. Galectins Accumulate in the Cytosol: Distinct Segregation from Glycan LigandsIn mammalian cells, the majority of glycans, i.e., oligosaccharides and polysaccharides, are covalently linked to either proteins Galectins are soluble, non-glycosylated lectins defined by a conserved carbohydrate recognition domain (CRD) that shows affinity for β-galactoside, especially glycans containing a number of lactosamine residues (Galβ1-4GlcNAc) (2-4). Detailed information on the carbohydrate binding specificity of galectins has been provided in the review by the group of Hirabayashi in the TIGG special issue 'Galectins updated' (5). In humans, 11 galectins have been identified to date (2). These proteins exhibit structural differences in the presentation of CRD (Fig. 1A). Some contain one CRD (prototype) and exist as either monomers or dimers while others (tandem repeats) contain two CRDs connected by a short linker region. Galectin-3 uniquely occurs as a chimeric protein with one CRD at the C-terminus and an additional non-CRD domain at the N-terminus, which is involved in its oligomerization.Upon binding to its glycan ligands, the conformation of galectin-3 appears altered. Subsequently, galectin-3 molecules oligomerize through self-assembly of the non-CRD domains and become multivalent in glycan binding (Fig. 1B) (6-12). In addition to N-terminal-mediated oligomerization, CRD of galectin-3 selfassociates upon binding to its ligands, thereby contributing to positive cooperativity in the formation of multivalency ...

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Section: A Galectins Accumulate In the Cytosol: Distinct Segregationmentioning

confidence: 99%

Section: A Galectins Accumulate In the Cytosol: Distinct Segregationmentioning

confidence: 99%

mentioning

confidence: 99%

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Cytosolic Galectins and Their Release and Roles as Carbohydrate-Binding Proteins in Host–Pathogen Interaction

Sato

2018

TIGG

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“…A galectina-3 é uma proteína ligante de β-galactosídeo e está envolvida em vários processos biológicos. Sua estrutura é formada por um domínio carboxiterminal que corresponde ao CRD; e por um pequeno domínio amino-terminal de ligação protéica, que contém sequências repetidas ricas em prolina, tirosina e glicina (BARONDES et al, 1994;KUKLINSKI;PROBSTMEIER, 1998).…”

Section: Lista De Ilustraçõesunclassified

“…Galectinas podem estar presentes em diversos compartimentos celulares tais como: núcleo, citosol e membrana plasmática, assim como no meio extracelular (BARONDES et al, 1994;HO;SPRINGER, 1982;KUKLINSKI;PROBSTMEIER, 1998 STAMATOGLOU; HUGHES, 1990;HAINES et al, 1983;NABARRA;PAPIERNIK, 1988;TRUONG et al, 1993).…”

Section: Lista De Ilustraçõesunclassified

Influência da galectina-3 na resposta de neutrófilos a patógenos periodontais

Garcia¹

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Influence of galectin-3 on neutrophil response to periodontal pathogensGalectin-3, a protein that binds β-galactosides, is expressed by neutrophils and numerous evidences indicate that this molecule acts as a possible regulator of the immune response. It is known that galectin-3 binding to LPS can lead to the formation of oligomers and thus changing the activation threshold of cells of the innate immune response. Although there are several studies that show the influence of galectin-3 in neutrophil response against bacterial components, the results are conflicting and inconclusive in their majority. To elucidate the influence of galectin-3 in the innate immune response to periodontal pathogens, the present study evaluated the in vitro antimicrobial activity of neutrophils, isolated from wild-type or galectin-3 deficient mice, previously stimulated with LPS of Aa and Pg. The results showed no significant differences in the number of colony forming units (CFU) recovered from cultured galectin-3 deficient neutrophils or control group. However, in a 18 hours time course of LPS stimulation, we observed reduction in the number of CFU, when compared to 3 hours of LPS stimulation.

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Galectin-3 promotes neural cell adhesion and neurite growth

et al. 1998

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Galectin-3 is a member of the galectin family and belongs to a group of soluble beta-galactoside-binding animal lectins. The molecule is expressed by neural and nonneural cells intra- (cytoplasm and nucleus) as well as extra-cellularly (plasma membrane and extracellular space). By using an in vitro cell-substratum adhesion assay, we have addressed the question whether galectin-3 present in the extracellular milieu may support the adhesion and/or neurite outgrowth of neural cells in a manner analogous to cell adhesion molecules. Galectin-3 was immobilized as a substratum and various cell types, N2A (neuroblastoma), PC12 (pheochromocytoma), and TSC (transformed Schwann cells) cell lines, neural cells from early postnatal mouse cerebellum, and dorsal root ganglion neurons from newborn mice were allowed to adhere to the lectin. Here we show that all cell types studied specifically adhered to galectin-3 by the following criteria: 1) the number of adherent cells was dependent on the galectin-3 concentration used for coating; 2) adhesion of cells to galectin-3, but not to collagen type I or laminin was inhibited by polyclonal antibodies to galectin-3; 3) upon addition of asialofetuin (a polyvalent carrier of terminal beta-galactosides) to the cell suspension prior to the adhesion assay, cell adhesion to galectin-3 was inhibited in a dose-dependent manner; and 4) cell adhesion to galectin-3 was abolished by treatment of cells with endo-beta-galactosidase. In addition, the adhesion of dorsal root ganglion neurons to galectin-3 could be inhibited by lactose. Notably, substratum-bound galectin-3 promoted the outgrowth of neurites from dorsal root ganglia explants and this neurite outgrowth promoting activity could be inhibited by polyclonal antibodies to galectin-3.

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Homophilic Binding Properties of Galectin‐3: Involvement of the Carbohydrate Recognition Domain

Abstract: Galectin-3, an animal lectin specific for fl-galactosides, is composed of three different domains. The N-terminal half of the molecule (N domain) consists of a short N-terminal segment followed by glycine-, proline-, and tyrosirie-rich tandem repeats. The C-terminal domain

Cited by 47 publications

References 16 publications

Cytosolic Galectins and Their Release and Roles as Carbohydrate-Binding Proteins in Host–Pathogen Interaction

Cytosolic Galectins and Their Release and Roles as Carbohydrate-Binding Proteins in Host–Pathogen Interaction

Influência da galectina-3 na resposta de neutrófilos a patógenos periodontais

Galectin-3 promotes neural cell adhesion and neurite growth

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