RRC ID |
42715
|
著者 |
Kato Y, Adachi Y, Ohno N.
|
タイトル |
Contribution of N-linked oligosaccharides to the expression and functions of beta-glucan receptor, Dectin-1.
|
ジャーナル |
Biol Pharm Bull
|
Abstract |
Dectin-1 is a C-type lectin receptor that recognizes fungal beta-glucan, and mediates the production of reactive oxygen species and inflammatory cytokines. Thus Dectin-1 is thought to be essential for anti-fungal immune responses. Murine Dectin-1 mRNA is alternatively spliced and generates two isoforms (isoform A and B). Human Dectin-1 mRNA is also alternatively spliced and its functional isoforms (isoform A and B) are structurally similar to each of the mouse isoforms. One of the major differences among the four murine and human isoforms is the position and number of N-linked glycosylation motifs. But the significance of the glycosylation to the recognition of beta-glucan is not known. In this paper, using various glycosylation consensus sequence mutants, we demonstrated that the N-linked glycosylation of Dectin-1 affects the cell surface expression of the molecule. The expression levels on the cell surface influence the ligand-binding and the collaboration with TLR2 in the activation of NF-kappaB. These results suggest that N-linked glycosylation on Dectin-1 is essential for the recognition of fungal beta-glucan and subsequent activation of NF-kappaB.
|
巻・号 |
29(8)
|
ページ |
1580-6
|
公開日 |
2006-8-1
|
DOI |
10.1248/bpb.29.1580
|
PII |
JST.JSTAGE/bpb/29.1580
|
PMID |
16880608
|
MeSH |
Amino Acid Sequence
Animals
Blotting, Western
Cell Line
Glycosylation
Humans
Lectins, C-Type
Membrane Proteins / chemistry
Membrane Proteins / genetics
Membrane Proteins / metabolism*
Mice
Molecular Sequence Data
NF-kappa B / metabolism
Nerve Tissue Proteins / chemistry
Nerve Tissue Proteins / genetics
Nerve Tissue Proteins / metabolism*
Oligosaccharides / metabolism*
RNA, Messenger / genetics
Sequence Homology, Amino Acid
|
IF |
1.863
|
引用数 |
26
|
WOS 分野
|
PHARMACOLOGY & PHARMACY
|
リソース情報 |
ヒト・動物細胞 |
RAW 264(RCB0535) |