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• W3016590989 abstract "About 2% to 5% of all glucose that enters the cell is directed to the Hexosamine Biosynthetic Pathway (HBP), which has glutamine fructose-6-phosphate aminotransferase (GFAT) as the rate-limiting step enzyme. HBP has UDP-N-acetylglucosamine (UDP-GlcNAc) as a final product, which can be used as substrate for intracellular O-GlcNAc; a post-translational modification (PTM) resulting from the covalent attachment of a GlcNAc to the hydroxyl groups on serine and threonine residues in proteins. This reaction is catalyzed by O-GlcNAc transferase (OGT), and the removal reaction of this monosaccharide is made by O-GlcNAcase (OGA). The balance of the activity of such enzymes and UDP-GlcNAc availability will regulate the levels of O-GlcNAcylated proteins, with an O-GlcNAcylation, similarly to phosphorylation, highly inducible, dynamic and active in many cellular processes. Tyrosine hydroxylase (TH) is the rate-limiting step enzyme in catecholamine synthesis, responsible for hydroxylate L-tyrosine at meta-position to obtain L-DOPA, the precursor of dopamine, which has a physiological role as a neurotransmitter. There are several supports on the literature that phosphorylation on serine 40 of TH increases its activity on a dynamical way, however, the mechanism of how O-GlcNAc plays a role on this modulation remains unknown. We showed in PC12 cells treated with the pharmacological inhibitor of OGA Thiamet G (TMG); and nerve growth factor (NGF), a compound that induces these cells in a process of neuritogenesis, that O-GlcNAcylation acts on the control of the phosphorylation levels of serine 40 in TH, where stimulation by 28% on the increase in phosphorylation at serine 40 decreases the levels of O-GlcNAc in 26% compared to control; while the increase of intracellular O-GlcNAc in 19% reduces the phosphorylation at serine 40 by 16%. In addition, HPLC analysis shows that the increase of intracellular O-GlcNAc reduces the levels of L-DOPA and dopamine by 80%. Finally, TH’s immunoprecipitation analysis reveals that it is O-GlcNacylated, and this PTM regulates its activity. These data suggest a cellular mechanism that integrates carbohydrate metabolism (by HBP) with the catecholamine biosynthetic pathway in a neuritogenesis process; where competition between O-GlcNAc and phosphate at serine 40 tyrosine hydroxylase site modulates its activity, controlling the synthesis of dopamine levels in PC12 cells. Support or Funding Information Funding: CNPq, CAPES, FAPERJ" @default.
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• W3016590989 date "2020-04-01" @default.
• W3016590989 modified "2023-09-25" @default.
• W3016590989 title "The Interplay between O‐GlcNAc And Phosphorylation on Tyrosine Hydroxylase Activity And Cathecolamine Synthesis in PC12 Cells" @default.
• W3016590989 doi "https://doi.org/10.1096/fasebj.2020.34.s1.00073" @default.
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