Human T Cell Activation Results in Extracellular Signal-regulated Kinase (ERK)-Calcineurin-dependent Exposure of Tn Antigen on the Cell Surface and Binding of the Macrophage Galactose-type Lectin (MGL)*

Vliet, Sandra J. van; Vuist, Ilona M.; Lenos, Kristiaan; Tefsen, Boris; Kalay, Hakan; García-Vallejo, Juan J.; Kooyk, Yvette van

doi:10.1074/jbc.m113.471045

Cited by 30 publications

(18 citation statements)

References 48 publications

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“…Comelli E.M. et al reported that the activation of murine T cells lead to a marked decrease of N-glycans carrying NeuAcα2,6Gal and the increase of O-glycans carrying the disaccharide Galβ1,3GalNAc on the cell surface 37. Similarly, van Vliet et al showed that the activation of human T cells via CD3/CD28 was accompanied by an increase in the expression of Galβ1,3GalNAc on the cell surface 38. We reported in this study direct visualization of a moesin-like protein on the activated CD4 + T cell surface.…”

Section: Discussionmentioning

confidence: 97%

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4⁺ T cells

Ángel

Legorreta-Herrera

Mendoza‐Hernández

et al. 2015

Immunity Inflam & Disease

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The Galβ1,3GalNAcα1,O-Ser/Thr specific lectin from Amaranthus leucocarpus (ALL) binds a ∼70 kDa glycoprotein on murine T cell surface. We show that in the absence of antigen presenting cells, murine CD4+ T cells activated by an anti-CD3 antibody plus ALL enhanced cell proliferation similar to those cells activated via CD3/CD28 at 48 h of culture. Moreover, ALL induced the production of IL-4, IL-10, TNF-alpha, and TGF-beta in CD3-activated cells. Proteomic assay using two-dimensional electrophoresis and far-Western blotting, ALL recognized two prominent proteins associated to the lipid raft microdomains in CD3/CD28-activated CD4+ T cells. By mass spectrometry, the peptide fragments from ALL-recognized proteins showed sequences with 33% homology to matricin (gi|347839 NCBInr) and 41% identity to an unnamed protein related to moesin (gi|74186081 NCBInr). Confocal microscopy analysis of CD3/CD28-activated CD4+ T cells confirmed that staining by ALL colocalized with anti-moesin FERM domain antibody along the plasma membrane and in the intercellular contact sites. Our findings suggest that a moesin-like O-glycoprotein is the ALL-recognized molecule in lipid rats, which induces costimulatory signals on CD4+ T cells.

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Section: Discussionmentioning

confidence: 97%

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4⁺ T cells

Ángel

Legorreta-Herrera

Mendoza‐Hernández

et al. 2015

Immunity Inflam & Disease

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“…In fact, Tn antigen presentation to T cells has been found to be preferentially done through the binding to C‐type macrophage galactose‐type lectin. This leads to a subsequent downstream activation of the ERK‐calcineurin axis and downregulation of C1GALT1C1 expression . Upper respiratory tract infections and tonsillitis are also among the clinical manifestations seen in IgAN patients.…”

Section: The Immunological Impact Of Glycosylation Defects—an Update mentioning

confidence: 99%

CDG and immune response: From bedside to bench and back

Pascoal

Francisco

Ferro

et al. 2019

J of Inher Metab Disea

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Glycosylation is an essential biological process that adds structural and functional diversity to cells and molecules, participating in physiological processes such as immunity. The immune response is driven and modulated by protein‐attached glycans that mediate cell‐cell interactions, pathogen recognition and cell activation. Therefore, abnormal glycosylation can be associated with deranged immune responses. Within human diseases presenting immunological defects are congenital disorders of glycosylation (CDG), a family of around 130 rare and complex genetic diseases. In this review, we have identified 23 CDG with immunological involvement, characterized by an increased propensity to—often life‐threatening—infection. Inflammatory and autoimmune complications were found in 7 CDG types. CDG natural history(ies) and the mechanisms behind the immunological anomalies are still poorly understood. However, in some cases, alterations in pathogen recognition and intracellular signaling (eg, TGF‐β1, NFAT, and NF‐κB) have been suggested. Targeted therapies to restore immune defects are only available for PGM3‐CDG and SLC35C1‐CDG. Fostering research on glycoimmunology may elucidate the involved pathophysiological mechanisms and open new therapeutic avenues, thus improving CDG patients' quality of life.

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“…The role of Tn antigen in the development of cancer remains unclear. Several studies have reported that Tn antigen is bound by the C‐type macrophage galactose binding lectin (MGL) in situ in colorectal tumors . MGL is expressed in dendritic cells and macrophages .…”

Section: Relationship Between Tn Antigen and Tumor Cellsmentioning

confidence: 99%

Tumor‐associated antigens: Tn antigen, sTn antigen, and T antigen

Zhao

Wang

et al. 2016

HLA

169

148

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Glycosylation is one of the major posttranslational modifications of proteins. N-glycosylation (Asn-linked) and O-glycosylation (Ser/Thr-linked) are the two main forms. Abnormal O-glycosylation is frequently observed on the surface of tumor cells, and is associated with an adverse outcome and poor prognosis in patients with cancer. O-glycans (Tn, sTn, and T antigen) can be synthesized in the Golgi apparatus with the aid of several glycosyltransferases (such as T-synthase and ST6GalNAc-I) in a suitable environment. The unique molecular chaperone of T-synthase is Cosmc, which helps T-synthase to fold correctly in the endoplasmic reticulum. Dysregulation of these glycosyltransferases, molecular chaperones, or the environment is involved in the dysregulation of O-glycans. Tn, sTn, and T antigen neo- or over-expression occurs in many types of cancer including gastric, colon, breast, lung, esophageal, prostate, and endometrial cancer. This review discusses the major synthetic pathway of O-glycans and the mechanism by which Tn, sTn, and T antigens promote tumor metastasis.

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Human T Cell Activation Results in Extracellular Signal-regulated Kinase (ERK)-Calcineurin-dependent Exposure of Tn Antigen on the Cell Surface and Binding of the Macrophage Galactose-type Lectin (MGL)*

Cited by 30 publications

References 48 publications

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4⁺ T cells

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4⁺ T cells

CDG and immune response: From bedside to bench and back

Tumor‐associated antigens: Tn antigen, sTn antigen, and T antigen

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Human T Cell Activation Results in Extracellular Signal-regulated Kinase (ERK)-Calcineurin-dependent Exposure of Tn Antigen on the Cell Surface and Binding of the Macrophage Galactose-type Lectin (MGL)*

Cited by 30 publications

References 48 publications

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4+ T cells

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4+ T cells

CDG and immune response: From bedside to bench and back

Tumor‐associated antigens: Tn antigen, sTn antigen, and T antigen

Contact Info

Product

Resources

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Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4⁺ T cells

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4⁺ T cells