RRC ID 42715
Author Kato Y, Adachi Y, Ohno N.
Title Contribution of N-linked oligosaccharides to the expression and functions of beta-glucan receptor, Dectin-1.
Journal 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.
Volume 29(8)
Pages 1580-6
Published 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
Times Cited 26
WOS Category PHARMACOLOGY & PHARMACY
Resource
Human and Animal Cells RAW 264(RCB0535)