= Emerging. More than 5 years before clinical availability. (9.82%)
= Expected to be clinically available in 1 to 4 years. (12.95%)
= Clinically available now. (22.77%)
MSACL 2018 EU : Pirro

MSACL 2018 EU Abstract

Topic: Proteomics

Podium Presentation in the Ether on Thursday at 14:30 (Chair: Yuri van der Burgt)

Proteomic Analysis of MGL Binding Protein in Human Cancer Cells

Martina Pirro (Presenter)
Leiden University Medical Center LUMC

Presenter Bio(s): I am Martina Pirro and I just started the 3rd year of my Phd program, part of the GlyCoCan Marie Curie training network. Since 2016, I am working under the supervision of Paul Hensbergen in the group of Prof. Dr. Manfred Wuhrer at the Center for Proteomics and Metabolomics (LUMC, Leiden). Here, my main focus involves the glycoproteomic analysis of secreted and cell surface glycoproteins from colorectal cancer.
In January-March 2018, I carried out part of the PhD training at the R&D department of Ludger, in Culham Science Center (Abingdon, UK), focusing on N- and O-glycomics of colorectal cancer cell lines.
In March-May 2017, I joined the CNRS (IPBS, Toulouse, France). There, I used quantitative mass spectrometry to identify glycoproteins as novel ligands of the macrophage galactose lectin (MGL), using T cell leukemia and colorectal cancer cell lines.

Authors: Martina Pirro (1), Esmee Schoof (1), Yassene Mohammed (1), Sandra van Vliet (2), Yoann Rombouts (3), Peter van Veelen (1), Manfred Wuhrer (1) and Paul Hensbergen (1)
(1) Leiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.


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 20 cell surface proteins as novel MGL-ligands.

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