Galectin-1 receptors in different cell types

Elola, María T.; Chiesa, María E.; Alberti, Alejandra Fernández; Mordoh, José; Fink, Nilda E.

doi:10.1007/s11373-004-8169-5

Cited by 123 publications

(118 citation statements)

References 95 publications

(109 reference statements)

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“…Gal-1 is well characterized as a lectin that can regulate cellular activity by binding specific glycoproteins on the cell surface (60,61). More recently, a role for intracellular gal-1 in regulating Ras membrane localization and downstream signaling has been reported in non-T cells (62,63).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, CD45 and CD43 represent excellent candidate gal-1 effectors. CD3, CD4, CD7, and GM1 represent alternate known gal-1 receptors with the potential to influence TCR binding and signal transduction and synaptic dynamics (13,15,19,29,60). A direct assessment of gal-1 effects on glycoprotein counterreceptor organization on CD8 T cells is necessary, because it is becoming increasingly clear that galectins can have alternate activities on distinct T cell subpopulations (8,9,69).…”

Section: Discussionmentioning

confidence: 99%

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Galectin-1 Tunes TCR Binding and Signal Transduction to Regulate CD8 Burst Size

Liu

Tomassian

Bruhn

et al. 2009

The Journal of Immunology

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T cell burst size is regulated by the duration of TCR engagement and balanced control of Ag-induced activation, expansion, and apoptosis. We found that galectin-1-deficient CD8 T cells undergo greater cell division in response to TCR stimulation, with fewer dividing cells undergoing apoptosis. TCR-induced ERK signaling was sustained in activated galectin-1-deficient CD8 T cells and antagonized by recombinant galectin-1, indicating galectin-1 modulates TCR feed-forward/feedback loops involved in signal discrimination and procession. Furthermore, recombinant galectin-1 antagonized binding of agonist tetramers to the TCR on activated OT-1 T cells. Finally, galectin-1 produced by activated Ag-specific CD8 T cells negatively regulated burst size and TCR avidity in vivo. Therefore, galectin-1, inducibly expressed by activated CD8 T cells, functions as an autocrine negative regulator of peripheral CD8 T cell TCR binding, signal transduction, and burst size. Together with recent findings demonstrating that gal-1 promotes binding of agonist tetramers to the TCR of OT-1 thymocytes, these studies identify galectin-1 as a tuner of TCR binding, signaling, and functional fate determination that can differentially specify outcome, depending on the developmental and activation stage of the T cell.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Galectin-1 Tunes TCR Binding and Signal Transduction to Regulate CD8 Burst Size

Liu

Tomassian

Bruhn

et al. 2009

The Journal of Immunology

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“…In addition to the carbohydrate-binding ability, galectin-1 associates with proteins through protein-protein interactions and participates in a variety of oncogenic processes including transformation and proliferation, cell cycle regulation, cell adhesion, metastasis, inhibition and the promotion of programmed cell death and apoptosis in activated T cells (10,11). Numerous ligands for galectin-1 have been described in different tissues and cells that include actin, laminin, fibronectin, vitronectin, integrins, CA-125, H-ras, CD45 and gemin-4 (6,(12)(13)(14)(15). Galectin-1 is expressed in a variety of cell types including breast epithelial, thymic epithelial, endothelial and dendritic cells, macrophages, fibroblasts and bone marrow cells (2,(16)(17)(18)(19)(20).…”

Section: Introductionmentioning

confidence: 99%

Varied expression and localization of multiple galectins in different cancer cell lines

Satelli

Rao²,

Gupta³

et al. 2008

Oncol Rep

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Abstract. Galectins play a key role in oncogenic processes. Although several galectins are known, their relative expression at the mRNA and protein levels, the subcellular localization, and their relationship to the oncogenic manifestation remains unclear. Herein we report a comprehensive characterization of the expression of major galectins in human breast cancer (drug-sensitive MCF-7 and drug-resistant MCF-7/Adr R ), colon cancer (HCT-116 and HT-29), and glioma (T98G) cell lines, as these cells are common model systems for studying oncogenic processes. The expected ~14.5 kDa galectin-1, predominantly cytosolic, was detected in the cancer and normal cell lines. Notably, two different molecular forms of galectin-1 with molecular masses of ~13.5 and 15 kDa were detected in T98G cells, the latter being in the extracellular medium, perhaps a result of post-translational processing. Immunocytochemistry indicated that the extracellular galectin-1 bound to the cell surface was punctated in appearance, suggesting that it was bound to specific receptors. Immunohistological studies indicated that metastasizing carcinomas express high levels of galectin-1. On the other hand, galectin-3 was readily detectable in all cancer cell lines but undetectable in normal cell lines, indicating that galectin-3 is a cancer-specific biomarker protein. Galectin-3 was a cytosolic protein but was not detected in the extracellular medium, indicating that cancer cells do not secrete this galectin. Finally, despite the RT-PCR analysis suggesting the presence of two transcripts of galectin-8 in all cancer cell lines, the corresponding ~36 kDa protein was only detectable in the nuclear and cytosolic fractions upon cell fractionation. Notably, a different molecular form of galectin-8 of ~18 kDa was immunoprecipitated from the extracellular media, suggesting that the secreted galectin-8 undergoes post-translational processing. These results highlight the expression of galectins in different molecular forms in cancers, warranting caution in interpreting the results of functional studies of individual galectins, particularly because these proteins function redundantly in cancer pathways.

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“…Only small numbers of microvessels were observed in tumors of Gal-1-null mice, indicating that Gal-1 is crucial for tumor angiogenesis (Thijssen et al, 2006). Gal-1 can bind to cell-surface receptors such as integrins (Fischer et al, 2005) and several cluster of differentiation (CD) receptors (Elola et al, 2005), and to extracellular matrix components fibronectin and laminin (Gu et al, 1994), to exert its functions extracellularly. More recently, studies have shown that various glycosylation patterns of cell surface glycoproteins on different types of T-helper and cancer cells modulate the susceptibility of these cells to Gal-1-induced apoptosis (Toscano et al, 2007;Valenzuela et al, 2007).…”

mentioning

confidence: 99%