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Titolo:
A remodeling system of the 3 '-sulfo-Lewis a and 3 '-sulfo-Lewis x epitopes
Autore:
Ikeda, N; Eguchi, H; Nishihara, S; Narimatsu, H; Kannagi, R; Irimura, T; Ohta, M; Matsuda, H; Taniguchi, N; Honke, K;
Indirizzi:
Osaka Univ, Sch Med, Dept Biochem, Osaka 5650871, Japan Osaka Univ OsakaJapan 5650871 h Med, Dept Biochem, Osaka 5650871, Japan Osaka Univ, Sch Med, Dept Surg, Osaka 5650871, Japan Osaka Univ Osaka Japan 5650871 Sch Med, Dept Surg, Osaka 5650871, Japan Soka Univ, Inst Life Sci, Div Cell Biol, Tokyo 1928577, Japan Soka Univ Tokyo Japan 1928577 e Sci, Div Cell Biol, Tokyo 1928577, Japan Natl Inst Adv Ind Sci & Technol, Inst Mol & Cell Biol, Tsukuba, Ibaraki 3058568, Japan Natl Inst Adv Ind Sci & Technol Tsukuba Ibaraki Japan 30585688568, Japan Aichi Canc Ctr, Program Expt Pathol, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr Nagoya Aichi Japan 4648681 l, Nagoya, Aichi 4648681, Japan Univ Tokyo, Grad Sch Pharmaceut Sci, Lab Canc Biol & Mol Immunol, Bunkyo Ku, Tokyo 1130033, Japan Univ Tokyo Tokyo Japan 1130033 Immunol, Bunkyo Ku, Tokyo 1130033, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 42, volume: 276, anno: 2001,
pagine: 38588 - 38594
SICI:
0021-9258(20011019)276:42<38588:ARSOT3>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ADHESION MOLECULE; SIALYL-LEWIS-X; LINKED OLIGOSACCHARIDES; L-SELECTIN; SULFATED OLIGOSACCHARIDES; CARBOHYDRATE CHAINS; MAST-CELLS; FUC-TIX; EXPRESSION; CANCER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Honke, K Osaka Univ, Sch Med, Dept Biochem, Room B1,2-2 Yamadaoka, Osaka 5650871, Japan Osaka Univ Room B1,2-2 Yamadaoka Osaka Japan 5650871 0871, Japan
Citazione:
N. Ikeda et al., "A remodeling system of the 3 '-sulfo-Lewis a and 3 '-sulfo-Lewis x epitopes", J BIOL CHEM, 276(42), 2001, pp. 38588-38594

Abstract

It has been reported that the chemically synthesized 3'-sulfo-Le(a) and 3'-sulfo-Le(x) epitopes have a high potential as a ligand for selectins. To elucidate the physiological functions of 3'-sulfated Lewis epitopes, a remodeling system was developed using a combination of a beta Ga1-3-O-sulfotransferase GP3ST, hitherto known alpha1,3/1,4-fucosyltransferases (FucT-III, IV, V, VI, VII, and IX) and arylsulfatase A. The pyridylaminated (PA) lacto-N-tetraose (Gal beta1-3GlcNAc beta1-3Gal beta1-4Glc) was first converted to 3'-sulfolacto-N-fucopentaose II (sulfo-3Gal beta1-3(Fuc alpha1-4)GlcNAc beta1-3Gal beta1-4Glc)-PA by sequential reactions with GP3ST and FucT-III. The3'-sulfolacto-N-fucopentaose III (sulfo-3Gal beta1-4(Fuc alpha1-3)GlcNAc beta1-3Gal beta1-4Glc)-PA was then synthesized from lacto-N-neotetraose (Galbeta1-4GlcNAc beta1-3Gal beta1-4Glc)-PA by GP3ST and FucT-III, -IV, -V, -VI, -VII, or -IX in a similar manner. The substrate specificity for the 3'-sulfated acceptor of the alpha1,3-fucosyltransferases was considerably different from that for the non-substituted and 3'-sialylated varieties. When the GP3ST gene was introduced into A549 and Chinese hamster ovary cells expressing FucT-III, they began to express 3'-sulfo-Lea and 3'-sulfo-Le(x) epitopes, respectively, suggesting that GP3ST is responsible for their biosynthesis in vivo. The expression of the 3'-sialyl-Le(x) epitope on Chinese hamster ovary cells was attenuated by the introduction of GP3ST gene, indicatingthat GP3ST and alpha2,3-sialyltransferase compete for the common Gal beta1-4GlcNAc-R oligosaccharides. Last, arylsulfatase A, which is a lysosomal hydrolase that catalyzes the desulfation of 3-O-sulfogalactosyl residues in glycolipids, was found to hydrolyze the sulfate ester bond on the 3'-sulfo-Le(x) (type 2 chain) but not that on the 3'-sulfo-Le(a) (type 1 chain). The present remodeling system might be of potential use as a tool for the studyof the physiological roles of 3'-sulfated Lewis epitopes, including interaction with selectins.

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Documento generato il 10/07/20 alle ore 08:07:57