Regulation and clinical significance of O-GlcNAc transferase in cancer

Abstract

O-GlcNAc Transferase (OGT) resides in both cytosolic and nuclear compartments and catalyzes O-GlcNAcylation of myriad proteins. Numerous excellent reviews concerning roles of OGT in organismal and cellular physiology have exist, and aberrant OGT and protein O-GlcNAcylation have been implicated in progression and metastasis of different cancer types. Thus, understanding the regulation mechanisms of OGT and O-GlcNAcylation in tumor cells and their difference compared to non-tumor cells may elucidate new mechanisms related to tumor generation and development, could provide a new marker to diagnosis and prognosis in patients with cancer and indicate a new target to cancer chemotherapy. While it has become evident that OGT plays critical roles in cancers, it remains unclear how they are deregulated. This review provides an overview of our current knowledge about the known/potential regulation of OGT, and also discusses the inhibition of OGT as a potential novel therapeutic target for cancer treatment.

O-GlcNAcylation in early stages of chronic lymphocytic leukemia: Protocol development for flow cytometry

“…nutrient supply in a different rate compared to normally functioning cells. Most types of tumors shift their energy metabolism towards glycolytic activity even under aerobic conditions which results in elevated lactate production and lower pyruvate transmission to the O-GlcNAcylation is proven to be altered in certain conditions, such as type 2 diabetes mellitus [9], Alzheimer's disease [10] and in cancer [11][12][13][14]. 52 Leukemic B cells have been reported to differ from 53 healthy B lymphocytes both in terms of overall intracel-54 lular glycosylation and O-GlcNAcylation of certain pro-55 teins as well [11,15].…”