Human Lectins, Their Carbohydrate Affinities and Where to Find Them

Raposo, Cláudia D.; Canelas, André B.; Barros, M. Teresa

doi:10.3390/biom11020188

Cited by 37 publications

(36 citation statements)

References 160 publications

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“…On the other hand, basophils also express galectins which are a family of animal lectins that bind β-galactoside containing sugars with high specificity. As many as 12 galectins have been found in humans ( 24 ). They are present as cytoplasmic or secreted forms.…”

Section: Discussionmentioning

confidence: 99%

An Evaluation of the Mechanisms of Galacto-Oligosaccharide (GOS)-Induced IgE Cross-Linking on Basophils in GOS Allergy

et al. 2022

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The prebiotics, galacto-oligosaccharides (GOS), are small carbohydrate molecules with 1–7 galactose units linked to glucose and have been shown to trigger IgE-mediated anaphylaxis in some cases following ingestion. It is still an unresolved question of how GOS cross-links IgE on basophils. In this study, we examined whether human galectins, a class of lectins that bind specifically to β-galactoside carbohydrates, are involved in GOS-induced basophil activation. Basophil activation test to GOS and control allergen, Blomia tropicalis (Blo t) extract were performed in the presence or absence of four sugar-based galectin inhibitors (lactose, thiodigalactoside [TDG], TD139, and GB1107) and one peptide-based inhibitor, G3-C12. Results showed that TD139, GB1107, and G3-C12 did not display a specific inhibitory effect on GOS-induced basophil activation as compared to control allergen. An inhibitory effect of lactose and TDG on GOS-induced basophil activation was observed and varied between subjects with up to 100% inhibition at low doses of GOS. The results of competitive ELISA suggest that the inhibitory effects of high dose lactose and TDG on the basophil activation is likely due to the cross-reactivity of GOS-specific IgE to lactose and TDG. Basophil activation is performed using purified basophils suggested that cell surface receptors on other blood cells were not required to induce basophil activation. In conclusion, our results suggest that GOS, a low molecular weight sugar, is able to cross-link IgE independently.

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Section: Discussionmentioning

confidence: 99%

An Evaluation of the Mechanisms of Galacto-Oligosaccharide (GOS)-Induced IgE Cross-Linking on Basophils in GOS Allergy

et al. 2022

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“…Human lectins are classified by considering their subcellular location and their structures. Lectins can be incorporate in the cellular membrane or have a soluble form and based on their form they can be divided into groups as C-type lectins, I-type lectins (including Siglecs), S-type lectins (also known as galectins), P-type lectins (known as Selectins) and pentraxins [ 104 ]. In tumor, they have been proposed to decipher the tumor glycocode that modulate immune tolerance/suppression [ 103 ].…”

Section: Glycan-lectin Interactions and Immunosuppressive Network In Gbmentioning

confidence: 99%

“…Siglecs function as immunomodulatory receptors that mainly mediate immunosuppressive responses through the phosphorylation of the immunoreceptor tyrosine-based inhibition motif (ITIM) depending on the cell which they are expressed by and on the ligand they interact with. All Siglecs are expressed on immune cells, except for the myelin-associated glycoprotein (MAG) [ 104 ]. Siglec1 and 12 expression is restricted on macrophages, CD22 on B lymphocytes, Siglec16 on MG while other Siglecs, such as CD33 and Siglec7, can be found on several immune cell subsets [ 121 , 122 , 123 , 124 ].…”

Section: Glycan-lectin Interactions and Immunosuppressive Network In Gbmentioning

confidence: 99%

Glycan-Lectin Interactions as Novel Immunosuppression Drivers in Glioblastoma

Pace

Scirocchi

Napoletano

et al. 2022

IJMS

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Despite diagnostic and therapeutic improvements, glioblastoma (GB) remains one of the most threatening brain tumor in adults, underlining the urgent need of new therapeutic targets. Lectins are glycan-binding proteins that regulate several biological processes through the recognition of specific sugar motifs. Lectins and their ligands are found on immune cells, endothelial cells and, also, tumor cells, pointing out a strong correlation among immunity, tumor microenvironment and vascularization. In GB, altered glycans and lectins contribute to tumor progression and immune evasion, shaping the tumor-immune landscape promoting immunosuppressive cell subsets, such as myeloid-derived suppressor cells (MDSCs) and M2-macrophages, and affecting immunoeffector populations, such as CD8+ T cells and dendritic cells (DCs). Here, we discuss the latest knowledge on the immune cells, immune related lectin receptors (C-type lectins, Siglecs, galectins) and changes in glycosylation that are involved in immunosuppressive mechanisms in GB, highlighting their interest as possible novel therapeutical targets.

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“…Galectins (formerly known as S-type lectins) are a family of lectin proteins which share a domain with high-affinity binding for β-galactoside sugars. Galectins are divided into three subfamilies based on their structures: prototypical, chimeric, and tandem-repeat [ 33 ]. Among other functions, galectins are players in the innate immune system, triggering immune responses as well as resolving inflammation [ 34 ].…”

Section: Introductionmentioning

confidence: 99%

KIT Mutations Correlate with Higher Galectin Levels and Brain Metastasis in Breast and Non-Small Cell Lung Cancer

Funkhouser

Strigenz

Blair

et al. 2022

Cancers

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To investigate a potential role for galectins as biomarkers that enable diagnosis or prognostication of breast or non-small cell lung cancer, the serum levels of galectins -1, -3, -7, -8, and -9 of cancer patients determined by ELISA assays were compared to the mutation status of 50 known cancer-critical genes, which were determined using multiplex PCR in tumors of the same patients. Mutations in the KIT proto-oncogene, which codes for the c-Kit protein, a receptor tyrosine kinase, correlated with higher levels of galectins -1, -3, -8, and -9 in breast cancer patients and galectin-1 in non-small cell lung cancer patients. Mutations in the KIT gene were more likely found in brain metastases from both of these primary cancers. The most common KIT mutation in our panel was p.M541L, a missense mutation in the transmembrane domain of the c-Kit protein. These results demonstrate an association between KIT oncogenic signaling and elevated serum galectins in patients with metastatic disease. Changes in protein trafficking and the glycocalyx composition of cancer cells may explain the observed alterations in galectin expression. This study can be useful for the targeted selection of receptor tyrosine kinase and galectin inhibitor anti-cancer treatments.

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Human Lectins, Their Carbohydrate Affinities and Where to Find Them

Cited by 37 publications

References 160 publications

An Evaluation of the Mechanisms of Galacto-Oligosaccharide (GOS)-Induced IgE Cross-Linking on Basophils in GOS Allergy

An Evaluation of the Mechanisms of Galacto-Oligosaccharide (GOS)-Induced IgE Cross-Linking on Basophils in GOS Allergy

Glycan-Lectin Interactions as Novel Immunosuppression Drivers in Glioblastoma

KIT Mutations Correlate with Higher Galectin Levels and Brain Metastasis in Breast and Non-Small Cell Lung Cancer

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