Early GalNAc O-Glycosylation: Pushing the Tumor Boundaries

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Early GalNAc O-Glycosylation: Pushing the Tumor Boundaries

Sexta, 09.02.2018

Cellular glycosylation occurring during cancer development and progression represent key features of tumor cell malignant behavior. In this publication, the authors preview and discuss the findings of Nguyen et al. (Cancer Cell. 2017 Nov 13;32(5):639-653) who identified a molecular mechanism in which the relocation of a glycosyltransferase mediating protein O-glycosylation initiation, from the Golgi to endoplasmic reticulum, leads to aberrant glycosylation. This process activates an extracellular matrix-degrading metalloproteinase and therefore induces tumor growth and invasion.


Autores e Afiliações:

Joana Gomes1,2, Stefan Mereiter1,2 , Ana Magalhaes1,2 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



Glycosylation alterations are frequently observed in cancer cells and shape tumor progression. In this issue of Cancer Cell, Nguyen et al. show that GALNT1 relocation from Golgi to endoplasmic reticulum drives liver tumor growth and invasion, due to enhanced glycosylation and consequential activation of the extracellular matrix-degrading metalloproteinase MMP14.


Revista: Cancer Cell


Link: http://www.cell.com/cancer-cell/fulltext/S1535-6108(17)30463-4