Endo-beta-N-Acetylglucosaminidase Proteine (ENGASE)

Human Endo-beta-N-Acetylglucosaminidase (ENGASE) Interaktionspartner

1. In patients with autosomal dominant polycystic kidney disease, urinary NAGase was correlated with urinary ET-1 (zeige EDN1 Proteine) which was inversely associated with eGFR (zeige EGFR Proteine) and positively correlated with total kidney volume.

2. Serological N-acetyl-glucosaminidase (zeige NAGLU Proteine), telomere length, and the UCP2 (zeige UCP2 Proteine)-886G>A variant are independent risk factors for type 2 diabetes.

3. As the generation of the bulk of fOS is unaffected by co-down regulation of Ngly1p and Engase1p, alternative quantitatively important mechanisms must underlie the liberation of these fOS from either LLO or glycoproteins during protein N (zeige NP Proteine)-glycosylation.

4. O-GlcNAcase (zeige MGEA5 Proteine) expression is increased in erythrocytes from both individuals with pre-diabetes and individuals with less well-controlled diabetes.

5. involved in processing of free oligosaccharides in the cytosol; identification of the gene encoding human cytosolic ENGase

6. endo-beta-n-acetylglucosaminidase present in the synovial fluid of rheumatoid arthritis patients, may contribute to the depletion of glycosaminoglycans from cartilage allowing the invasion of synovial cells

7. identification of O-GlcNAcase (zeige MGEA5 Proteine) as a caspase-3 (zeige CASP3 Proteine) substrate with a novel caspase-3 (zeige CASP3 Proteine) cleavage site and provide insight about O-GlcNAcase (zeige MGEA5 Proteine) regulation during apoptosis.

Mouse (Murine) Endo-beta-N-Acetylglucosaminidase (ENGASE) Interaktionspartner

1. These observations strongly suggest that the Ngly1 (zeige NGLY1 Proteine)- or Ngly1 (zeige NGLY1 Proteine)/Engase-deficient mice could serve as a valuable animal model for studies related to the pathogenesis of the NGLY1 (zeige NGLY1 Proteine)-deficiency, and that cytoplasmic ENGase represents one of the potential therapeutic targets for this genetic disorder.

2. ENGase efficiently hydrolyzes phosphorylated oligosaccharides that are larger than Man4GlcNAc2-P, generating GlcNAc-1-P and neutral Gn1 (zeige GYG1 Proteine)-type free oligosaccharides.