EC Number   |
Protein Variants |
Reference |
|---|
   2.3.1.297 | more |
CerS2 knockdown by shRNA |
753223 |
| 2.3.1.297 | more |
CerS2 knockdown by siRNA |
-, 754083 |
| 2.3.1.297 | more |
CerS2 null mouse generation from embryonic stem cells harboring a gene trap (GT) retroviral vector insertion in the first intron of the CerS2 gene, and characterization of the changes in the long chain base and sphingolipid composition of livers from these mice. Ceramide and downstream sphingolipids are devoid of very long (C22-C24) acyl chains, consistent with the substrate specificity of CerS2 toward acyl-CoAs. C16-ceramide levels are elevated, and as a result, total ceramide levels are unaltered. C16-ceramide synthesis in vitro is not increased. Levels of sphinganine are significantly elevated by up to 50fold, reminiscent of the effect of the ceramide synthase inhibitor fumonisin B1. With the exceptions of glucosylceramide synthase and neutral sphingomyelinase 2, none of the other enzymes tested in either the sphingolipid biosynthetic or degradative pathways are significantly changed. Total glycerophospholipid and cholesterol levels are unaltered, although there is a marked elevation in C18:1 and C18:2 fatty acids in phosphatidylethanolamine, concomitant with a reduction in C18:0 and C20:4 fatty acids |
754089 |
| 2.3.1.297 | more |
cloning of a chimeric HA-tagged CerS5:CerS2 isozymes heterodimer, insertion of a transmembrane (TM) domain3 between the two monomers of the dimer (CerS5:TM:CerS5-HA). Chimeric mutant CerS5:TM:CerS2-HA displays slightly more activity using C16-CoA as substrate than CerS5, but remarkably, CerS2 activity measured using C22-CoA is elevated by 3fold. Isozymes CerS5 and CerS6 modulate CerS2 activity upon coexpression. This increase in CerS2 activity is abolished using a noncatalytically active form of CerS5 in the constitutive dimer (CerS5HH:TM:CerS2-HA), demonstrating that optimal CerS2 activity depends on an interaction with a catalytically active form of CerS5 |
754101 |
| 2.3.1.297 | more |
complementation of the growth defect of DELTAlag1/DELTAlac1 yeast deletion mutant by recombinant GST-/FLAG-tagged LOH1. Upon isolation of a microsomal membrane fraction from yeast expressing the construct, LOH1 shows significant activity by an in vitro ceramide synthase assay |
752718 |
| 2.3.1.297 | more |
complementation of the growth defect of DELTAlag1/DELTAlac1 yeast deletion mutant by recombinant GST-/FLAG-tagged LOH3. Upon isolation of a microsomal membrane fraction from yeast expressing the construct, LOH3 shows significant activity by an in vitro ceramide synthase assay |
752718 |
| 2.3.1.297 | more |
in HeLa cells overproducing the fatty acid 2-hydroxylase FA2H, knockdown of CerS2 by siRNA results in a reduction in total long-chain 2-hydroxy-ceramides, confirming enzyme substrate specificity for chain length. Profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview |
754361 |
| 2.3.1.297 | more |
Lass4 overproduction causing increases in both middle- and long-chain ceramides |
752700 |
| 2.3.1.297 | more |
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview |
754361 |
| 2.3.1.297 | more |
topology study of Lag1p and Lac1p using insertion of glycosylation sites and fXa (factor Xa)-cleavage sites in the loops between the predicted transmembrane segments, hydropathy profiles of Lag1p and Lac1p and positions of fusion insertions, method, overview |
-, 752702 |
