Aberrant Glycosylation in Cancer: A Novel Molecular Mechanism Controlling Metastasis – PREVIEW

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Aberrant Glycosylation in Cancer: A Novel Molecular Mechanism Controlling Metastasis – PREVIEW

Sexta, 21.07.2017

Major alterations in cell glycosylation occurring during cancer development and progression represent key features of tumor cell malignant behavior. In this publication, the authors preview and put in context the findings of Agrawal et al. (Cancer Cell, Vol. 31, Issue 6, 2017) that identified and characterized a novel molecular mechanism in which aberrant glycosylation actively tunes the metastatic capacity of melanoma cells by preventing the proteolytic cleavage of the L1CAM adhesion molecule.

 

Autores e Afiliações:

Ana Magalhães1,2, Henrique O. Duarte1,2,3 and Celso A. Reis1,2,3,4

1Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal

2Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP), 4200-135 Porto, Portugal

3Instituto de Ciências Biomédicas Abel Salazar (ICBAS), University of Porto, 4050-313 Porto, Portugal

4Faculty of Medicine of the University of Porto, 4200-319 Porto, Portugal

 

Abstract:

Glycosylation alterations are involved in several steps of human cancer pathogenesis. In this issue of Cancer Cell, Agrawal et al. identified the glycosyltransferase FUT8 as a previously unrecognized mediator of melanoma metastasis, establishing core fucosylation as a potential therapeutic target for prevention and treatment of metastatic tumors.

 

Journal: Cancer Cell

 

Link: https://linkinghub.elsevier.com/retrieve/pii/S1535-6108(17)30208-8