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O-linked oligosaccharide on the 75-kDa neurotrophin receptor.
Chapman, B S; Eckart, M R; Kaufman, S E; Lapointe, G R.
Afiliação
  • Chapman BS; Department of Pharmaceutical Chemistry, University of California School of Pharmacy, San Francisco, USA.
J Neurochem ; 66(4): 1707-16, 1996 Apr.
Article em En | MEDLINE | ID: mdl-8627329
Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR). An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix. This peptide, the transmembrane helix, and intracellular sequences are highly conserved in vertebrate evolution. To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells. Addition during biosynthesis of O-linked glycans was evaluated, and structures were characterized by lectin blotting and glycosidase digestion. Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured. Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels. NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc. Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor. The results are discussed in reference to a potential role for the stalk region in ligand binding and signaling.
Assuntos
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Base de dados: MEDLINE Assunto principal: Oligossacarídeos / Receptores de Fator de Crescimento Neural Limite: Animals / Humans Idioma: En Ano de publicação: 1996 Tipo de documento: Article
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Base de dados: MEDLINE Assunto principal: Oligossacarídeos / Receptores de Fator de Crescimento Neural Limite: Animals / Humans Idioma: En Ano de publicação: 1996 Tipo de documento: Article