Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor.

Jouvin, Marie-Hélène; Adamczewski, Martin; Numerof, Robert P.; Letourneur, Odile; Vallé, Alain; Kinét, Jean-Pierre

doi:10.1016/s0021-9258(17)37549-x

Cited by 328 publications

(37 citation statements)

References 49 publications

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“…In contrast to the distinct aggregation of ␤and ␥-chains in cells stimulated with an optimal concentration of antigen (Figures 3C and 5C), only ␥-chains were aggregated on surfaces of cells stimulated with a suboptimal concentration of antigen, while ␤-chains remained dispersed (Figures 4C and 5B). These results are consistent with earlier studies on chimeric receptors (Letourneur and Klausner 1991;Jouvin et al 1994;Wilson et al 1995) and provide direct evidence at the intact cell level that the aggregation of ␥-chains alone can evoke a cellular response. Moreover, these results are also consistent with the current model on the role of ␤-chains as a signaling amplifier of the FcεRI system (Lin et al 1996).…”

Section: Discussionsupporting

confidence: 92%

“…However, topographical distribution of the signaling chains of Fc ε RI ␤ and ␥ at the electron microscopic level has not yet been investigated. Current biochemical evidence using chimeric receptor molecules indicates that the ␥ -chain aggregation alone can evoke cellular responses (Letourneur and Klausner 1991;Jouvin et al 1994;Wilson et al 1995), and the ␤ -chain amplifies the ␥ -chain-mediated signal (Lin et al 1996). Moreover, the results obtained with mice deficient in ␤ -or ␥ -chains of Fc ε RI have supported such important functions of these chains (Takai et al 1994;Dombrowicz et al 1998).…”

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confidence: 99%

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Distinct Aggregation of β- and γ-Chains of the High-affinity IgE Receptor on Cross-Linking

Asai

Fujimoto

Harazaki

et al. 2000

J Histochem Cytochem.

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S U M M A R YThe high-affinity IgE receptor (Fc ε RI) on mast cells and basophils consists of a ligand-binding ␣ -chain and two kinds of signaling chains, a ␤ -chain and disulfide-linked homodimeric ␥ -chains. Crosslinking by multivalent antigen results in the aggregation of the bound IgE/ ␣ -chain complexes at the cell surface, triggering cell activation, and subsequent internalization through coated pits. However, the precise topographical alterations of the signaling ␤ -and ␥ -chains during stimulation remain unclarified despite their importance in ligand binding/signaling coupling. Here we describe the dynamics of Fc ε RI subunit distribution in rat basophilic leukemia cells during stimulation as revealed by immunofluorescence and immunogold electron microscopy. Immunolocalization of ␤ -and ␥ -chains was homogeneously distributed on the cell surfaces before stimulation, while crosslinking with multivalent antigen, which elicited optimal degranulation, caused a distinct aggregation of these signaling chains on the cell membrane. Moreover, only ␥ -but not ␤ -chains were aggregated during the stimulation that evoked suboptimal secretion. These findings suggest that high-affinity IgE receptor ␤ -and ␥ -chains do not co-aggregate but for the most part form homogenous aggregates of ␤ -chains or ␥ -chains after crosslinking.

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Section: Discussionsupporting

confidence: 92%

mentioning

confidence: 99%

Distinct Aggregation of β- and γ-Chains of the High-affinity IgE Receptor on Cross-Linking

Asai

Fujimoto

Harazaki

et al. 2000

J Histochem Cytochem.

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“…This article must therefore be hereby marked "advertisement" in accordancewith 18 FceRI (10)(11)(12). A fraction of FceRI on RBL cells is associated with Lyn prior to activation, and additional Lyn is associated with the receptor after activation (13)(14)(15)). Syk appears not to be pre-associated with the receptor, but there is evidence that it associates with both the f3 and the ' Y subunits, primarily 'Y, following activation (13,14).…”

mentioning

confidence: 99%

Kinetics of Tyrosine Phosphorylation When IgE Dimers Bind to FC∊ Receptors on Rat Basophilic Leukemia Cells

Wofsy

Kent

Mao

et al. 1995

Journal of Biological Chemistry

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Previously, we demonstrated that aggregates of the high affinity receptor for IgE (Fc epsilon RI), formed by the binding of chemically cross-linked oligomers of IgE, continue to signal early and late cellular responses long after the formation of new aggregates is blocked. In the present work, we explore quantitatively the relationship between aggregation of the receptors and one of the earliest biochemical changes this initiates. We compare the time course of aggregate formation, inferred from studies of the binding of dimers of IgE, and the time course of phosphorylation of tyrosines on receptor subunits when the receptors are aggregated. A simple model does not fit the data. It appears that aggregates formed late in the response are less effective signaling units than those formed initially. We propose new explanations for the persistence of the response and the unusual kinetics.

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“…209 Recent studies have suggested that triggering of the IgE receptor activates Lyn (which is already associated with the b subunit), which # 1998 Blackwell Science Ltd, Veterinary Dermatology, 9, 145±166 phosphorylates both the b and g subunits. 217 This activates Syk which in turn phosphorylates and activates phospholipase C-g1, 217 an important enzyme in the generation of inositol triphosphate (see below). In this scheme, the b subunit is thought to act as an ampli®er of the signal generated by the g subunit.…”

Section: Tyrosine Kinasesmentioning

confidence: 99%

A review of mast cell biology

Hill

[]

1998

Veterinary Dermatology

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In recent years, the mast cell has been a focus of intense scientific study, predominantly because of its role as a key effector cell in immediate hypersensitivity reactions. Continuous research over the last 20 years has finally characterized the origin of mast cells, and determined many of the factors involved in mast cell differentiation and proliferation. In addition, different subpopulations of mast cell have been defined with distinct biochemical and functional characteristics. The mechanisms involved in stimulus–secretion coupling, the process by which mast cells release their inflammatory mediators, has received particular attention because these mechanisms may be future targets for anti‐allergic drugs. However, it is now recognized that mast cells play a much wider role than mediating allergic diseases. They are involved in non specific inflammatory reactions, fibrosis, angiogenesis and wound healing, and play an important role in protection of the host against gastrointestinal nematodes and certain bacterial infections. In this review, the advances made in determining the origins, heterogeneity and function of mast cells are described.

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Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor.

Cited by 328 publications

References 49 publications

Distinct Aggregation of β- and γ-Chains of the High-affinity IgE Receptor on Cross-Linking

Distinct Aggregation of β- and γ-Chains of the High-affinity IgE Receptor on Cross-Linking

Kinetics of Tyrosine Phosphorylation When IgE Dimers Bind to FC∊ Receptors on Rat Basophilic Leukemia Cells

A review of mast cell biology

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