| First Author | Tokuda N | Year | 2013 |
| Journal | Glycobiology | Volume | 23 |
| Issue | 10 | Pages | 1175-83 |
| PubMed ID | 23882130 | Mgi Jnum | J:260410 |
| Mgi Id | MGI:6150528 | Doi | 10.1093/glycob/cwt054 |
| Citation | Tokuda N, et al. (2013) beta4GalT6 is involved in the synthesis of lactosylceramide with less intensity than beta4GalT5. Glycobiology 23(10):1175-83 |
| abstractText | Glycosphingolipids are expressed on the cell membrane and act as important factors in various events that occur across the plasma membrane. Lactosylceramide (LacCer) is synthesized from glucosylceramide and is a common precursor of various glycosphingolipids existing in whole body. Based on the enzyme purification, beta1,4-galactosyltransferase 6 (B4galt6) cDNA was isolated as a LacCer synthase-coding gene in the rat brain. We generated B4galt6 gene knockout (KO) mice and analyzed their phenotypes to examine roles of beta4GalT6. B4galt6 KO mice were born and grew up apparently normal. LacCer synthase activity and the composition of acidic glycosphingolipids in the brain were almost equivalent or minimally different between wild-type and KO mice. Studies by mouse embryonic fibroblasts (MEFs) revealed that the silencing of B4galt5 gene resulted in the marked reduction in LacCer synthase activity and this reduction was more severe in MEFs derived from B4galt6 KO mice than those from wild-type mice. These results suggested that beta4GalT6 plays a role as a LacCer synthase, whereas beta4GalT5 acts as a main enzyme for LacCer biosynthesis in these tissues and cells. |
