EC Number   |
General Information |
Reference |
|---|
   2.7.8.27 | malfunction |
down-regulation of isoform SMS1 and SMS2 reduces the localization of the DAG-binding protein, protein kinase D to the Golgi |
723537 |
| 2.7.8.27 | malfunction |
down-regulation of isoform SMS1 and SMS2 reduces the localization of the DAG-binding protein, protein kinase D to the Golgi. Inhibition of the enzyme significantly reduces insulin secretion in rat INS-1 cells |
723537 |
| 2.7.8.27 | malfunction |
glucose kinetics study using the radiolabeled glucose analog 18F-2-fluoro-2-deoxy-D-glucose (18F-FDG), in wild-type (WT) and SMS2 knockout (KO) mice: insulin signaling is enhanced in the liver, white adipose tissue and skeletal muscle of SMS2 KO mice compared with those of wild-type mice. In addition, compared with in wild-type mice, blood clearance of 18F-FDG is accelerated in SMS2 KO mice when they are fed either a normal or a high fat diet. 18F-FDG uptake is also increased in insulin-targeted tissues such as skeletal muscle in the SMS2 KO mice, whereas skeletal muscle sphingolipid content is not clearly affected. Plasma levels of very long-chain fatty acid (VLCFA)-containing ceramides are markedly increased in SMS2 KO mice compared with in wild-type mice. Genetic inhibition of SMS2 elevates glucose clearance through activation of glucose uptake into insulin-targeted tissues such as skeletal muscle by a mechanism independent of hepatic SMS2. This occurs, at least in part, via indirect mechanisms such as elevation of VLCFA-containing ceramides |
-, 737776 |
| 2.7.8.27 | malfunction |
inhibition of SGMS activity by siRNA transient transfection or by tricyclodecan-9-yl-xanthogenate (D609) significantly reduces the level of amyloid-beta peptide in a dose and time dependent manner. The decrease in amyloid-beta peptide level occurs without changes in amyloid precursor protein expression or cell viability |
739480 |
| 2.7.8.27 | malfunction |
inhibition of sphingomyelin synthase activity profoundly impairs the killing ability of neutrophils against Cryptococcus neoformans by preventing the extracellular release of an antifungal factors |
723525 |
| 2.7.8.27 | malfunction |
SMS2 deficiency causes significant induction of cholesterol efflux in vitro and in vivo, SMS2 deficiency in the macrophages reduces atherosclerosis in mice |
708149 |
| 2.7.8.27 | malfunction |
sphingomyelin synthase (SMS) deficiency promotes cell migration through a CXCL12/CXCR4-dependent signaling pathway involving extracellular signal-regulated kinase activation. In addition, SMS1/SMS2 double-knockout cells have heightened sensitivity to CXCL12. SMS deficiency facilitates relocalization of CXCR4 to lipid rafts, which form platforms for the regulation and transduction of receptor-mediated signaling. Furthermore, SMS deficiency potentiates CXCR4 dimerization, which is required for signal transduction |
723175 |
| 2.7.8.27 | metabolism |
sphingomyelin synthase (SMS) is the last key enzyme in the sphingosine-1-phosphocholine synthesis process |
738955 |
| 2.7.8.27 | more |
minimal mathematical model for the sphingomyelin synthase 1 (SMS1) driven conversion of ceramide to sphingomyelin based on chemical reaction kinetics, modeling sphingomyelin synthase 1 driven reaction at the Golgi apparatus can explain data by inclusion of a positive feedback mechanism, this model is not able to qualitatively reproduce experimental measurements on lipid compositions after altering SMS1 activity, overview |
738936 |
| 2.7.8.27 | physiological function |
enzyme SGMS activity impacts on amyloid precursor protein processing to produce amyloid-beta peptide and it seems to be a contributing factor in amyloid-beta peptide pathology associated with Alzheimer's disease. SGMS1 activity regulates amyloid precursor protein processing and not production |
739480 |
