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Changes in sugar metabolism are well documented in diabetes, neurodegenerative, and cancer diseases. This phenomenon is conjugated to impaired protein glycosylation. It has been reported recently that the unique -N-acetyl glucose amine proteins modification is altered in diabetes and Alzheimer diseases. The current study hypothesize that O-GlcNAcylation is altered during cancer metastasis which leads to dysregulation of the modified proteins and thus contribute to the metastasis phenotype. Proteomics analysis of nuclear proteins showed, that GlcNAcylation profile is different between the metastatic and nonmetastatic colorectal cancer clones. Interestingly, GlcNAcylation of several proteins is elevated in the metastatic clone while the GlcNAcylation of others is elevated in the nonmetastatic clones. Metastatic and metastatic clones treatments with glucose, GlcNAc and streptozotocin—an inhibitor of O-GlcNAcase— leads to the elevation in total proteins GlcNAcylation. Remarkably, several proteins possess GlcNAcylation only after cancer cell treatments. Glucose and GlcNAc treatments lead to reduced viability of the metastatic and nonmetastatic cell cultures in dose response manner. surprisingly, the metastatic clone renders higher sensitivity to those treatments. STZ treatment in combination with GlcNAc is additive and more effective than STZ alone. These results shed lights on GlcNAcylation involvement in cancer metastasis and pave the way for comprehensive elucidation.