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Fahie, K. M. M., Papanicolaou, K. N., & Zachara, N. E. (2022). Integration of o-glcnac into stress response pathways. Cells, 11(3509). Added by: Dr. Enrique Feoli (07/11/2025, 23:56) Last edited by: Dr. Enrique Feoli (07/11/2025, 23:59) |
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| Resource type: Journal Article DOI: 10.3390/cells11213509 ID no. (ISBN etc.): 2073-4409 BibTeX citation key: Fahie2022 View all bibliographic details  |
Categories: BioAcyl Corp, BioAcyl Corp Subcategories: Cell injury cytoprotection, Resilience Creators: Fahie, Papanicolaou, Zachara Collection: Cells |
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| Abstract |
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The modification of nuclear, mitochondrial, and cytosolic proteins by O-linked βN-acetylglucosamine (O-GlcNAc) has emerged as a dynamic and essential post-translational modification of mammalian proteins. O-GlcNAc is cycled on and off over 5000 proteins in response to diverse stimuli impacting protein function and, in turn, epigenetics and transcription, translation and proteostasis, metabolism, cell structure, and signal transduction. Environmental and physiological injury lead to complex changes in O-GlcNAcylation that impact cell and tissue survival in models of heat shock, osmotic stress, oxidative stress, and hypoxia/reoxygenation injury, as well as ischemic reperfusion injury. Numerous mechanisms that appear to underpin O-GlcNAc-mediated survival include changes in chaperone levels, impacts on the unfolded protein response and integrated stress response, improvements in mitochondrial function, and reduced protein aggregation. Here, we discuss the points at which O-GlcNAc is integrated into the cellular stress response, focusing on the roles it plays in the cardiovascular system and in neurodegeneration.
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Added by: Dr. Enrique Feoli Last edited by: Dr. Enrique Feoli |