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Golgi linked protein glycosylation and associated diseases.
Ungar, Daniel.
Afiliação
  • Ungar D; University of York, Department of Biology (area 9), PO Box 373, York YO10 5YW, UK. du500@york.ac.uk
Semin Cell Dev Biol ; 20(7): 762-9, 2009 Sep.
Article em En | MEDLINE | ID: mdl-19508859
ABSTRACT
One of the Golgi's main functions is the glycosylation of secreted proteins. A large variety of glycan chains can be synthesized in the Golgi, and it is increasingly clear that these are critical in basic cellular functions as well as the development of multicellular organisms. The structurally best-documented glycans are N-glycans, yet these are also the most enigmatic in their function. In contrast, O-glycan function is far better understood, but here the structures and biosynthetic pathways are very incomplete. The critical importance of glycans is highlighted by the broad spectrum of diseases they are associated with, such as a number of inherited diseases, but also cancers or diabetes. The molecular clues to these, however, are only just being elucidated. Although some glycan structures are known to be involved in signaling or adhesion to the extracellular matrix, for most the functions are not yet known. This review aims at summarizing current knowledge as much as to point out critical areas key for future progress.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doença / Complexo de Golgi Tipo de estudo: Risk_factors_studies Limite: Animals / Humans Idioma: En Revista: Semin Cell Dev Biol Assunto da revista: EMBRIOLOGIA Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Reino Unido

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doença / Complexo de Golgi Tipo de estudo: Risk_factors_studies Limite: Animals / Humans Idioma: En Revista: Semin Cell Dev Biol Assunto da revista: EMBRIOLOGIA Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Reino Unido