Galectin-8: a complex sub-family of galectins (Review)

Bidon, Nathalie; Brichory, Franck; Bourguet, P.; Pennec, Le; Dazord, L.

doi:10.3892/ijmm.8.3.245

Cited by 46 publications

(43 citation statements)

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“…A primary target of Gal-8 could be the sugar chains on members of the integrin family, which are abundantly expressed on the surface of leukocytes. [46][47][48][49][50] Gal-9 is able to induce decreased levels of pro-inflammatory cytokines such as IL-17, IL-12 and IFNc. Gal-9 decreases numbers of CD4(+) TIM-3(+) T cells in peripheral blood.…”

Section: Role Of Galectins In Trophoblast Invasionmentioning

confidence: 99%

REVIEW ARTICLE: Governing the Invasive Trophoblast: Current Aspects on Intra‐ and Extracellular Regulation

Fitzgerald

Germeyer

Huppertz

et al. 2010

American J Rep Immunol

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Citation Fitzgerald JS, Germeyer A, Huppertz B, Jeschke U, Knöfler M, Moser G, Scholz C, Sonderegger S, Toth B, Markert UR. Governing the invasive trophoblast: current aspects on intra‐ and extracellular regulation. Am J Reprod Immunol 2010This review summarizes several aspects especially of regulating factors governing trophoblast invasion. Those include the composition of the extracellular matrix containing a variety of matrix metalloproeinases and their inhibitors, but also intracellular signals. Furthermore, a newly described trophoblast subtype, the endoglandular trophoblast, is presented. Its presence may provide a possible mechanism for opening and connecting uterine glands into the intervillous space. Amongst others, two intracellular signalling pathways are crucial for regulation of trophoblast functions and development: Wnt‐ and signal transducer and activator of transcription (STAT)3 signalling. Wnt signalling promotes implantation, placentation and trophoblast differentiation. Several Wnt‐dependent cascades and regulatory mechanisms display different functions in trophoblast cells. The STAT3 signalling system is fundamental for induction and regulation of invasiveness in physiological trophoblastic cells, but also in tumours. The role of galectins (Gal) in trophoblast regulation and placenta development comes increasingly into focus. The Gal‐ 1–4, 7–10 and 12–14 have been detected in humans. Detailed information is only available for Gal‐1, ‐2, ‐3, ‐4, ‐9 and ‐12 in endometrium and decidua. Gal‐1, ‐3 and ‐13 (‐14) have been detected and studied in trophoblast cells.

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Section: Role Of Galectins In Trophoblast Invasionmentioning

confidence: 99%

REVIEW ARTICLE: Governing the Invasive Trophoblast: Current Aspects on Intra‐ and Extracellular Regulation

Fitzgerald

Germeyer

Huppertz

et al. 2010

American J Rep Immunol

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“…Gal-8 is one of the most widely expressed galectins in human tissues (Hadari et al, 1995;Bidon et al, 2001) and is also common in cancerous cells (Bidon-Wagner and Le Pennec 2004;Lahm et al, 2004). In the immune system Gal-8 can play important roles in the homeostasis of T- Tribulatti et al, 2007;Norambuena et al, 2009;Tribulatti et al, 2009;Tribulatti et al, 2012) and B-cells (Tsai et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Galectin-8 binds to LFA-1, blocks its interaction with ICAM-1 and is counteracted by anti-Gal-8 autoantibodies isolated from lupus patients

et al. 2013

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Galectin-8 belongs to a family of mammalian lectins that recognize glycoconjugates present on diff erent cell surface components and modulate a variety of cellular processes. A role of Gal-8 in the immune system has been proposed based on its eff ects in immune cells, including T and B lymphocytes, as well as the presence of anti-Gal-8 autoantibodies in the prototypic autoimmune disease systemic lupus erythematosus (SLE). We have previously described that Gal-8 induces apoptosis in activated T cells interacting with certain β1 integrins and this eff ect is counteracted by the anti-Gal-8 autoantibodies. Given that Gal-8 can potentially interact with several glycoproteins, here we analyzed the β2 integrin Lymphocyte Function-Associated Antigen-1 (LFA-1), which is involved in leukocyte cell adhesion and immunological synapses. We show by GST-pull down assays that Gal-8 interacts with LFA-1 and this interaction is inhibited by anti-Gal-8 autoantibodies isolated from SLE patients. In cell adhesion assays, Gal-8 precluded the interaction of LFA-1 with its ligand Intracellular Adhesion Molecule-1 (ICAM-1). These results suggest that Gal-8 can exert immunosuppressive action not only by inducing apoptosis in activated T cells but also by negatively modulating the crucial function of LFA-1 in the immune system, while function-blocking autoantibodies counteract these eff ects.

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“…Some galectin-8 splice variants consist only of the N-terminal CRD and different elongations without a second CRD. Those variants can rather be grouped to the prototypic galectins (Bidon et al, 2001;Al-Ansari et al, 2009Zick et al, 2004. Prototype galectins such as galectin-1 form homodimers through hydrophobic interactions at the N-terminal amino acid residues (Cho & Cummings, 1997;Lobsanov et al, 1993).…”

Section: Galectin Familiesmentioning

confidence: 99%

“…At least 6 different isoforms are described so far of which some only consist of the N-terminal CRD with an extension and others consist of both CRDs linked by different hinge domains (Bidon et al, 2001;Delgado et al, 2011;Zick et al, 2004). The two galectin-8 CRDs show approximately 35% sequence similarity but reveal different fine specificity for glycan structures.…”

Section: Galectin-8: Several Isoforms Of a Tandem-repeat Galectinmentioning

confidence: 99%