EC Number   |
General Information |
Reference |
|---|
   2.3.1.297 | evolution |
Lass proteins are known to contain a TLC [TRAM/Lag1p/CLN8 (ceroid-lipofuscinoses, neuronal 8)] homology domain with the Lag1 motif. Lass family members Lass2, Lass4 and Lass5, but not Lass1, also contain a HOX (homeobox) domain |
752700 |
| 2.3.1.297 | malfunction |
about 50% of enzyme-null mice develop pheochromocytoma by about 13 months, and the rest shows signs of medullary hyperplasia |
756598 |
| 2.3.1.297 | malfunction |
ceramide synthase 2 null mice are more susceptible to dextran sodium sulfate-induced colitis, and their survival rate is markedly decreased compared with that of wild type littermates. In the colon of enzyme-deficient mice, the expression of junctional adhesion molecule-A is markedly decreased and the phosphorylation of myosin light chain 2 is increased. Enzyme deficiency influences intestinal barrier function and the severity of experimental colitis |
757295 |
| 2.3.1.297 | malfunction |
CerS2 null mouse show ceramide and downstream sphingolipids 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 C22-, C24:0-, and C24:1-sphingolipids are reduced by 10-100fold in the CerS2 null mouse, but no significant reduction is seen in C20-sphingolipids. Levels of C26:1- and C26:0-sphingolipids are relatively low in the wild-type, and only a small reduction is observed in the CerS2 null mouse. 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. Liver microsomal membranes from CerS2 null mice display higher membrane fluidity and show morphological changes. Expression of CerS5 is increased in the Cers2 mutants, and of CerS6 slightly. Mutant phenotype, overview |
754089 |
| 2.3.1.297 | malfunction |
CerS2-deficient (gene trap) mice exhibit myelin and behavioral abnormalities |
-, 736217 |
| 2.3.1.297 | malfunction |
disruption of the enzyme enhances plant sensitivity to dark submergence, but displays more resistance to submergence under light than wild type |
758106 |
| 2.3.1.297 | malfunction |
enzyme inhibition leads to altered root development and auxin transport |
757966 |
| 2.3.1.297 | malfunction |
enzyme-deficient mice show increased susceptibility to LCMV infection. Reduced levels of invariant natural killer T cells in the thymus of enzyme-null mice is due to their impaired maturation in the thymus |
756777 |
| 2.3.1.297 | malfunction |
in HeLa cells overproducing the fatty acid 2-hydroxylase FA2H, knockdown of CerS2 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 | malfunction |
inhibition of CerS is able to protect from cell death. Moreover, this protection occurs downstream or independently of mitochondrial permeabilization. Inhibition of CerS greatly inhibits plasma membrane permeabilization. Individual CerS knockdown does not significantly inhibit total ceramide accumulation. Knockdown of CerS2 in untreated cells reduces very long-chain Cer and increases long-chain Cer both in untreated and UV-C-treated cells. Inhibition of CerS but not de novo synthesis inhibits plasma membrane rupture that is not specific to UV-C irradiation or MCF-7 cells |
754096 |
