Recombinant Human Diacylglycerol kinase epsilon (DGKE)

1. mutations can lead to atypical hemolytic uremic syndrome or membranoproliferative glomerulonephritis PMID:28526779
2. Letter/Case Report: atypical haemolytic uraemic syndrome in a Japanese patient with DGKE genetic mutations. PMID:26018111
3. Report DGKE intronic mutations located beyond the exon-intron boundaries in familial hemolytic uremic syndrome. PMID:25854283
4. Data suggest that complement dysregulation influences the onset and disease severity in carriers of diacylglycerol kinase-epsilon mutations PMID:25135762
5. DGKE silencing in resting endothelial cells does not affect complement activation at their surface. PMID:25498910
6. Our study expands the clinical phenotypes associated with mutations in DGKE and challenges the benefits of complement blockade treatment in such patients PMID:24511134
7. DGKzeta localizes to the nucleus and is considered to regulate nuclear diacylglycerol signaling.[review] PMID:24119575
8. Fully activating high-density transfected muscarinic receptors (M1Rs) by oxotremorine-M (Oxo-M) leads to similar calcium, DAG, and PKC signals, but PIP2 is depleted. PMID:23630338
9. Recessive mutations in DGKE cause atypical hemolytic-uremic syndrome. PMID:23542698
10. Substrate specificity of DGKE is not a consequence of competition with hydrolysis of ATP. PMID:23261795
11. performed homozygosity mapping and whole exome sequencing in a Turkish consanguineous family and identified DGKE gene variants as the cause of a membranoproliferative-like glomerular microangiopathy PMID:23274426
12. Inhibition of lipid signaling enzyme diacylglycerol kinase epsilon attenuates mutant huntingtin toxicity. PMID:22511757
13. A role for diacylglycerol kinase (DGK) and its downstream product phosphatidic acid (PA) in ANCA-induced neutrophil exocytosis, is reported. PMID:21833457
14. The region responsible for this arachidonoyl specificity is the lipoxygenase (LOX)-like motif found in the accessory domain, adjacent to DGKvarepsilon's catalytic site. PMID:22266092
15. diacylglycerol kinase-epsilon (DGKepsilon) has less preference for the acyl chain at the sn-1 position of diacylglycerol (DAG) than the one at the sn-2 position PMID:22108654
16. DGK activity is reduced by oxidative stress in human mesangial cells cultured under high glucose conditions. PMID:21725595
17. The hydrophobic domain of diacylglycerol kinase epsilon does not contribute to substrate specificity but plays a role in permanently sequestering the enzyme to a membrane. PMID:17455907
18. The alpha and zeta isoforms of diacylglycerol kinase are inhibited by 2,3-dioleoylglycerol, but not the more substrate-selective epsilon isoform PMID:18004883
19. Substrate specificity of diacylglycerol kinase epsilon is determined by selectivity of the sn-1 and sn-2 acyl chains phosphatidic acid or diacylglycerol. PMID:19744926

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HGNC: 2852

UNIGENE: Hs.239514

KEGG: hsa:8526

STRING: 9606.ENSP00000284061

OMIM: 601440