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Results for “Galectin 1”

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At least 19 recordsLinked to original sources

PubMed2006

Interaction of human neutrophils with endothelial cells regulates the expression of endogenous proteins annexin 1, galectin-1 and galectin-3.

Annexin 1 (ANXA1), galectin-1 (Gal-1) and galectin-3 (Gal-3) proteins have been identified as important mediators that promote or inhibit leukocyte migration. The expression of these proteins was studied in human neutrophils and endothelial cells (ECs) during a transmigration process induced by IL-8. Upon neutrophil adhesion to EC, a significant increase in the cleaved ANXA1 (LCS3, raised against all ANXA1 isoforms) expression was detected in the plasma membrane of adhered neutrophils and ECs compared to intact ANXA1 isoform (LCPS1, against N-terminus of protein). Adherent neutrophils had elevated Gal-3 levels in the nucleus and cytoplasm, and ECs in their plasma membranes. In contrast, a decrease in the total amounts of Gal-1 was detected in migrated compared to non-migrated neutrophils. Therefore, ANXA1 and Gal-3 changed in their content and localization when neutrophils adhere to endothelia, suggesting a process of sensitive-balance between two endogenous anti- and pro-inflammatory mediators.

Annexin A1↗

PubMed1997

Differential expression of galectin 3 and galectin 1 in colorectal cancer progression.

BACKGROUND & AIMS: Galectins are beta-galactoside-binding proteins possibly involved in tumor progression. The aim of this study was to determine the pattern of galectin 3 and galectin 1 expression and involvement in colorectal cancer progression. METHODS: Galectin 3 expression was examined immunohistochemically in 39 samples of normal mucosae, 25 adenomas, 87 carcinomas, and 39 lymph node metastases. Galectin 1 was analyzed in 25 samples of mucosae, 15 adenomas, 25 carcinomas, and 11 metastases. Western blot analysis was also performed. RESULTS: All normal mucosae showed strong nuclear galectin 3 expression, which was down-regulated in the neoplastic progression, because only 60% of adenomas, 48% of carcinomas, and 44% of metastases were strongly positive (P < 0.0001). Cytoplasmic expression was down-regulated in adenomas (16%) but increased again in carcinomas (64%) (P < 0.0001). Galectin 1 expression was mainly detected in stromal cells and correlated with tumor progression from normal mucosae to adenomas and carcinomas (P < 0.0001). CONCLUSIONS: Galectin 3 expression is down-regulated in the initial stages of neoplastic progression, whereas a dissociated cytoplasmic expression increases in later phases of tumor progression. Galectin 1 in colorectal mucosa is predominantly a stromal product whose overexpression is associated with the neoplastic progression of colorectal cancer.

Adenoma↗

PubMed1998

Binding of synthetic sulfated ligands by human splenic galectin 1, a beta-galactoside-binding lectin.

The carbohydrate-binding site of galectin 1, a vertebrate beta-galactoside-binding lectin, has a pronounced specificity for the betaGal(1-->3)- and betaGal(1-->4)GlcNAc sequences. The binding inhibition study reported herein was carried out to determine whether sulfation of saccharides would influence their binding by galectin 1. The presence of 6'-OSO3- on LacNAc greatly reduces the inhibitory potency relative to LacNAc. 3'-OSO3-LacNAc, 3'-OSO3-Galbeta(1-->3)GlcNAc(beta)1-OBzl and 3-OSO3-Galbeta1-OMe are more potent inhibitors than the non-sulfated parent compounds. Surprisingly, 2'-OSO3-LacNAc showed over 40 fold less inhibitory potency relative to LacNAc. Ovarian carcinoma A121 cells were shown to synthesize sulfated macromolecules that bind to galectin 1. Modulation in vivo of saccharide sulfation may lead to modulation of galectin 1 interaction with glycoconjugates; hence, sulfation could play a role in modulating lectin functions.

Asialoglycoproteins↗

PubMed2003

Modulation of O-glycans and N-glycans on murine CD8 T cells fails to alter annexin V ligand induction by galectin 1.

Thymic negative selection and contraction of responding T cell oligoclones after infection represent important cell ablation processes required for maintaining T cell homeostasis. It has been proposed that galectin 1 contributes to these processes through interaction with lactosyl sequences principally on cell surface glycoproteins bearing core 2 (C2GnT1)-branched O-glycans. According to this model, specific T cell surface proteins cross-linked by galectin 1 induce signaling, ligand redistribution, and apoptosis in both immature thymocytes and activated T cells. The influence of lactosyl residues contained in branched O-glycans or complex N-glycans on galectin 1 binding and induction of annexin V ligand in murine CD8 T cells was assessed. Neither galectin binding nor galectin-induced expression of annexin V ligand was perturbed under conditions in which: 1) C2GnT1 activity was differentially induced by CD8 T cell activation/culture with IL-2 vs IL-4; 2) activated CD8(+) T cells lacked C2GnT1 expression; or 3) complex N-glycan formation was blocked by swainsonine. The maintenance of galectin 1 binding and induced annexin V expression under conditions that alter lactosamine abundance on O- or complex N-glycans suggest that galectin 1-mediated apoptosis is neither a simple function of fluctuating C2GnT1 activity nor a general C2GnT1-dependent mechanism underlying contraction of CD8 T cells subsequent to activation.

Amino Sugars↗

PubMed1997

Anti-galectin-1 autoantibodies in serum of patients with neurological diseases.

The presence of autoantibodies to human brain galectin-1 was investigated in serum from patients with multiple sclerosis, patients with or without evidence of other neurological disorders, and healthy controls, using an ELISA on purified brain galectin-1. Levels of autoantibodies to galectin-1 were significantly higher in patients than in healthy controls. Comparison of levels of anti-galectin-1 and anti-idiotypic antibodies mimicking human brain galectin-1 (L-IgG) showed that the highest levels of autoantibodies were present in patients with low levels of L-IgG. This finding can be explained by hypothesizing that the concentration of autoantibodies to galectin-1 is possibly associated with impairment of the regulation of the immune system.

Adult↗

PubMedDate not supplied

Galectin 1 modulates attachment, spreading and migration of cultured vascular smooth muscle cells via interactions with cellular receptors and components of extracellular matrix.

Galectin 1 (Gal-1), a lactose-binding lectin, is a component of vascular extracellular matrix and secreted by human vascular smooth muscle cells (SMCs). The purpose of this study was to investigate a possible role of Gal-1 in controlling adhesion and migration of cultured human vascular SMCs. Gal-1 co-localised with laminin and cellular fibronectin in extracellular matrix (ECM) secreted by cultured human vascular SMCs. Recombinant glutathione S-transferase (GST)-Gal-1 fusion protein bound to laminin and cellular fibronectin in ELISA. GST-Gal-1 inhibited SMC attachment to laminin via interactions with both SMCs and laminin. GST-Gal-1 inhibited SMC spreading on plastic or on laminin, but not on cellular fibronectin. GST-Gal-1 modulated SMC migration on laminin and inhibited migration on cellular fibronectin. GST-Gal-1 bound to several 35S-labelled proteins in SMC extracts including laminin and alpha1beta1 integrin, identified by depletion of SMC protein extracts with respective antibodies. We conclude that Gal-1 is able to modulate SMC attachment, spreading and migration via interactions with ECM proteins and alpha1beta1 integrin.

Adjuvants, Immunologic↗

PubMed2000

Galectin 1 is involved in vascular smooth muscle cell proliferation.

OBJECTIVE: Smooth muscle cell (SMC) migration and proliferation are the key steps in the development of atherosclerosis and restenosis. Matricellular proteins have been implicated in cell adhesion, migration and proliferation. Here we investigated the role of the matricellular protein galectin-1 (Gal-1), a beta-galactoside-binding lectin, in SMC proliferation in atheroma and DNA synthesis in cell culture. METHODS: Protein expression was visualised by tissue section immunostaining. RNA expression was analysed using Northern blot analysis. DNA synthesis of human vascular SMCs was determined by 3H-thymidine incorporation. Recombinant glutathione S-transferase-galectin-1 fusion protein (Gal FP) binding to extracellular matrix (ECM) proteins was measured by ELISA. Gal-1 binding to cells and ECM was estimated using 125I-labelled Gal FP. RESULTS: Prominent Gal-1 staining coincided with SMC proliferation in human coronary endarterectomy samples in organoid culture. In cell culture, Gal-1 mRNA was upregulated in growing SMCs. Gal FP increased serum-induced DNA synthesis of human SMCs on plastic or endogenous ECM, but not of a rat PAC1 SM cell line. Also, Gal FP slightly increased SMC adhesion to ECM. SMCs exhibited a complex pattern of receptor-ligand interactions with Gal FP. The Gal-1 binding to SMCs was much stronger than to ECM, produced by these SMCs. We identified new ECM proteins: thrombospondin, vitronectin and osteopontin, which bound to Gal FP in a dose- and beta-galactoside-dependent manner in ELISA. CONCLUSIONS: Gal-1 binding to SMCs was stronger than to ECM, although ECM of atherosclerotic blood vessels contained additional ECM proteins which bound to Gal-1. Gal-1 was upregulated during SMC growth and Gal FP enhanced serum-induced DNA synthesis in SMCs. Overall, Gal-1 upregulation is likely to provide a reinforcement of serum-induced events during vascular injury.

Arteriosclerosis↗

PubMed2004

The effect of galectin 1 on 3T3 cell proliferation on chitosan membranes.

Galectin-1 (GAL1), a beta-galactoside-binding protein, functions in cell adhesion, development, and growth regulation. A number of studies suggest that GAL1 play an important role in enhancing cell adhesion to extracellular matrix and inducing cell proliferation. Chitosan is a derivative of chitin extracted from lobsters, crabs and shrimps' exoskeletons. In clinical medicine, chitosan membrane had been used as a semi-permeable biological dressing. Although chitosan membranes show no cytotoxicity, some cell types (e.g. 3T3 cells) fail to attach and proliferate on their surface. In these studies, we show that over-expression of GAL1 does not enhance 3T3 cell proliferation on chitosan membranes. However, coating the chitosan membrane with recombinant GAL1 proteins significantly expedites 3T3 cells proliferation. The enhanced cell growth was inhibited by thiodigalactoside (TDG, a potent inhibitor of beta-galactoside binding) and GAL1 monoclonal antibodies, suggesting GAL1's specific effect on the proliferation of 3T3 cells upon chitosan membranes. Moreover, immunoblotting detected a markedly suppressed tyrosine phosphorylation in several proteins on 3T3 cell growths upon GAL1-coated chitosan membrane. Pretreating the cells with sodium fluoride (NaF, a phosphatase inhibitor) inhibits the attachment and proliferation of 3T3 cells. These findings support a proposed role for altered levels of protein phosphorylation in GAL1-mediated cell attachment and proliferation on chitosan membranes.

3T3 Cells↗

PubMed2000

Analysis of galectin 1-mediated cell signaling by combined precipitation and electrophoresis techniques.

Galectin-1 (GAL1) is a beta-galactoside-binding protein that has been implicated in the regulation of viability of lymphoid cells. However, the signaling pathway governed by the binding of GAL1 to the cell membrane is not understood yet. As a first step toward the elucidation of GAL1-initiated signaling events, electrophoresis techniques such as sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and two-dimensional electrophoresis (2-DE) were used together with precipitation techniques. This allowed us to identify the membrane receptor of GAL1, and to characterize the signal resulting from the binding of GAL1 to this receptor. Our results demonstrate that the tyrosine phosphatase CD45 is the receptor for GAL1, and that the src-type tyrosine kinase Lyn is a target for the effects of GAL1/CD45 interactions in B-cells. Furthermore, these results show the usefulness of combined precipitation and electrophoresis techniques to analyze phosphotyrosine-dependent mechanisms during the study of cell functions.

Blotting, Western↗

PubMed2003

Galectin 1 inhibits incorporation of vitronectin and chondroitin sulfate B into the extracellular matrix of human vascular smooth muscle cells.

Galectin-1, a beta-galactoside-binding dimeric lectin, interacts with the extracellular matrix (ECM) of smooth muscle cells (SMCs) and with particular ECM proteins. Enrichment of the ECM with galectin-1 affects adhesion and proliferation of cultured SMCs. Here we investigated whether galectin-1 (1) interacts with glycosaminoglycan (GAG) chains, (2) cross-links between ligands and facilitates the incorporation of GAGs, vitronectin and plasma fibronectin in the ECM of vascular SMCs. A recombinant galectin-1 fusion protein GalH, used in this study, formed dimers and interacted with ECM proteins. GAG chains inhibited these interactions. Among the studied GAG chains, only chondroitin sulfate B interacted with GalH in beta-galactoside-dependent manner. GalH did not bridge between ECM proteins on solid phase and [125I]-labelled ECM proteins or GAGs in solution. The ECM incorporated less vitronectin in the presence of soluble GalH. GalH-enriched ECM incorporated less vitronectin and chondroitin sulfate B. The ECM partially depleted of endogenous galectins incorporated more chondroitin sulfate B compared to untreated ECM. These results suggest that galectin-1 is likely to be involved in the ECM assembly affecting incorporation of some ECM components important for SMC behaviour.

Cells, Cultured↗

PubMed2006

Circulating anti-galectin-1 antibodies are associated with the severity of ocular disease in autoimmune and infectious uveitis.

PURPOSE: Galectin (Gal)-1, an endogenous lectin found at sites of immune privilege, plays a critical role in the regulation of the immune response. Therapeutic administration of Gal-1 or its genetic delivery suppresses chronic inflammation in experimental models of autoimmunity. The purpose of this work was to investigate the occurrence of circulating anti-Gal-1 antibodies in patients with autoimmune and infectious uveitis as potential determinant factors of disease progression. METHODS: IgG, IgE, and IgA anti-Gal-1 antibodies were assessed by ELISA and Western blot in sera from patients with autoimmune (n = 47) and infectious (n = 15) uveitis compared with healthy control subjects (n = 30). The frequency of anti-Gal-1 antibodies was examined in patients experiencing poor clinical outcome (n = 21) or good evolution (n = 9). Anti-Gal-1 antibodies were eluted by incubating patient sera with nitrocellulose filters adsorbed with rGal-1. The ability of these antibodies to recognize retinal tissue was assessed by ELISA, Western blot, and immunohistochemistry. RESULTS: IgE, IgG, and IgA anti-Gal-1 antibodies were increased in sera from patients with autoimmune uveitis (P < 0.001 vs. controls) and toxoplasmic retinochoroiditis (P < 0.001). The level of anti-Gal-1 IgE and IgG antibodies was associated with progressive disease and poor outcome in autoimmune and infectious uveitis. Furthermore, these antibodies strongly immunoreacted with retinal lysates and recognized retinal structures mainly photoreceptors in retinal sections. CONCLUSIONS: Anti-retinal Gal-1 antibodies are present in sera from patients with uveitis and can be associated with the progression of ocular disease, suggesting their potential use in follow-up observations of these patients.

Adolescent↗

PubMed2001

Anti-galectin-1 autoantibodies in human Trypanosoma cruzi infection: differential expression of this beta-galactoside-binding protein in cardiac Chagas' disease.

The pathogenesis of Chagas' disease has been subject of active research and still remains to be ascertained. Galectin-1 (Gal-1), a member of a conserved family of animal beta-galactoside-binding proteins, localized in human heart tissue, has been suggested to play key roles in immunological and inflammatory processes. In the present study we demonstrated the occurrence of anti-Gal-1 autoAb in sera from patients in the acute and chronic stages of Chagas' disease (ACD and CCD) by means of ELISA and Western blot analysis. We found a marked increase in the level and frequency of Ig E anti-Gal-1 antibodies in sera from patients with ACD, but a low frequency of Ig M anti-Gal-1 immunoreactivity. Moreover, Ig G immunoreactivity to this beta-galactoside-binding protein was found to be correlated with the severity of cardiac damage in CCD, but was absent in nonrelated cardiomyopathies. We could not detect immunoreactivity with Trypanosoma cruzi antigens using a polyclonal antibody raised to human Gal-1 and no hemagglutinating activity could be specifically eluted from a lactosyl-agarose matrix from parasite lysates. Moreover, despite sequence homology between Gal-1 and shed acute phase antigen (SAPA) of T. cruzi, anti-Gal-1 antibodies eluted from human sera failed to cross-react with SAPA. In an attempt to explore whether Gal-1 immunoreactivity was originated from endogenous human Gal-1, we finally investigated its expression levels in cardiac tissue (the main target of Chagas' disease). This protein was found to be markedly upregulated in cardiac tissue from patients with severe CCD, compared to cardiac tissue from normal individuals.

Acute Disease↗

PubMed1998

Embryonic implantation in galectin 1/galectin 3 double mutant mice.

Galectin 1 and galectin 3 are first expressed in the trophectoderm cells of the implanting embryo and have been implicated in the process of implantation. However, we had previously shown that the lack of galectin 1 in galectin 1 null mutant mice is compatible with implantation. In this study, we describe the generation of galectin 3 null mutant mice and show that they are viable and have no overt abnormalities. The importance of galectin 1 and galectin 3 in implantation was assessed by obtaining double mutant mice [gal1 -/-; gal3 -/-]. We find that implantation can still occur in the absence of both galectin 1 and galectin 3. However, we show that galectin 5, a third member of this gene family, is also present in the blastocyst at the time of implantation.

Animals↗

PubMedDate not supplied

Changes in the distribution pattern of galectin-1 and galectin-3 in human placenta correlates with the differentiation pathways of trophoblasts.

Human placentation is a complex biological phenomenon that results from precisely regulated interactions between cells and the extracellular matrix. Galectin- 1 and galectin-3 belong to a newly defined family of galactose-binding lectins that can bind several glycoconjugates such as the basement membrane glycoprotein laminin, and are involved in many biological events including cell adhesion. In this study, the expression of these two galectins in first and third trimester normal human placenta was examined using single and double immunohistochemical staining and specific antibodies for galectins and cytokeratins. Galectin-3 was detected in all trophoblastic lineages including villous cytotrophoblasts and extravillous trophoblasts (trophoblastic cell columns, infiltrating trophoblasts, endovascular trophoblasts and placental bed giant cells). On the contrary, galectin-1 distribution was restricted to endometrium. A reduction of galectin-3 expression was observed from the villous trophoblasts to the trophoblastic cell columns. This pattern correlated with the switch from a proliferative to a migratory phenotype. Galectin-1 and galectin-3 were both detected in maternal decidual cells. Our data demonstrate a specific pattern of galectin-1 and galectin-3 expression in trophoblastic tissue, and suggest these lectins could contribute to cell-cell and cell matrix interactions of trophoblast during placentation.

Antigens, Differentiation↗

PubMed1998

Complement receptor 3 of macrophages is associated with galectin-1-like protein.

We have previously identified a 16-kDa protein with a pI of 5.1 (P16/5.1) that is associated with macrophage CR3. Microsequencing of P16/5.1 indicated exclusive homology to the beta-galactoside-binding lectin, galectin-1. Abs specific to a galectin-1 unique peptide reacted with P16/5.1. The association of P16/5.1 with CR3 was specifically inhibited by lactose, which binds with high affinity to galectin-1. These data together with similarities in molecular mass and pI suggest that P16/5.1 is galectin-1. Two-color immunofluorescence staining revealed the expression of galectin-1 on the macrophage surface and its colocalization with CR3. However, a surplus of CR3 was free of galectin-1, and some galectin-1 molecules were associated with cell surface receptors other than CR3. Based on these results we propose two models depicting the functional significance of CR3-galectin-1 association: 1) homodimeric galectin-1 possessing a divalent sugar binding site may act as an extracellular adapter molecule that cross-links CR3 with other receptors; and 2) association of galectin-1 with beta-galactosides on the extracellular domain of CR3 may modify the binding affinity of the receptor to its ligand. These possibilities are not mutually exclusive and can clarify the mode by which CR3 transmits signals in macrophages.

Animals↗

PubMed1996

Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor (TGF) activity: the relationship between intramolecular disulfide bridges and TGF activity.

Previously we demonstrated that overexpression of a beta-galactoside binding protein, galectin-1, caused the transformation of BALB3T3 fibroblast cells [Yamaoka, K., Ohno, S., Kawasaki, H., and Suzuki, K. (1991) Biochem. Biophys. Res. Commun. 179, 272-279]. We have now studied the structure-function relationship between the sugar-binding activity and the mitogenic activity of galectin-1 purified from an avian sarcoma virus-transformed rat NRK cell line, 77N1. The purified galectin-1 (t-galectin-1) had potent mitogenic activity in BALB3T3 cells, but no sugar-binding activity. Treatment of t-galectin-1 with 2-mercaptoethanol decreased its mitogenic activity, but resulted in the appearance of a sugar binding activity. Chemical modification of sulfhydryl groups in purified t-galectin-1 with [14C]-iodoacetamide suggested the presence of intramolecular disulfide bonds. MALDI-TOF mass spectrometric analysis of the native and reduced forms of the tryptic peptides from t-galectin-1 showed that t-galectin-1 has two intramolecular disulfide bonds (Cys2-Cys16 and Cys42-Cys60). These studies suggest that these intramolecular disulfide bonds of t-galectin-1 are essential for its mitogenic activity and that the different activities may be regulated by structural changes caused by intramolecular disulfide bond-breakage.

Amino Acid Sequence↗

PubMed2001

Isolation and characterization of galectins in the mammalian retina.

PURPOSE: Previous studies have suggested that galectins may be involved in retinal adhesion and photoreceptor cell survival. To elucidate the underlying mechanisms, the authors isolated retinal galectins, determined their types and distributions, and investigated the validity of the hypothesis, using rat models. METHODS: An antibody was prepared against a bovine retinal lectin that was isolated by use of a lactose-agarose column. cDNA of the lectin was isolated by screening of a bovine retinal cDNA library, using the antibody, and then was sequenced. The cDNAs of rat retinal galectins were also isolated by means of polymerase chain reaction and used to produce an antibody against recombinant galectin-3. Using the described antibodies, the authors examined the distributions of galectins in bovine and rat retinas, morphologic changes of rat retinas induced by the antibodies, and distributional changes of galectins in constant-light-exposed rat retinas. RESULTS: The cDNAs of bovine galectin-1, rat galectin-1, and rat galectin-3 were isolated. Galectin-1 was found in various regions, including the retinal pigment epithelium, outer limiting membrane, and outer plexiform layer in bovine and rat retinas. Galectin-3 was increasingly detected in the cytoplasm of Müller cells after constant light exposure after an increase in its transcript. Retinal detachment and vacuolation of the outer plexiform layer were induced in rat eyes by intravitreous injection of the anti-galectin-1 antibody. CONCLUSIONS: Galectin-1 may be involved in adhesion of the photoreceptor and outer plexiform layers by interacting with glycoconjugates with beta-galactoside residues in the interphotoreceptor matrix and synaptic cleft matrix. Galectin-3 may increase in Müller cells of a degenerative rat retina, probably through endogenous anti-apoptosis.

Animals↗

PubMed2003

Galectin 3 and its binding protein in rheumatoid arthritis.

OBJECTIVE: To characterize the expression pattern and role of galectin 3 and galectin 3 binding protein (G3BP) in rheumatoid arthritis (RA), in comparison with galectin 1, and to explore whether soluble galectin 3 and G3BP, investigated in serum, synovial fluid, or cell culture supernatant, are associated with disease. METHODS: Synovial tissues from patients with RA or osteoarthritis (OA), as well as from healthy controls, were analyzed for galectins 1 and 3 and G3BP by in situ hybridization and immunohistochemistry. Levels of galectin 3 and G3BP in serum and synovial fluid from patients with RA and OA and controls, as well as in cell culture supernatants, were determined by enzyme-linked immunosorbent assay (ELISA). In vitro, the intracellular expression of galectin 3 in RA and OA synovial fibroblasts after modulation with tumor necrosis factor alpha (TNFalpha), interleukin-1beta (IL-1beta), and anti-CD40 monoclonal antibodies was measured by flow cytometry. RESULTS: In RA, galectin 3 messenger RNA and protein stained throughout the synovial membrane, whereas G3BP was particularly expressed at sites of bone destruction. In contrast, the expression of galectin 1 was not uniform in different RA specimens, and was never found at sites of invasion. In OA and normal synovial tissues, only a small number of cells were positive for galectins and/or G3BP. Galectin 3 was elevated in RA sera and synovial fluids, whereas G3BP was increased in RA synovial fluids only. In RA, serum galectin 3 correlated with C-reactive protein levels, whereas G3BP was associated with joint destruction and/or synovial cell activation as measured by the levels of cartilage oligomeric matrix protein. In vitro, RA synovial fibroblasts showed an increased release of galectin 3 into culture medium, as measured by ELISA, but decreased secretion of G3BP. In RA synovial fibroblasts with low basal expression of galectin 3, TNFalpha increased its intracellular level in a dose-dependent manner. In contrast, IL-1beta or anti-CD40 monoclonal antibodies showed no effect. CONCLUSION: Our data indicate that galectin 3 and G3BP are not only involved in inflammation, but also contribute to the activation of synovial fibroblasts. The intracellular accumulation of galectin 3 can be enhanced by TNFalpha. Thus, galectin 3 and G3BP represent novel markers of disease activity in RA.

Arthritis, Rheumatoid↗