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Identification of Galectin-9 binding partners in dendritic cells

ABSTRACT: Galectins are lectin-binding proteins expressed both at the plasma membrane and intracellularly. Our research focuses on identifyingthe role of these proteins (mostly galectin-9) on dendritic cell function. For this, we wanted to run an unbiased approach to identify the galectin-9 binding partners in primary dendritic cells.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Dendritic Cell

DISEASE(S): Disease Free

SUBMITTER: Cornelia Spruijt

LAB HEAD: Laia Querol Cano

PROVIDER: PXD039781 | Pride | 2023-10-13

REPOSITORIES: Pride

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Nutrient Responsive O-GlcNAcylation Dynamically Modulates Galectin 3 Secretion

Project description:Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and in fact, characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer. These changes in glycosylation have important functional roles and can drive disease progression. However, little is known about the molecular mechanisms underlying how these signals are integrated and transduced into biological effects. Galectins are proteins that bind glycans and are secreted by a poorly characterized non-classical secretory mechanism. Once outside the cell, galectins bind to terminal galactose residues of cell surface glycans and modulate numerous extracellular functions like clathrin independent endocytosis (CIE). Originating in the cytoplasm, galectins are predicted substrates for O-GlcNAc addition and removal; and, as we have shown, galectin 3 is a substrate for OGT. This study also shows that galectin 3 secretion is sensitive to changes in O-GlcNAc levels. We determined that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3. We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions and these changes were dependent on dynamic O-GlcNAcylation. Importantly, we showed that these O-GlcNAc driven alterations in galectin 3 secretion drove changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function of transducing nutrient sensing information coded in cell surface glycosylation into biological effects.

2022-04-01 | PXD028139 | Pride

Galectin-3 interacts with components of the nuclear ribonucleoprotein complex

Project description:The multifunctional -galactoside-binding protein galectin-3 is found in many distinct subcellular compartments including the cell nucleus. Expression and distribution of galectin-3 between the cell nucleus and the cytosol changes during cell differentiation and cancer development. Nuclear functions of galectin-3 and how they contribute to tumorigenesis are not understood. In order to identify nuclear galectin-3 interaction partners, we used affinity chromatography and co-immunoprecipitation. Spatial proximity in the nucleus was assessed by immunofluorescence and proximity ligation assay. We also investigated the function of galectin-3 on mRNA-export by fluorescence in situ hybridization and on mRNA-processing by RNA-sequencing.

2016-06-07 | E-MTAB-4783 | biostudies-arrayexpress

SILAC-based proteomic profiling of the human colon cancer cell line LS 180 in response to exogenous galectin-4

Project description:Galectins constitute a family of ß-galactoside binding proteins that translate sugar-encoded signals of cell surface glycoconjugates into biological effects. The expression pattern of different human galectins changes during tissue development and is altered at sites of inflammation and tumor. Galectins have been known to be involved in colorectal cancer development, progression and metastasis. Galectin-4 has already been reported to function as tumor suppressor in this type of malignancy. However, its detailed impact on the tumor phenotype is still unknown. Our previous work indicates that galectin-4 inhibits cell proliferation and induces morphological changes in analyzed human colon cancer cell lines, including LS 180.

2016-12-23 | PXD003489 | Pride

Galectin-8 induces functional disease markers in human osteoarthritis and cooperates with galectins-1 and -3.

Project description:The reading of glycan-encoded signals by tissue lectins is considered a major route of the flow of biological information in many (patho)physiological processes. The arising challenge for current research is to proceed from work on a distinct protein to family-wide testing of lectin function. Having previously identified homodimeric galectin-1 and chimera-type galectin-3 as molecular switches in osteoarthritis progression, we here provide proof-of-principle evidence for an intra-network cooperation of galectins with three types of modular architecture. We show that the presence of tandem-repeat-type galectin-8 significantly correlated with cartilage degeneration and that it is secreted by osteoarthritic chondrocytes. Glycan-inhibitable surface binding of galectin-8 to these cells increased gene transcription and the secretion of functional disease markers. The natural variant galectin-8 (F19Y) was less active than the prevalent form. Genome-wide array analysis revealed induction of a pro-degradative/inflammatory gene signature, largely under control of NF-κB signaling. This signature overlapped with respective gene-expression patterns elicited by galectins-1 and -3, but also presented supplementary features. Functional assays with mixtures of galectins that mimic the pathophysiological status unveiled cooperation between the three galectins. Our findings shape the novel concept to consider individual galectins as part of a so far not realized teamwork in osteoarthritis pathogenesis, with relevance beyond this disease.

2021-02-17 | GSE131822 | GEO

Expression data of primary osteoarthritic chondrocytes treated with Galectin-4

Project description:The severity of osteoarthritis is linked to elevated levels of galectins. Here, the aim of the study was to evaluate the role of Galectin-4 in osteoarthritic cartilage.

2022-02-23 | GSE183531 | GEO

Galectin-9 suppresses growth of hepatocellular carcinoma in vitro

Project description:Galectin-9 suppresses growth of Li-7 cells, a cell line of human hepatocellular carcinoma, in vitro study. Micro RNA expression of Li-7 cells, a cell line of hepatocellular carcinoma, with or without administration of galectin-9 were assessed in vitro.

2015-03-01 | E-GEOD-55665 | biostudies-arrayexpress

Galectin-9 suppresses growth of hepatocellular carcinoma in vivo

Project description:Galectin-9 suppresses growth of Li-7 cells, a cell line of human hepatocellular carcinoma, in xenograft model analysis. Micro RNA expression in xenografts of Li-7 cells, a cell line of hepatocellular carcinoma, with or without administration of galectin-9 were assessed.

2015-03-01 | E-GEOD-55666 | biostudies-arrayexpress

Gene expression change induced by TIM-3/galectin-9 interaction in primary AML

Project description:Analysis of gene expression change after galectin-9 stimulation in primary CD34+TIM-3+ AML cells Total RNA obtained from purified CD34+TIM-3+ primary AML cells with or without recombinant human galectin-9 stimulation (20hrs) was subjected to transcriptome analysis

2014-10-10 | E-GEOD-62223 | biostudies-arrayexpress

Quantitative proteomic analysis of apical interacting partners of canine galectin 8

Project description:Primary cilium is a specialized sensory organelle protruding from apical surface of most cells that transmits environmental information into cells. Its length is tightly controlled by various mechanisms such as the frequency or the cargo size of the intraflagellar transport trains which deliver the building materials essential for the growing cilia. We demonstrate that the sialoglycan interacting galectin 8 regulates the process of primary ciliogenesis, and as the epithelia become polarized, there are more galectin 8 being apically secreted. These extracellular galectin 8 molecules apparently bind to a lipid raft enriched domain at the base of the primary cilia, and binding of galectin 8 at this critical region triggers rapid growth of primary cilia by perturbing the barrier function of transition zone. To identify the ciliary molecule which mediates the cilia-lengthening effect of galectin 8, we approached by adopting sequential apical domain selective biotinylation, surface GST-galectin 8 fusion protein incubation, followed by two-step affinity purification scheme. We then processed these apical surface galectin 8-interacting candidates by mass spectrometry. We totally identified 254 reproducible candidates in two independent experiments. There were 96 and 117 plasma membrane candidates noted from the first and second experiments respectively. We focused on 66 candidates categorized as plasma membrane proteins (~25% of total candidates) which were repetitively identified in two separate experiments.

2023-11-25 | PXD038021 | Pride

Study of microRNA associated with galectin-9 and anti-tumor effect in cholangiocarcinoma

Project description:The miRNAs expression was markedly altered with the treatment of galectin-9 in vivo and various miRNAs induced by galectin-9 also may contribute to tumor growth of cholangiocarcinoma in vivo. Using a custom microarray platform, we analyzed the expression levels of 2019 human miRNA probes in the tumorous tissues in vivo that was treated with and without galectin-9.

2016-09-01 | E-GEOD-71684 | biostudies-arrayexpress

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