A novel glycosyltransferase with a polyglutamine repeat; a new candidate for GD1α synthase (ST6GalNAc V)
- 7 December 1999
- journal article
- Published by Wiley
- Vol. 463 (1-2) , 92-96
- https://doi.org/10.1016/s0014-5793(99)01605-1
Abstract
The fifth type GalNAcα2,6-sialyltransferase (mST6GalNAc V) was cloned from a mouse brain cDNA library. mST6GalNAc V exhibited type II transmembrane topology containing a polyglutamine repeat, which showed 42.6% and 44.8% identity to mouse ST6GalNAc III and IV, respectively. Northern blot analysis revealed that the mST6GalNAc V gene was specifically expressed in forebrain and cerebellum. mST6GalNAc V exhibited GD1α synthetic activity from GM1b the same as mST6GalNAc III and IV. The activity ratio of GM1b toward fetuin and the expression pattern were completely different among the three ST6GalNAcs. Interestingly, the polyglutamine repeat number was different from that of inbred mice. We report the first glycosyltransferase with a polymorphic polyglutamine repeat.Keywords
This publication has 24 references indexed in Scilit:
- α1,3‐Fucoslytransferase IX (Fuc‐TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc‐TIXFEBS Letters, 1999
- Molecular Cloning and Functional Expression of Two Members of Mouse NeuAcα2,3Galβ1,3GalNAc GalNAcα2,6-Sialyltransferase Family, ST6GalNAc III and IVJournal of Biological Chemistry, 1999
- Molecular Cloning of a Novel α2,3-Sialyltransferase (ST3Gal VI) That Sialylates Type II Lactosamine Structures on Glycoproteins and GlycolipidsJournal of Biological Chemistry, 1999
- Expression Cloning of Mouse cDNA of CMP-NeuAc:Lactosylceramide α2,3-Sialyltransferase, an Enzyme That Initiates the Synthesis of GangliosidesJournal of Biological Chemistry, 1999
- Molecular Cloning and Functional Expression of a Fifth-Type α2,3-sialyltransferase (mST3Gal V: GM3 synthase)Biochemical and Biophysical Research Communications, 1998
- Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for α2,8‐sialyltransferase activity toward N‐linked oligosaccharidesFEBS Letters, 1995
- Biosynthetic pathway for a new series of gangliosides, GT1aα and GQ1bαFEBS Letters, 1994
- Expression of sialyl-Tn antigen is correlated with survival time of patients with gastric carcinomasEuropean Journal Of Cancer, 1993
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Prediction of protein conformationBiochemistry, 1974