Proteomics

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Glycoproteomic analysis of MGL binding protein on acute T cell leukemia cells


ABSTRACT: O-glycosylation is generally initiated by the transfer of a N-acetylgalactosamine to Ser/Thr residues of proteins, forming the Tn antigen. This truncated surface glycan is expressed at high levels by tumor cells and is associated with higher metastatic behaviour and poor prognosis of patients. The Tn antigen is recognised by the C-type macrophage galactose lectin (MGL), which induces the activation of immunosuppressive responses. Here, we investigated the MGL binding proteins in Jurkat cells. The optimization of pull-down assays and subsequent glycoproteomic analysis by mass spectrometry, allowed us to identify 17 cell surface proteins as novel MGL-ligands.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell, Cell Culture

DISEASE(S): Acute Leukemia

SUBMITTER: Yassene Mohammed  

LAB HEAD: Paul Hensbergen

PROVIDER: PXD011307 | Pride | 2019-01-02

REPOSITORIES: Pride

Dataset's files

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L20182000421a.raw Raw
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Publications

Glycoproteomic Analysis of MGL-Binding Proteins on Acute T-Cell Leukemia Cells.

Pirro Martina M   Schoof Esmee E   van Vliet Sandra J SJ   Rombouts Yoann Y   Stella Alexandre A   de Ru Arnoud A   Mohammed Yassene Y   Wuhrer Manfred M   van Veelen Peter A PA   Hensbergen Paul J PJ  

Journal of proteome research 20190109 3


C-type lectins are a diverse group of proteins involved in many human physiological and pathological processes. Most C-type lectins are glycan-binding proteins, some of which are pivotal for innate immune responses against pathogens. Other C-type lectins, such as the macrophage galactose-type lectin (MGL), have been shown to induce immunosuppressive responses upon the recognition of aberrant glycosylation on cancer cells. MGL is known to recognize terminal N-acetylgalactosamine (GalNAc), such as  ...[more]

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