High impact information on ST8SIA6

• Substrate specificities and kinetic properties also showed that ST8Sia VI prefers O-glycans to glycolipids as acceptor substrates [1].
• The recombinant soluble form of ST8Sia VI expressed in COS-7 cells exhibited alpha2,8-sialyltransferase activity toward both glycolipids and glycoproteins that have the NeuAcalpha2,3(6)Gal sequence at the nonreducing end of their carbohydrate groups [1].
• A novel member of the mouse alpha2,8-sialyltransferase (ST8Sia) family, designated ST8Sia VI, was identified by BLAST analysis of expressed sequence tags [1].
• ST8Sia VI also exhibited activity toward oligosaccharides such as sialyllactose and sialyllactosamine, and the structure of the minimal acceptor substrate for ST8Sia VI was determined as the NeuAcalpha2,3(6)Gal sequence [1].
• Unlike T cells, B cells, and monocytes, NK cells consistently expressed mRNA encoding ST8Sia VI, which creates alpha2,8-linked disialic acids on O-linked glycans of glycoproteins [2].

Anatomical context of ST8SIA6

• We have established a mammary cell line (MDA-MB-231) stably transfected with the full-length hST8Sia VI and the analysis of sialylated carbohydrate structures expressed at the cell surface clearly indicated the disappearance of Neu5Acalpha2-3-sialylated structures [3].

Associations of ST8SIA6 with chemical compounds

• Detailed substrate specificity analysis of the hST8Sia VI recombinant enzyme in vitro, revealed that this enzyme required the trisaccharide Neu5Acalpha2-3Galbeta1-3GalNAc (where Neu5Ac is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) to generate diSia (disialic acid) motifs specifically on O-glycans [3].

Analytical, diagnostic and therapeutic context of ST8SIA6

• Molecular cloning and expression of a human hST8Sia VI (alpha2,8-sialyltransferase) responsible for the synthesis of the diSia motif on O-glycosylproteins [3].

References