Carbohydrate-dependent biological activities of glycosylated human interferon-beta on human hepatoblastoma cells in vitro.
To evaluate the relationship between the sugar chain structure and biological activity, fibroblast-derived glycosylated human interferon-beta, Chinese hamster ovary cell-derived glycosylated recombinant human interferon-beta and Escherichia coli-derived unglycosylated recombinant human interferon-beta were evaluated using human hepatoblastoma cells in vitro. Native fibroblast interferon-beta expressed more cell-growth inhibitory action, 2'5'-oligoadenylate synthetase induction, and the inhibition of hepatitis B virus DNA replication than its asialoform and two recombinant interferon-betas. These results showed that the sugar chain structure of human interferon-beta affects its biological activity on human hepatoblastoma cells.
Utsumi
J
J
Basic Research Laboratories, Toray Industries, Inc., Kanagawa, Japan.
Matsuo-Ogawa
E
E
Nagahata
T
T
Kasama
K
K
Kagawa
Y
Y
Satoh
Y
Y
D015088:2',5'-Oligoadenylate Synthetase / Q000096:biosynthesis; D001681:Biological Assay; D002455:Cell Division / Q000187:drug effects; D004790:Enzyme Induction / Q000187:drug effects; D006023:Glycoproteins / Q000494:pharmacology*; D006031:Glycosylation; D006515:Hepatitis B virus / Q000254:growth & development; D018197:Hepatoblastoma; D006801:Humans; D016899:Interferon-beta / Q000494:pharmacology*; D008113:Liver Neoplasms; D011994:Recombinant Proteins / Q000494:pharmacology; D013329:Structure-Activity Relationship; D014407:Tumor Cells, Cultured; D014779:Virus Replication / Q000187:drug effects
D006023:Glycoproteins; D011994:Recombinant Proteins; D016899:Interferon-beta; D015088:2',5'-Oligoadenylate Synthetase