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РЖ ВИНИТИ 34 (BI39) 97.01-04К1.72

IgM polymerization inhibits the Golgi-mediated processing of the 'мю'-chain carboxy-terminal glycans [Text] / Marie-Madeleine Cals [et al.] // Mol. Immunol. - 1996. - Vol. 33, N 1. - P15-24 . - ISSN 0161-5890
Перевод заглавия: Полимеризация IgM подавляет обусловленной системой Гольджи процессинг гликанов с концевой 'мю'-цепью
Аннотация: Secreted glycoproteins generally contain oligosaccharides of the complex type. However, several molecules have been described in which individual glycans are processed differently from one another. Folding, assembly and oligomerization could affect the maturation of certain glycans by hindering them to the Golgi processing machinery. Were tested this possibility by analysing a panel of engineered murine 'мю' chains secreted as 'мю'2L2 monomers or as polymers, and having or not the carboxy-terminal glycan (Asn563). In secreted IgM polymers, Asn563 bears high-mannose oligosaccharides, while complex sugars are found at the other four sites. Polymeric and monomeric IgM contain 'мю' chains whose glycans are processed differently. This is mainly due to the differential processing at the Asn563 glycan, which undergoes Golgimediated processing when IgM are secreted in the monomeric form. These results indicate that the oligomerization-dependent accessibility to the sugar modifying enzymes can be one of the key features that dictate the extent of oligosaccharide processing in multimeric glycoproteins. The presence of high mannose glycans at Asn563 implies that IgM polymerization takes place before encountering mannosidase II, likely in a pre-Golgi compartment. Италия, Molec. Immunol., DIBIT-HSR, Milano. Библ. 46

ГРНТИ	34.43.33

ВИНИТИ 341.43.33.05
Рубрики: ИММУНОГЛОБУЛИН M
ПОЛИМЕРИЗАЦИЯ
ПОДАВЛЕНИЕ РАСЩЕПЛЕНИЯ ГЛИКАНОВ
СИСТЕМА ГОЛЬДЖИ
МЫШИ

Доп.точки доступа:
Cals, Marie-Madeleine; Guenzi, Silvia; Carelli, Stephana; Simmen, Thomas; Sparvoli, Antonella; Sitia, Roberto

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