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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2002-2-11
pubmed:abstractText
We investigated the ability of a baculovirus-insect cell system to produce sialylated glycoproteins. Despite the presence of enzymes for synthesizing complex-type N-glycans, the most frequent structure of insect N-glycan is the paucimannosidic type, Man(3)GlcNAc(2)(+/-Fuc). The reason for the overwhelming assembly of paucimannosidic N-glycans is not yet well understood. We hypothesized that this predominance might be due to insect-specific, Golgi-associated beta-N-acetylglucosaminidase (GlcNAcase)-mediated removal of N-acetylglucosamine residues from the precursor N-glycan, thereby preventing its galactosylation and terminal sialylation. As we expected, the suppression of intrinsic GlcNAcase activity with a specific inhibitor, 2-acetamido-1,2-dideoxynojirimycin, allowed the accumulation of sialylated glycoproteins in the supernatants of insect cell cultures after baculoviral infection. Our observation indicates that GlcNAcase-dependent depletion of N-acetylglucosamine residues from intermediate N-glycans is critical for the assembly of paucimannosidic N-glycans in insect cells and, more importantly, that insect cells (under specific conditions) retain the ability to construct sialylated N-glycans like those in mammalian cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5090-3
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11741890-Acetylglucosaminidase, pubmed-meshheading:11741890-Animals, pubmed-meshheading:11741890-Baculoviridae, pubmed-meshheading:11741890-Binding Sites, pubmed-meshheading:11741890-Blotting, Western, pubmed-meshheading:11741890-Cattle, pubmed-meshheading:11741890-Cell Line, pubmed-meshheading:11741890-DNA, Complementary, pubmed-meshheading:11741890-Enzyme Inhibitors, pubmed-meshheading:11741890-Glycoproteins, pubmed-meshheading:11741890-Golgi Apparatus, pubmed-meshheading:11741890-Insects, pubmed-meshheading:11741890-Lectins, pubmed-meshheading:11741890-Mice, pubmed-meshheading:11741890-Models, Chemical, pubmed-meshheading:11741890-N-Acetylneuraminic Acid, pubmed-meshheading:11741890-Polysaccharides, pubmed-meshheading:11741890-Protein Binding, pubmed-meshheading:11741890-RNA, Messenger, pubmed-meshheading:11741890-Recombinant Proteins
pubmed:year
2002
pubmed:articleTitle
Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under beta-N-acetylglucosaminidase inhibition.
pubmed:affiliation
Department of Immunology, National Institute of Animal Health, 3-1-5 Kannondai, Tsukuba, Ibaraki 305-0856, Japan. satochan@affrc.go.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't