RRC ID 33247
Author Kojima Y, Mizutani A, Okuzaki Y, Nishijima K, Kaneoka H, Sasamoto T, Miyake K, Iijima S.
Title Analyses of chicken sialyltransferases related to N-glycosylation.
Journal J Biosci Bioeng
Abstract Proteins exogenously expressed and deposited in the egg whites of transgenic chickens did not contain terminal sialic acid in their N-glycan. Since this sugar is important for the biological stability of therapeutic proteins, we examined chicken sialyltransferases (STs). Based on homologies in DNA sequences, we cloned and expressed several chicken STs, which appeared to be involved in N-glycosylation in mammals, in 293FT cells. Enzymatic activity was detected with ST3Gal3, ST3Gal6 and ST6Gal1 using galactose-β1,4-N-acetylglucosamine (Galβ1,4GlcNAc) as an acceptor. Using Golgi fractions from the cell-free extracts of chicken organs, α2,3- and/or α2,6-ST activities were detected in the liver and kidney, but were absent in the oviduct cells in which egg-white proteins were produced. This result suggested that the lack of ST activities in oviduct cells mainly caused the lack of sialic acid in the N-glycan of proteins exogenously expressed and deposited in egg white.
Volume 119(6)
Pages 623-8
Published 2015-6-1
DOI 10.1016/j.jbiosc.2014.11.009
PII S1389-1723(14)00448-4
PMID 25499752
MeSH Acetylglucosamine / analogs & derivatives Acetylglucosamine / metabolism Animals Cell Line Cell-Free System Chickens* / genetics Cloning, Molecular Egg White / chemistry Female Galactose / analogs & derivatives Galactose / metabolism Glycosylation* Golgi Apparatus / metabolism Humans Kidney / enzymology Liver / enzymology Organ Specificity Oviducts / cytology Oviducts / enzymology Sialic Acids / metabolism* Sialyltransferases / genetics Sialyltransferases / metabolism*
IF 2.366
Times Cited 3
Chicken / Quail