Early GalNAc O-Glycosylation: Pushing the Tumor Boundaries

Joana Gomes; Stefan Mereiter; Ana Magalhães; Celso A Reis

doi:10.1016/j.ccell.2017.10.010

Early GalNAc O-Glycosylation: Pushing the Tumor Boundaries

Cancer Cell. 2017 Nov 13;32(5):544-545. doi: 10.1016/j.ccell.2017.10.010.

Authors

Joana Gomes¹, Stefan Mereiter¹, Ana Magalhães¹, Celso A Reis²

Affiliations

¹ i3S - Institute for Research and Innovation in Health, University of Porto, 4200-135 Porto, Portugal; IPATIMUP - Institute of Molecular Pathology and Immunology, University of Porto, 4200-465 Porto, Portugal.
² i3S - Institute for Research and Innovation in Health, University of Porto, 4200-135 Porto, Portugal; IPATIMUP - Institute of Molecular Pathology and Immunology, University of Porto, 4200-465 Porto, Portugal; Instituto de Ciências Biomédicas Abel Salazar (ICBAS), University of Porto, 4050-313 Porto, Portugal; Faculty of Medicine, University of Porto, 4200-319 Porto, Portugal. Electronic address: celsor@ipatimup.pt.

PMID: 29136499
DOI: 10.1016/j.ccell.2017.10.010

Abstract

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.

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MeSH terms

Endoplasmic Reticulum
Glycosylation
Golgi Apparatus
Humans
Liver Neoplasms*
Matrix Metalloproteinase 14
N-Acetylgalactosaminyltransferases*

Substances

N-Acetylgalactosaminyltransferases
MMP14 protein, human
Matrix Metalloproteinase 14