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30 September 2024
Published online 5 May 2010
Post-translational modification by β-N-acetyl-D-glucosamine (O-GlcNAc) is a highly dynamic response to cellular stress. However, a lack of O-GlcNAc-specific antibodies dampens efforts to detect and isolate these modified versions of proteins for studying.
A group of researchers, including Galal Elsayed from Ain Shams University, Egypt, obtained a large array of O-GlcNAc-specific antibodies using a three-component immunogen. This procedure allowed the researchers to identify >200 different mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
An increased level of O-GlcNAc in a rat model during resuscitation led to an improvement in organ function and decreased tissue injury. An increase in the breakdown of O-GlcNAc was also associated with an increase in markers of liver injury. Although the specific proteins that led to modifications of O-GlcNAc levels in response to trauma-haemorrhage and resuscitation were difficult to indentify, the new antibodies helped to distinguish a group of them that might help to regulate the response of the liver to stress.
Previous studies have linked alterations of O-GlcNAc levels to many widespread human diseases such as type II diabetes and Alzheimer's disease. The new tools put forward by the researchers might allow further investigation into how O-GlcNAc-modified proteins could be used to treat these diseases.
Full access to the original paper can be found through Nature Middle East's "Our Picks" page.
doi:10.1038/nmiddleeast.2010.146
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