Aberrant protein glycosylation in cancer: implications in targeted therapy

• Type: Another Publication in an International Scientific Journal
• Date: 2021

Authors

Rodrigues, JG (Author) Other; Duarte, HO (Author) Other; Celso Reis (Author) ICBAS; Gomes, J (Author) Other

Journal

Title: Biochemical Society Transactions

Vol. 49

Pages: 843-854

ISSN: 0300-5127

Publisher: PORTLAND PRESS LTD

Indexing

ISI Web of Knowledge - 4 Citations

Scopus - 4 Citations

Other information

Authenticus ID: P-00T-WMF

DOI: 10.1042/bst20200763

Abstract (EN): Aberrant cell surface glycosylation signatures are currently known to actively drive the neoplastic transformation of healthy cells. By disrupting the homeostatic functions of their protein carriers, cancer-associated glycans mechanistically underpin several molecular hallmarks of human malignancy. Furthermore, such aberrant glycan structures play key roles in the acquisition of molecular resistance to targeted therapeutic agents, which compromises their clinical efficacy, by modulating tumour cell aggressiveness and supporting the establishment of an immunosuppressive microenvironment. Recent advances in the study of the tumour cell glycoproteome have unravelled previously elusive molecular mechanisms of therapeutic resistance, guided the rational design of novel personalized therapeutic strategies, and may further improve the clinical performance of currently approved anti-cancer targeted agents. In this review, we highlight the impact of glycosylation in cancer targeted therapy, with particular focus on receptor tyrosine kinase-targeted therapy, immune checkpoints blockade therapy, and current developments on therapeutic strategies directed to glycan-binding proteins and other innovative glycan therapeutic strategies.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 12