Molecular cloning of cDNAs encoding dog high-affinity IgE receptor α, β, and γ chains

Goitsuka, Ryo; Hayashi, Nariyuki; Nagase, Masayuki; Sasaki, Nobuo; Ra, Chisei; Tsujimoto, Hajime; Hasegawa, Atsuhiko

doi:10.1007/s002510050541

Cited by 10 publications

(6 citation statements)

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“…Despite the necessity of their assemby for full function, expression pro¢les of these three genes are not always identical. Mast cells and basophils express all three genes, rendering them capable of expressing fully functional FceRI on their cell surface in humans and mice (Ravetch and Kinet, 1991;Ra et al, 1989) and also in canines (Goitsuka et al, 1999). By contrast, epidermal LC and other DC subsets, even other APC, express just two genes out of the three, missing expression of b chain (Maurer et al, 1994(Maurer et al, , 1996Jurgens et al, 1995).…”

Section: Resultsmentioning

confidence: 91%

Canine Epidermal Langerhans Cells Express α and γ but not β Chains of High-Affinity IgE Receptor

et al. 2005

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Epidermal Langerhans cells (LC) express a high-affinity receptor for IgE (FcepsilonRI), consisting of two chains (alpha and gamma chains) in humans that allows LC to perform Fc receptor-mediated uptake of allergens. We found that canine LC express alpha and gamma chains but not beta chain of FcepsilonRI, identical to human but not to mouse LC, which do not express functional FcepsilonRI (only gamma chain is expressed). This finding indicates that canine LC have FcepsilonRI-mediated function similar to or identical to human LC, raising the possibility that canine species provides a better model than mouse to understand the pathogenesis of human atopic dermatitis and investigate the therapeutic effect of drugs.

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Section: Resultsmentioning

confidence: 91%

Canine Epidermal Langerhans Cells Express α and γ but not β Chains of High-Affinity IgE Receptor

et al. 2005

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“…The α chains are type I membrane proteins and contain the Fc binding sites in their extracellular (N‐terminal) region, whereas the β and γ chains exert mainly cytoplasmic functions and act in cell signalling [7]. Among genetic variations of the FcɛRI gene, the β chain shows considerable variation, although the α and γ chains are highly conserved among species [8]. Previous linkage studies have suggested that atopy, AHR, or both are linked to the β chain of the high‐affinity IgE receptor (FcɛR1‐β) on chromosome 11q13 [9–11].…”

Section: Introductionmentioning

confidence: 99%

Association and functional relevance of E237G, a polymorphism of the high‐affinity immunoglobulin E‐receptor β chain gene, to airway hyper‐responsiveness

Yk¹,

Hw²,

Yang³

et al. 2007

Clin Experimental Allergy

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“…On the other hand, the amino acid sequence homology between canine and human FcεRIα is 54% [21], which explains the failure to detect the binding of FITC-labeled human IgE to canine FcεRI on CM-MC with flow cytometry (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Canine Mast Cell Activation via Human IgG1 and IgG4

Sato

Teshima

Nakamura

et al. 2004

Int Arch Allergy Immunol

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Background: We have reported that canine mastocytoma-derived CM-MC cells are activated via canine IgG and express a high-affinity IgG receptor (canine FcγRI). The predicted amino acid sequence of the canine FcγRI α subunit was found to be 72% similar to that of humans. These results suggest that canine FcγRI have binding activity with human IgG and led us to investigate CM-MC activation via canine FcγRI and human IgG. Methods: The binding of human IgG to canine FcγRI was examined by flow cytometry using FITC-conjugated human IgG. [Ca²⁺]i increase or histamine release via canine FcγRI and the four human IgG subclasses was measured following aggregation of IgG-bound FcγRIs by anti-human IgG. To determine the binding activity of canine FcγRI with human IgG1 or IgG3, the displacement of ¹²⁵I-labeled canine IgG from canine FcγRI was examined by unlabeled human IgG1 or IgG3. Results: The fluorescence intensity of CM-MC cells was markedly (about 50 times) elevated by incubation with FITC-human IgG compared with the fluorescence of the control cells. A significant (p < 0.01) calcium response and histamine release were observed following aggregation of canine FcγRIs bound with human IgG1 or IgG4. ¹²⁵I-labeled canine IgG was displaced from canine FcγRI by preincubation with unlabeled total human IgG or human IgG1 dose-dependently, whereas no displacement was detected by preincubation with human IgG3. Conclusions: Canine FcγRI possesses a significant binding activity with human IgG1 or IgG4, while IgG2 or IgG3 did not significantly react with canine FcγRI on CM-MC cells.

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Molecular cloning of cDNAs encoding dog high-affinity IgE receptor α, β, and γ chains

Cited by 10 publications

References 4 publications

Canine Epidermal Langerhans Cells Express α and γ but not β Chains of High-Affinity IgE Receptor

Canine Epidermal Langerhans Cells Express α and γ but not β Chains of High-Affinity IgE Receptor

Association and functional relevance of E237G, a polymorphism of the high‐affinity immunoglobulin E‐receptor β chain gene, to airway hyper‐responsiveness

Canine Mast Cell Activation via Human IgG1 and IgG4

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