Immunoprecipitation of spliceosomal RNAs by antisera to galectin-1 and galectin-3

Wang, Weizhong; Park, Jung W.; Wang, John L.; Patterson, Ronald J.

doi:10.1093/nar/gkl673

Cited by 42 publications

(51 citation statements)

References 22 publications

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“…Our data provide strong evidence that the reduction of contact allergy responses induced by galectin-2 injections was primarily mediated by impaired CD8 ϩ T cell effector function. T cell-mediated autoimmune or delayed-type hypersensitivity responses can be suppressed by regulatory CD4 ϩ CD25 ϩ T cells (47). Indeed, galectin-1 treatment reduced the development of experimental autoimmune uveitis in mice (40).…”

Section: Discussionmentioning

confidence: 99%

Galectin-2 Suppresses Contact Allergy by Inducing Apoptosis in Activated CD8+ T Cells

Loser

Sturm

Voskort³

et al. 2009

The Journal of Immunology

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Galectins, a family of structurally related β-galactoside-binding proteins, are expressed by various cells of the immune systems and seem to be important for the regulation of immune responses and immune cell homeostasis. Since it has been demonstrated that galectin-2 regulates cell-mediated inflammatory bowel disease and colitis in mice, we intended to investigate the role of galectin-2 in inflammatory cutaneous T cell-mediated immune responses. To address this issue, groups of naive mice were sensitized to the contact allergen 2,4-dinitro-1-fluorobenzene and systemically treated with galectin-2 to analyze the effects of galectin-2 on contact allergy. Here we show that galectin-2 is expressed in murine skin and is up-regulated upon cutaneous inflammation. Interestingly, treatment of mice with galectin-2 significantly reduced the contact allergy response. This effect was long-lasting since rechallenge of galectin-2-treated mice after a 14-day interval still resulted in a decreased ear swelling. We were able to demonstrate that galectin-2 induced a reduction of MHC class I-restricted immune responses in the treated animals, which was mediated by the induction of apoptosis specifically in activated CD8+ T cells. Additionally, we report that the galectin-2-binding protein CD29 is up-regulated on the surface of activated CD8+ T cells compared with naive CD8+ T cells or CD4+ T cells, suggesting that increased galectin-2/CD29 signaling might be responsible for the proapoptotic effects of galectin-2 on activated CD8+ T cells. Taken together, these data indicate that galectin-2 may represent a novel therapeutic alternative for the treatment of CD8-mediated inflammatory disorders such as contact allergy.

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Section: Discussionmentioning

confidence: 99%

Galectin-2 Suppresses Contact Allergy by Inducing Apoptosis in Activated CD8+ T Cells

Loser

Sturm

Voskort³

et al. 2009

The Journal of Immunology

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“…One possibility, currently under investigation, is that GAL3 may interact with the RNA-binding proteins heterogeneous nuclear ribonucleoproteins to control PTEN RNA turnover. It has been previously reported that GAL3 binds directly to hnRnpA1 (54) and heterogeneous nuclear ribonucleoprotein C1/C2 (55) and that heterogeneous nuclear ribonucleoproteins form a multiprotein complex that regulates c-fos RNA degradation (56) and inhibit the mRNA editing action of Apobec (57). Binding of P-GAL3 to PTEN may also potentially alter the spatial structure of PTEN affecting its degradation.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylated Galectin-3 Mediates Tumor Necrosis Factor-related Apoptosis-inducing Ligand Signaling by Regulating Phosphatase and Tensin Homologue Deleted on Chromosome 10 in Human Breast Carcinoma Cells

Mazurek

Sun

Liu

et al. 2007

Journal of Biological Chemistry

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Galectin-3 (GAL3), a ␤-galactoside-binding lectin, confers chemoresistance to a wide variety of cancer cell types. It may exhibit anti-or pro-apoptotic activity depending on the nature of the stimulus. We report here that introducing phosphorylated galectin-3 (P-GAL3) into GAL3-null, tumor necrosis factorrelated apoptosis-inducing ligand (TRAIL)-resistant human breast carcinoma cells promotes TRAIL-induced apoptotic cell death by stimulating the phosphorylation/inactivation of the pro-apoptotic molecule Bad resulting in the inhibition of mitochondrial depolarization and the release of cytochrome c. Exposure of the transfectant cells to TRAIL leads to the recruitment of the initiator capase-8 followed by activation of the effector caspase-9, independent of cytochrome c, and subsequently the processing of the executioner caspase-3. P-GAL3 and phosphatase and tensin homologue deleted on chromosome 10 (PTEN) were coordinately expressed, with concomitant dephosphorylation of Akt in TRAIL-sensitive cells. In contrast, overexpression of phospho-mutant GAL3 (incapable of phosphorylation) failed to elicit similar responses. Depletion of PTEN using small interference RNAs reinstated Akt phosphorylation and conferred TRAIL resistance. In addition phosphatidylinositol 3-kinase inhibitors rendered the phospho-mutant GAL3-resistant cells sensitive to TRAIL. These findings suggest a pivotal role for P-GAL3 in promoting TRAIL sensitivity through activation of a nonclassic apoptotic pathway and identify P-GAL3 as a novel regulator of PTEN.

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“…Two remarkable Gal-1 intracellular functions discovered so far are the membrane anchorage of the oncogene H-Ras [20] and the interaction with spliceosomes via Gemin4 [21]. Neither of these functions requires sugar binding activity of Gal-1 [22,23].…”

Section: Introductionmentioning

confidence: 99%

Novel role for galectin-1 in T-cells under physiological and pathological conditions

Deák¹,

Hornung²,

Novák³

et al. 2015

Immunobiology

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Secreted, extracellular galectin-1 (exGal-1) but not intracellular Gal-1 (inGal-1) has been described as a strong immunosuppressive protein due to its major activity of inducing apoptosis of activated T-cells. It has previously been reported that T-cells express Gal-1 upon activation, however its participation in T-cell functions has remained largely elusive. To determine function of Gal-1 expressed by activated Tcells we have carried out a series of experiments. We have shown that Gal-1, expressed in Gal-1-transgenic Jurkat cells or in activated T-cells, remained intracellularly indicating that Gal-1-induced T-cell death was not a result of an autocrine effect of the de novo expressed Gal-1. Rather, a particular consequence of the inGal-1 expression was that T-cells became more sensitive to exGal-1 added either as a soluble protein or bound to the surface of a Gal-1-secreting effector cell. This was also verified when the susceptibility of activated T-cells from wild type or Gal-1 knockout mice to Gal-1-induced apoptosis were compared. Murine T-cells expressing Gal-1 were more sensitive to the cytotoxicity of the exGal-1 than their Gal-1 knockout counterparts. We also conducted a study with activated T-cells from patients with systemic lupus erythematosus (SLE), a disease in which dysregulated T-cell apoptosis has been well described. SLE T-cells expressed lower amounts of Gal-1 than healthy T-cells and were less sensitive to exGal-1. These results suggested a novel role of inGal-1 in T-cells as a regulator of T-cell response to exGal-1, and its likely contribution to the mechanism in T-cell apoptosis deficiency in lupus.

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Immunoprecipitation of spliceosomal RNAs by antisera to galectin-1 and galectin-3

Cited by 42 publications

References 22 publications

Galectin-2 Suppresses Contact Allergy by Inducing Apoptosis in Activated CD8+ T Cells

Galectin-2 Suppresses Contact Allergy by Inducing Apoptosis in Activated CD8+ T Cells

Phosphorylated Galectin-3 Mediates Tumor Necrosis Factor-related Apoptosis-inducing Ligand Signaling by Regulating Phosphatase and Tensin Homologue Deleted on Chromosome 10 in Human Breast Carcinoma Cells

Novel role for galectin-1 in T-cells under physiological and pathological conditions

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