Polylactosamine synthesis and branch formation of N-glycans in beta1,4-galactosyltransferase-1-deficient mice.

Kotani, Norihiro; Asano, Masahide; Inoue, Noboru; Iwakura, Yoichiro; Takasaki, Seiichi

Kotani, Norihiro; Asano, Masahide; Inoue, Noboru; Iwakura, Yoichiro; Takasaki, Seiichi.

Afiliación

Kotani N; Division of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.

Arch Biochem Biophys ; 426(2): 258-65, 2004 Jun 15.

Article en En | MEDLINE | ID: mdl-15158676

RESUMEN

Analysis of glycans from erythrocyte membrane glycoproteins from beta1,4-galactosyltransferase-1 (beta4GalT-1)-deficient mice revealed moderately decreased galactosylation but comparable polylactosamine content compared to control beta4GalT-1(+/-) mice. The increased expression of more branched N-glycans was observed in beta4GalT-1(-/-) mice, and its extent was more remarkable in elder beta4GalT-1(-/-) mice (28 weeks old) than in younger beta4GalT-1(-/-) mice (6-9 weeks old). In relation to this issue, the less galactosylation of biantennary glycans was observed in the elder group, suggesting that beta4GalTs actually compete with N-acetylglucosaminyltransferases IV and V in erythroid cells. In contrast, approximately 80% of core 2 O-glycans were not beta1,4-galactosylated regardless of age of the knockout mice. These results suggest that beta4GalT-1 expressed in erythroid cells may regulate a constant branch formation of N-glycans and plays a predominant role in beta1,4-galactosylation of core 2 O-glycan.

Asunto(s)

Amino Azúcares/biosíntesis; Amino Azúcares/química; Membrana Eritrocítica/química; Membrana Eritrocítica/metabolismo; Galactosiltransferasas/deficiencia; Polisacáridos/biosíntesis; Polisacáridos/química; Polisacáridos/metabolismo; Envejecimiento/fisiología; Animales; Glicoproteínas de Membrana/química; Glicoproteínas de Membrana/metabolismo; Ratones; Ratones Noqueados; Peso Molecular; Oligosacáridos de Cadena Ramificada/biosíntesis; Oligosacáridos de Cadena Ramificada/química; Conformación Proteica; Relación Estructura-Actividad

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Polisacáridos / Membrana Eritrocítica / Galactosiltransferasas / Amino Azúcares Límite: Animals Idioma: En Revista: Arch Biochem Biophys Año: 2004 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos

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