| Literature DB >> 25656895 |
Anna Arnal-Estapé1, Don X Nguyen2.
Abstract
Glycosylation is one of the most predominant forms of cell-surface protein modifications, yet its deregulation in cancer and contribution to tumor microenvironment interactions remain poorly understood. In this issue of Cancer Discovery, Reticker-Flynn and Bhatia characterize an enzymatic switch in lung cancer cells that triggers aberrant surface protein glycosylation patterns, adhesion to lectins on the surface of inflammatory cells, and subsequent metastatic colonization of the liver. ©2015 American Association for Cancer Research.Entities:
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Year: 2015 PMID: 25656895 PMCID: PMC4340588 DOI: 10.1158/2159-8290.CD-15-0013
Source DB: PubMed Journal: Cancer Discov ISSN: 2159-8274 Impact factor: 39.397