Disease relevance of ST6GAL1

• Partial characterization of microsomal sialyltransferase from chicken liver and hepatoma Mc-29: I. Effect of nucleotides and metal ions [1].
• By using influenza virus neuraminidase an attempt was made for partial structural characterization of the sialylation sites in asialofetuin applied as exogenous acceptor for sialyltransferase determination [2].

High impact information on ST6GAL1

• These results clearly show that the expressed enzyme is a novel type of sialyltransferase that requires beta-galactoside residues linked to GalNAc residues, whereas sialic acid residues linked to galactose residues are not essential for the activity [3].
• By incubation of erythrocytes with sialyltransferase and the CMP-activated analogues, the cell surface was modified to contain sialic acid with one of the following C-9 substituents: an azido, an amino, an acetamido, or a hexanoylamido group [4].
• Chondroitin polymerization and sulfation had a dual distribution similar to the galactosyl ovalbumin transferase and sialyltransferase in separate later and lighter medial and trans compartments, or in an extended medial or trans compartment [5].
• Membranes from chick embryo epiphyseal cartilage were fractionated by equilibrium sucrose density gradient centrifugation and assayed for galactosyl xylose transferase, chondroitin polymerization and sulfation as well as the marker enzymes glucose-6-phosphatase, NADH cytochrome c reductase, galactosyl ovalbumin transferase, and sialyltransferase [5].
• Sialic acid incorporated into adult rat brain membranes was resistant to endoneuraminidase, indicating that the poly-alpha-2,8-sialosyl sialyltransferase activity is restricted to an early developmental epoch [6].

Chemical compound and disease context of ST6GAL1

• Microsomal sialyltransferase was assayed in chicken liver and hepatoma Mc-29 utilizing liver and hepatoma microsomal glycoprotein fractions, treated with Triton X-100, as exogenous acceptors [7].

Biological context of ST6GAL1

• DNA clones encoding beta-galactoside alpha 2,6-sialyltransferase have been isolated from chick embryonic cDNA libraries using sequence information obtained from the conserved amino acid sequence of the previously cloned enzymes [8].
• CMP-NeuNAc:poly-alpha-2,8-sialosyl sialyltransferase and the biosynthesis of polysialosyl units in neural cell adhesion molecules [6].

Anatomical context of ST6GAL1

• Molecular cloning and expression of chick embryo Gal beta 1,4GlcNAc alpha 2,6-sialyltransferase. Comparison with the mammalian enzyme [8].
• An alpha 2----3 glycolipid galactosyl sialyltransferase (SAT3/4) has been partially purified from embryonic chicken skeletal muscle [9].
• Microsomal sialyltransferase from hepatoma Mc-29 has typical forms with pI = 5.69, 7.43, 8.05 and 8.56, while in plasma membrane, enzymes with pI = 5.00 and 8.70 occur [10].

Associations of ST6GAL1 with chemical compounds

• Comparative rates of transfer of N-acetylneuraminic acid to acceptors bearing one or more Gal(beta 1-4)GlcNAc terminus by the Gal(beta 1-4)GlcNAc(NeuAc-Gal) (alpha 2-6)-sialyltransferase from embryonic chicken liver. Utilization of oligosaccharides as acceptors in sialyltransferase assays [11].
• Characterization of the product of the sialyltransferase catalysis was accomplished by separation and permethylation of double-labelled ([14C]NeuAc, [3H]Gal) oligosaccharides following their release from the glycoprotein fetuin by hydrazinolysis [12].
• Kinetic parameters of a beta-D-galactoside alpha 2 leads to 6 sialyltransferase from embryonic chicken liver [12].
• A sharp decrease of activities of the glycolipid sialyltransferases: SAT-2 (CMP-NeuAc; GD3 alpha2-8 sialyltransferase) and SAT-4 (CMP-NeuAc: GM1a alpha2-3 sialyltransferase) was observed in the apoptotic carcinoma cells treated with L-PPMP compared with cis-platin [13].
• Biosynthesis of GM1b and similar neolactoseries gangliosides by a partially purified chicken skeletal muscle sialyltransferase. Effect of sphingomyelin and acetylcholine [9].

Analytical, diagnostic and therapeutic context of ST6GAL1

• By preparative isoelectric focusing the multiple forms of sialyltransferase from both kind of serums was studied as well [2].
• Smooth membrane preparations of 13-day embryonic chicken livers, characterized by electron microscopy and marker enzyme analyses, have been found to contain sialyltransferase activity which displayed precise acceptor specificity [14].

References