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Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure

Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure
Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure

The monoglucosylated oligomannose N-linked oligosaccharide (Glc 1Man9GlcNAc2) 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.

Calnexin, Calreticulin, Complement component C3, Glycosylation, Monoglucosylation
0014-5793
270-274
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Ritchie, Gayle E.
8768dda8-a8ca-4fe8-a30f-76e1e53580dc
Critchley, Alison J.
9a4b18bc-223e-405a-8226-f218404e9961
Morgan, B. Paul
56398ab3-c1e1-4757-8b12-c5c223257055
Wilson, Ian A.
7865d500-d638-4a67-ad6d-fefad0ae83bb
Dwek, Raymond A.
d8d9d5f8-f2c0-414e-b6b0-df77a33f0da4
Sim, Robert B.
d48628cc-2ae8-4a8c-949a-4d5c35a514ec
Rudd, Pauline M.
4bbd1e70-98ae-4c28-84e6-c6a18d98e7ee
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Ritchie, Gayle E.
8768dda8-a8ca-4fe8-a30f-76e1e53580dc
Critchley, Alison J.
9a4b18bc-223e-405a-8226-f218404e9961
Morgan, B. Paul
56398ab3-c1e1-4757-8b12-c5c223257055
Wilson, Ian A.
7865d500-d638-4a67-ad6d-fefad0ae83bb
Dwek, Raymond A.
d8d9d5f8-f2c0-414e-b6b0-df77a33f0da4
Sim, Robert B.
d48628cc-2ae8-4a8c-949a-4d5c35a514ec
Rudd, Pauline M.
4bbd1e70-98ae-4c28-84e6-c6a18d98e7ee

Crispin, Max, Ritchie, Gayle E., Critchley, Alison J., Morgan, B. Paul, Wilson, Ian A., Dwek, Raymond A., Sim, Robert B. and Rudd, Pauline M. (2004) Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure. FEBS Letters, 566 (1-3), 270-274. (doi:10.1016/j.febslet.2004.04.045).

Record type: Article

Abstract

The monoglucosylated oligomannose N-linked oligosaccharide (Glc 1Man9GlcNAc2) 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.

Full text not available from this repository.

More information

Published date: 21 May 2004
Keywords: Calnexin, Calreticulin, Complement component C3, Glycosylation, Monoglucosylation

Identifiers

Local EPrints ID: 414573
URI: https://eprints.soton.ac.uk/id/eprint/414573
ISSN: 0014-5793
PURE UUID: d7dd8703-c8b0-4697-b3dc-bb5e02b49ff8
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 04 Oct 2017 16:30
Last modified: 14 Mar 2019 01:25

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