Ma, J.F., Hart, G.W.: Protein O-GlcNAcylation in diabetes and diabetic complications. Exp. Rev. Proteom. 10 , 365–380 (2013)Ma J,Hart GW (2013). Protein O-GlcNAcylation in diabetes and diabetic complications . Expert review of proteomics , 10 : 365-380...
O-GlcNAcylation can be viewed as the essential 'grease and glue' of the cell: it acts as a 'grease' by coating target proteins (folded or unfolded, mature or nascent) and preventing unwanted protein aggregation or modification; it also acts as a 'glue' by modulating protein–protein interact...
O-GlcNAcylation is a post-translational modification of protein in response to genetic variations or environmental factors, which is controlled by two highly conserved enzymes, i.e. O-GlcNAc transferase (OGT) and protein O-GlcNAcase (OGA). Protein O-GlcN
Protein O-GlcNAcylation: a new signaling paradigm for the cardiovascular system The posttranslational modification of serine and threonine residues of nuclear and cytoplasmic proteins by the O-linked attachment of the monosaccharide be... B Laczy,BG Hill,W Kai,... - 《Am J Physiol Heart Circ ...
The posttranslational modification of serine and threonine residues of nuclear and cytoplasmic proteins by the O-linked attachment of the monosaccharide beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic and ubiquitous protein modification. Protein O-GlcNAcylation is rapidly emerging as a key regula...
We hypothesized that the auto-protective stress signal, known as protein O-GlcNAcylation, would confer a pro-survival benefit in CPCs. Methods/Results We genetically and pharmacologically augmented O-GlcNAc levels in CPCs (c-kit + /lin ) with loss- and gain-of-function approaches, i.e., ...
Thus, we report the primary demonstration of protein O-GlcNAcylation as an important pro-survival signal in CSCs, which could enhance CSC survival prior to in vivo autologous transfer. 展开 关键词: Adult stem cells Cardiac Cell biology Hypoxia ...
As reported in AD, defective HBP is responsible for flawed protein O‐GlcNAcylation coupled by a mutual inverse increase of protein phosphorylation on Ser/Thr residues, which gives to O‐GlcNAcylation the ability to modulate various pathways involved in AD progression. Previous studies have shown the...
Here, we studied protein O-GlcNAcylation, OGT, and OGA in the rat brain at various ages from embryonic day 15 to the age of 2 years. We found a gradual decline of global protein O-GlcNAcylation during developmental stages and adulthood. This decline correlated positively to the total protein...
Post-hypoxic CSCs responded by time-dependently increasing protein O-GlcNAcylation upon reoxygenation. We utilized pharmacological interventions for loss- and gain-of-function, i.e., enzymatic inhibition of OGT (adds the O-GlcNAc modification to proteins) by TT04, or inhibition of OGA (removes O-...