2010
DOI: 10.1074/jbc.m109.058370
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Functional Interaction of Common Allergens and a C-type Lectin Receptor, Dendritic Cell-specific ICAM3-grabbing Non-integrin (DC-SIGN), on Human Dendritic Cells

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Cited by 87 publications
(73 citation statements)
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“…DC-SIGN shares 77% amino acid sequence identity, similar overall structure and ligand-binding characteristics with the human receptor, DC-SIGNR (L-SIGN; CD299). Ara h 1, Der p 1, Der p 2, Can f 1 and Cyn d 1 (Bermuda grass pollen) have been reported as ligands for DC-SIGN and/or DC-SIGNR [41,42]. DC-SIGN has been suggested to modulate human DC activation for Th1 cell polarization, or IL-10-mediated regulatory responses [40,43,44].…”
Section: C-type Lectinsmentioning
confidence: 99%
“…DC-SIGN shares 77% amino acid sequence identity, similar overall structure and ligand-binding characteristics with the human receptor, DC-SIGNR (L-SIGN; CD299). Ara h 1, Der p 1, Der p 2, Can f 1 and Cyn d 1 (Bermuda grass pollen) have been reported as ligands for DC-SIGN and/or DC-SIGNR [41,42]. DC-SIGN has been suggested to modulate human DC activation for Th1 cell polarization, or IL-10-mediated regulatory responses [40,43,44].…”
Section: C-type Lectinsmentioning
confidence: 99%
“…Lately, natural Der p 2 was shown to elicit the production of TNF-α through direct binding with DC-SIGN on DCs, whereas the unglycosylated recombinant form was ineffective in receptor activation [63]. Recombinant Der p 2 caused nuclear factor ĸB-dependent upregulation of pro-inflammatory cytokines in bronchial (BEAS-2B and NHBE) but not alveolar (A549) airway epithelial cells [64], whereas recombinant Der f 2 can directly stimulate IL-13 production in BEAS-2B cells [65].…”
Section: Biological Activity Of Purified Hdm Allergens and Airway Innmentioning
confidence: 99%
“…It is difficult to avoid peanut due to many factors, including cross-contamination during food processing. What makes peanut such a potent allergen is not understood, although in human in vitro systems it was described that Ara h 1 from peanut could bind to DC-specific ICAM3-grabbing nonintegrin (DC-SIGN) in a glycosylation-dependent manner, resulting in a modified DC phenotype and increased capacity for Th2 skewing (3,4). Innate recognition of allergens has been described for other clinically relevant allergens, including dust mite allergens that activate epithelial cells and DCs through TLR4 and dectin-1 (5,6).…”
Section: Introductionmentioning
confidence: 99%