Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
Study reports that OGA is upregulated in a wide range of human cancers and drives aerobic glycolysis and tumor growth by inhibiting pyruvate kinase M2 (PKM2). PKM2 is dynamically O-GlcNAcylated in response to changes in glucose availability. Under high glucose conditions PKM2 is a target of OGA-associated acetyltransferase activity which facilitates O-GlcNAcylation of PKM2 by O-GlcNAc transferase (OGT).
role of the tubular biomarkers NAG kidney injury molecule-1 and neutrophil gelatinase-associated lipocalin in patients with chest pain before contrast media exposition
OGT promotes carcinogenesis and metastasis of cervical cancer cells. OGT's expression is significantly upregulated in cervical cancer and low OGT level is correlated with improved prognosis
OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1beta and a purified OGA-SPT5-TIF1beta complex has elongation properties.
Estrogen replacement therapy and plyometric training influence muscle OGT and OGA gene expression which may be one of the mechanisms by which HRT and PT prevent aging-related loss of muscle mass.
O-linked beta-N-acetylglucosaminylation (O-GlcNAcylation) in primary and metastatic colorectal cancer clones and effect of N-acetyl-beta-D-glucosaminidase silencing on cell phenotype and transcriptome.
Data show that the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
Reducing ChREBP(OG) levels via OGA overexpression decreased lipogenic protein content (ACC FAS) prevented hepatic steatosis and improved the lipidic profile of OGA-treated db/db mice.
This study analyzes the activity of the enzyme involved in the removal of these sugar residues i.e. beta-N-acetylglucosaminidase (O-GlcNAcase) as well as the level of N-acetylglucosamine in benign and malignant thyroid lesions.
the short nuclear variant of O-GlcNAcase which has the identical catalytic domain as the full-length enzyme has similar trends in a pH-rate profile and Taft linear free energy analysis as the full-length enzyme
review of modifications phosphorylation and a specific form of glycosylation O-linked -N-acetylglucosaminylation by O-GlcNAc relevant to pathological tau phosphorylation
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.