Journal article
The chicken leukocyte receptor complex encodes a primordial, activating, high affinity IgY Fc receptor
Publication Details
Authors: | Viertlböck, B.; Schweinsberg, S.; Hanczaruk, M.; Schmitt, R.; Herberg, F.; Göbel, T. |
Publication year: | 2007 |
Pages range : | 11718-23 |
Volume number: | 104 |
ISSN: | 0027-8424 |
Abstract
Fc receptors are key players of the immune system that I ink the fine specificity of immunoglobulins and innate effector responses. Here, we describe a nonmammalian Fc gamma receptor, CHIR-AB1, a member of the leukocyte receptor complex, that binds IgY with high affinity with its single Ig domain. it is expressed on immature and mature B lymphocytes, monocytes, macrophages, and natural killer cells and harbors motifs of activating and inhibitory Fc receptors. In the absence of Fc epsilon Rl gamma, CHIR-AB1 can be expressed on B cells but cross-linking does not induce intracellular calcium release. In contrast, cells expressing CHIR-AB1 and Fc epsilon Rl gamma are triggered to release intracellular calcium upon stimulation with heat-aggregated IgY. CHIR-AB1 thus represents a primordial Fc receptor that combines features of different mammalian counterparts.
Fc receptors are key players of the immune system that I ink the fine specificity of immunoglobulins and innate effector responses. Here, we describe a nonmammalian Fc gamma receptor, CHIR-AB1, a member of the leukocyte receptor complex, that binds IgY with high affinity with its single Ig domain. it is expressed on immature and mature B lymphocytes, monocytes, macrophages, and natural killer cells and harbors motifs of activating and inhibitory Fc receptors. In the absence of Fc epsilon Rl gamma, CHIR-AB1 can be expressed on B cells but cross-linking does not induce intracellular calcium release. In contrast, cells expressing CHIR-AB1 and Fc epsilon Rl gamma are triggered to release intracellular calcium upon stimulation with heat-aggregated IgY. CHIR-AB1 thus represents a primordial Fc receptor that combines features of different mammalian counterparts.
