Zaburzenia procesu O-GlcNAcylacji w nowotworach
Journal Title: Folia Medica Lodziensia - Year 2014, Vol 41, Issue 1
Abstract
O-GlcNAcylation is a post-translational modification involving the addition of a N-acetylglucosamine moiety to the serine/threonine residues of cytosolic or nuclear proteins. Two enzymes are responsible for cyclic O-GlcNAcylation: O-GlcNAc transferase (OGT) which catalyzes the addition of the GlcNAc moiety from UDP-GlcNAc to target proteins and O-GlcNAcase (OGA) which catalyses the hydrolytic removal of the sugar moiety from proteins. Dynamic and reversible O-GlcNAcylation is emerging as an important regulator of diverse cellular processes, such as signal transduction, metabolism, transcription, translation, proteasomal degradation and cell cycle. O-GlcNAcylation occurs on serine or threonine residues of proteins at sites that may also be phosphorylated. Therefore, an extensive crosstalk exists between phosphorylation and O GlcNAcylation. Recent studies indicate that increased O-GlcNAcylation is a general feature of cancer. Elevated O-GlcNAcylation (hyper-O-GlcNAcylation) occurs in many human malignancies including solid tumors such as lung, prostate, breast, colorectal, liver, pancreatic cancers as well as non solid cancers such as chronic lymphocytic leukemia. The changes in O GlcNAcylation are associated with the changes in OGT and OGA expression levels. Hyper-O-GlcNAcylation may be linked to the various hallmarks of cancer, including cancer cell proliferation, survival, invasion, metastasis and metabolism. This paper reviews recent findings related to O GlcNAc-dependent regulation of signaling pathways, cell cycle, transcription factors, and metabolic enzymes in cancer cells.
Authors and Affiliations
Piotr Ciesielski, Anna Krześlak
Keywords
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