Glycosylationis an importantpost-translational modification that plays critical roles in cellularphysiology, cell–cell interactions, and cancer developmentand progression. Aberrant glycosylation is a hallmark of the tumormicroenvironment, and the activities of specific glycosidases andglycosyltransferases underpin these molecular changes.1 These enzymes are responsible for modifying proteins andlipids with glycans that may modulate their functions and activities.Here, Urano and co-workers exploit the enzymatic activities of theglycosidase α-mannosidase and γ-glutamyltranspeptidase(GGT) to design fluorogenic activity-based probes that enable rapiddetection and discrimination of malignant and benign human breasttumors from the surrounding tissues.2 Thisfeat could enable accurate differentiation of breast cancer from healthytissues during breast tumor resection in the clinic.
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