Shusaku Yanagidani

TL;DR: Northern blotting analyses of rat adult tissues showed that α1-6FucT was highly expressed in brain, and no sequence homology was found with other previously cloned fucosyl transferases, but the enzyme appears to be a type II transmembrane protein like the other glycosyltransferases.

TL;DR: No putative N-glycosylation sites were found in the predicted amino acid sequence of the human MKN45 cell enzyme or that of porcine brain, thus, the enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha 1-3, andalpha1-4 fucose addition.

TL;DR: It is suggested that the enhancement of α1‐6 FucT expression increased the fucosylation of several proteins, including AFP, and that the level of α 1‐6–fucosyated AFP in patients with HCC was in part caused by up‐regulation of the α1 •fucT gene expression.

TL;DR: In this paper, the α-1-6 fucosyltransferase with a human or swine origin was described, which transferred fucose from guanosine diphosphate to the hydroxyl group at the 6 position of GluNAc closest to R in the receptor.

TL;DR: 5'-Untranslated sequences found in ESTs and the cDNA for the FUT8 suggest the presence of an additional exon(s) at the upstream of the first exon identified in this study, and therefore, the transcription of the gene would be regulated by multiple promoters.