Pathways Also Have Strong Connection
The importance of O-GlcNAcylation in maintaining normal cell function in mammalian organisms has en demonstrat by the three lines of evidence. 1. Mechanistically, protein O-GlcNAcylation, primarily regulat by OGT and OGA levels and activities, can regulate gene transcription and proteasomal activities, as well as autophagy (Wells et al., 2001; Zhang et al., 2003; Wani et al., 2015; Wani et al., 2017c; Dodson et al., 2018; and Zhang et al., 2018). 2. Genetically, OGT mutations are associat with X-link intellectual disability in humans. In rodents, an OGA splice variant is link to a genetic model of diates in the Goto-Kakizaki (GK) diatic.
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While OGT and OGA gene disruption are either embryonic or perinatal lethal in mice (O’Donnell et al., 2004; Shafi et al., 2000; Watson et al., 2014; and Yang et al., 2012). 3. Pharmacological inhibitors have en develop, and the effects of inhibition of OGA have en assess in different models of disease. The OGA inhibitor thiamet G is of special interest as it has an IC50 in the nM range and oral delivery of thiamet G decreases pathogenic tau phosphorylation in the brain in transgenic mice Georgia Email List overexpressing tau (Yuzwa et al., 2008; Yuzwa et al., 2012). These and similar observations have result in an increas interest in O-GlcNAc biology in various cells and tissues in response to diverse signals. Traditionally, the overall O-GlcNAcylation levels in an experimental system have en detect by western blot analyses using a few antibodies develop against a handful of O-GlcNAcylat proteins.
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A key assumption is that the levels of O-GlcNAcylation of these proteins represent the overall O-GlcNAcylation levels of most other cellular proteins (Arnold et al., 1996; Comer et al., 2001). This assumption is not without its caveats. For example, the antigens us for generating anti-O-GlcNAc antibodies are from abundant proteins in the cell. The epitopes these antibodies recognize do not represent all possible epitopes for cellular O-GlcNAcylat protein sites. Thus, the signals from TH Lists antibody-bas assays for total levels of O-GlcNAcylation can only give limit information on the levels of O-GlcNAcylation of less abundant proteins such as those involv in cell signaling.
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