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Titolo:
N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: effects of mammalian galactosyltransferase
Autore:
Ailor, E; Takahashi, N; Tsukamoto, Y; Masuda, K; Rahman, BA; Jarvis, DL; Lee, YC; Betenbaugh, MJ;
Indirizzi:
Johns Hopkins Univ, Dept Chem Engn, Baltimore, MD 21218 USA Johns Hopkins Univ Baltimore MD USA 21218 m Engn, Baltimore, MD 21218 USA Nakano Vinegar Co Ltd, GlycoLab, Cent Res Lab, Handa City, Aichi 4758585, Japan Nakano Vinegar Co Ltd Handa City Aichi Japan 4758585 Aichi 4758585, Japan Suntory Inst Bioorgan Res, Shimamoto, Osaka 618, Japan Suntory Inst Bioorgan Res Shimamoto Osaka Japan 618 oto, Osaka 618, Japan Univ Wyoming, Dept Microbiol, Laramie, WY 82071 USA Univ Wyoming Laramie WY USA 82071 , Dept Microbiol, Laramie, WY 82071 USA Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA Johns Hopkins UnivBaltimore MD USA 21218 t Biol, Baltimore, MD 21218 USA
Titolo Testata:
GLYCOBIOLOGY
fascicolo: 8, volume: 10, anno: 2000,
pagine: 837 - 847
SICI:
0959-6658(200008)10:8<837:NPOHTP>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
ASPARAGINE-LINKED OLIGOSACCHARIDES; BACULOVIRUS EXPRESSION VECTORS; SPODOPTERA-FRUGIPERDA CELLS; 2-DIMENSIONAL SUGAR MAP; HUMAN-SERUM TRANSFERRIN; HUMAN SEROTRANSFERRIN; MEMBRANE-GLYCOPROTEINS; GLYCOSYLATION PATHWAY; PREFERENTIAL TRANSFER; BRANCH SPECIFICITY;
Keywords:
baculovirus; glycosylation; glycosyltransferase; oligosaccharide; expression;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Betenbaugh, MJ Johns Hopkins Univ, Dept Chem Engn, Baltimore, MD 21218 USAJohns Hopkins Univ Baltimore MD USA 21218 re, MD 21218 USA
Citazione:
E. Ailor et al., "N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: effects of mammalian galactosyltransferase", GLYCOBIOLOG, 10(8), 2000, pp. 837-847

Abstract

The N-glycans of human serum transferrin produced in Trichopulsia ni cellswere analyzed to examine N-linked oligosaccharide processing in insect cells. Metabolic radiolabeling of the intra- and extracellular protein fractions revealed the presence of multiple transferrin glycoforms with molecular weights lower than that observed for native human transferrin, Consequently, the N-glycan structures of transferrin in the culture medium were determined using three-dimensional high performance liquid chromatography. The attached oligosaccharides included high mannose, paucimannosidic, and hybrid structures with over 50% of these structures containing one fucose, alpha(1,6)-, or two fucoses, alpha(1,6)- and alpha(1,3)-, linked to the Asn-linked N-acetylglucosamine. Neither sialic acid nor galactose was detected on any of the N-glycans, However, when transferrin was coexpressed with beta(1,4)-galactosyltransferase three additional galartose-containing hybrid oligosaccharides were obtained. The galactose attachments were exclusive to the alpha(1,3)-mannose branch and the structures varied by the presence of zero, one, or two attached fucose residues. Furthermore, the presence of the galactosyltransferase appeared to reduce the number of paucimannosidic structures, which suggests that galactose attachment inhibits the ability of hexosaminidase activity to remove the terminal N-acetylglucosamine The ability to promote galactosylation and reduce paucimannosidic N-glycans suggests that the oligosaccharide processing pathway in insect cells mag be manipulated to mimic more closely that of mammalian cells.

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Documento generato il 30/11/20 alle ore 11:20:12