Mammalian galectins: Structure, carbohydrate specificity, and functions

Rapoport, E. M.; Kurmyshkina, Olga; Bovin, Nicolai V.

doi:10.1134/s0006297908040032

Cited by 62 publications

(48 citation statements)

References 92 publications

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“…It is of interest to note that in a recent study, based on the findings that Gal-7-null mice show a defect in reepithelialization of skin wounds and in the distribution of cortactin (a protein localized at the lamellipodia), it has been suggested that Gal-7 modulates the formation and/or stabilization of lamellipodia (Gendronneau et al, 2008). Although all mammalian galectins specifically recognize galactose-containing glycans, each galectin has fine specificity for more complex glycans, and saccharides in the vicinity of galactose considerably influence the affinity for a given galectin (reviewed by Brewer, 2004;Hirabayashi et al, 2002;Rapoport et al, 2008). For example, the affinity of Gal-1 for the blood group A tetrasaccharide is about 100-fold lower than that for Gal-3 (Sparrow et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Galectin-3 promotes lamellipodia formation in epithelial cells by interacting with complex N-glycans on α3β1 integrin

Saravanan

Liu

Gipson

et al. 2009

Journal of Cell Science

105

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Recent studies in our laboratory have shown that galectin‐3, a β‐galactoside binding lectin, mediates re‐epithelialization of corneal wounds. In an effort to characterize the molecular mechanism by which galectin‐3 stimulates the cell migration, the goals of the present study are to: (i) characterize the lectin‐induced migratory phenotypes and Rac1 activation in corneal epithelial cells in vitro, and (ii) determine whether carbohydrate‐based interactions between galectin‐3 and integrins play a role in the lectin‐induced lamellipodia formation in corneal epithelium. Specifically, exogenous galectin‐3 but not galectin‐1, and ‐8 induced formation of lamellipodia in human corneal epithelial cells in a β‐lactose‐inhibitable manner and increased Rac1 activity. α3β1, α6β1, α6β4 and & αv‐integrins and laminin‐5 were identified as major galectin‐3‐binding proteins in corneal epithelial cells by affinity chromatography of corneal epithelial cell lysates on a galectin‐3‐Sepharose column, followed by MALDI‐TOF MS analysis. Furthermore, preincubation of cells with anti‐α3 integrin function‐blocking antibody (P1B5) significantly inhibited the galectin‐3‐induced lamellipodia. These data suggest that galectin‐3 may influence re‐epithelialization of corneal wounds by initiating the formation of lamellipodia, at least in part, through its interaction with α3β1 integrins.

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Section: Discussionmentioning

confidence: 99%

Galectin-3 promotes lamellipodia formation in epithelial cells by interacting with complex N-glycans on α3β1 integrin

Saravanan

Liu

Gipson

et al. 2009

Journal of Cell Science

105

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“…They form a molecular family composed of Ca +2 -independent soluble lectins (also known as galaptins or S-lectins)-defined by a conserved CRD that binds β-galactoside-containing glycans-and present a conserved β-sandwich structure formed by six S1-S6 and five F1-F5 strand sheets. The S4-S6 strands contain the conserved carbohydrate-binding amino acids (Hirabayashi & Kasai, 1993;Loris, 2002;Rabinovich et al, 2007;Rapoport et al, 2008;Rini & Lobsanov, 1999).…”

Section: Galectinsmentioning

confidence: 99%

Routes in Innate Immunity Evolution: Galectins and Rhamnose‐binding Lectins in Ascidians

Ballarin

Cammarata

Franchi

et al. 2013

Marine Proteins and Peptides

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“…Galectins are components of a lectin family of extensive taxonomic distribution and striking evolutionary conservation, characterized by a conserved carbohydrate recognition domain (CRD) with a relatively high affinity to β-galactosides [22,23]. They are involved in immunity, cell communication, self not-self recognition, cell proliferation, development, differentiation and malignant transformation [22][23][24][25].…”

Section: Introductionmentioning

confidence: 99%

“…They are involved in immunity, cell communication, self not-self recognition, cell proliferation, development, differentiation and malignant transformation [22][23][24][25]. Intracellular galectins participate in a wide variety of biological phenomena, and a single galectin can exert multiple roles [25,26,27].…”

Section: Introductionmentioning

confidence: 99%

In the ovary of Ciona intestinalis (Type A), immune-related galectin and phenoloxidase genes are differentially expressed by the follicle accessory cells

Parrinello¹,

Sanfratello²,

Parisi³

et al. 2018

Fish & Shellfish Immunology

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A B S T R A C TRiboprobes (in situ hybridization) and antibodies (immunohistochemistry), previously used to show the upregulation of Ciona intestinalis (Type A) galectins (CiLgals-a, CiLgals-b) and phenoloxidase (CinPO2) immunerelated genes, were tested on histological sections of the ovary. The ovarian follicles are composed of oocytes encased by follicular cells (FCs) and test cells (TCs). Results show the transcription upregulation of both CiLgals and CinPO2 genes in the vitellogenic FCs, conversely distinct cytolocalization of the proteins are shown. At vitellogenic stage, the CiLgals are localized in the FCs, in the oocyte cytoplasm, and close to the germinal vesicle (GV), whereas the CinPO2 was never identified in the FCs. In a presumptive advanced phase and at the postvitellogenic stage the TCs appear to be labelled by the CinPO2 riboprobe, and the protein identified by the antibody suggesting an mRNA transcytosis process from FCs. At post-vitellogenic stage the CiLgals mainly enrich the GV nucleoplasm, whereas the CinPO2 is contained in TCs and in the ooplasm but never found in the GV. This finding sheds new light on a former paper in which TCs were reported to be the only CinPO2-producing cells in the ovarian follicle. Finally, CiLgals and CinPO2 genes transcription and proteins production seem to be associated with accessory cells during their differentiation from vitellogenic to post-vitellogenic stage. The present findings promote further research on the early upregulation of immune-related genes, and the potential multifunctional role of the produced proteins. In addition further insight on the accessory cells involvement in ascidian oogenesis are reported.

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Mammalian galectins: Structure, carbohydrate specificity, and functions

Cited by 62 publications

References 92 publications

Galectin-3 promotes lamellipodia formation in epithelial cells by interacting with complex N-glycans on α3β1 integrin

Galectin-3 promotes lamellipodia formation in epithelial cells by interacting with complex N-glycans on α3β1 integrin

Routes in Innate Immunity Evolution: Galectins and Rhamnose‐binding Lectins in Ascidians

In the ovary of Ciona intestinalis (Type A), immune-related galectin and phenoloxidase genes are differentially expressed by the follicle accessory cells

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