Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure |
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Authors: | Crispin M D Max Ritchie Gayle E Critchley Alison J Morgan B Paul Wilson Ian A Dwek Raymond A Sim Robert B Rudd Pauline M |
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Affiliation: | Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. |
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Abstract: | The monoglucosylated oligomannose N-linked oligosaccharide (Glc(1)Man(9)GlcNAc(2)) is a retention signal for the calnexin-calreticulin quality control pathway in the endoplasmic reticulum. We report here the presence of such monoglucosylated N-glycans on the human complement serum glycoprotein C3. This finding represents the first report of monoglucosylated glycans on a human serum glycoprotein from non-diseased individuals. The presence of the glucose moiety in 5% of the human C3 glycoprotein suggests that this glycosylation site is sequestered within the protein and is consistent with previous studies identifying a cryptic conglutinin binding site on C3 that becomes exposed upon its conversion to iC3b. |
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