mRNA Variants Encoding Multiple Forms of the High-Affinity IgE Receptor Alpha Subunit in Transformed and Nontransformed Mast Cells

1991 ◽  
Vol 96 (4) ◽  
pp. 289-295 ◽  
Author(s):  
Michael W. Robertson ◽  
Virginia S. Mehl ◽  
Mark L. Richards ◽  
Fu-Tong Liu
Keyword(s):  
Mast Cells ◽  
Alpha Subunit ◽  
Multiple Forms ◽  
Ige Receptor ◽  
Receptor Alpha ◽  
High Affinity ◽  
Mrna Variants ◽  
High Affinity Ige Receptor

scholarly journals Extracellular Signal-Regulated Kinases 1 and 2 Phosphorylate Gab2 To Promote a Negative-Feedback Loop That Attenuates Phosphoinositide 3-Kinase/Akt Signaling

2017 ◽  
Vol 37 (7) ◽  
Author(s):  
Xiaocui Zhang ◽  
Geneviève Lavoie ◽  
Antoine Méant ◽  
Léo Aubert ◽  
Marie Cargnello ◽  
...  
Keyword(s):  
Mast Cells ◽  
Negative Feedback ◽  
Feedback Loop ◽  
Akt Signaling ◽  
Negative Feedback Loop ◽  
Ige Receptor ◽  
High Affinity ◽  
Extracellular Signal ◽  
Phosphoinositide 3 Kinase ◽  
High Affinity Ige Receptor

ABSTRACT The scaffolding adapter protein Gab2 (Grb2-associated binder) promotes cell proliferation, survival, and motility by engaging several signaling pathways downstream of growth factor and cytokine receptors. In particular, Gab2 plays essential roles in mast cells, as it is required for phosphoinositide 3-kinase (PI3K) activation in response to Kit and the high-affinity IgE receptor. While the positive role of Gab2 in PI3K signaling is well documented, very little is known about the mechanisms that attenuate its function. Here we show that Gab2 becomes phosphorylated on multiple proline-directed sites upon stimulation of the Ras/extracellular signal-regulated kinase (ERK) signaling pathway. We demonstrate that ERK1 and ERK2 interact with Gab2 via a novel docking motif, which is required for subsequent Gab2 phosphorylation in response to ERK1/2 activation. We identified four ERK1/2-dependent phosphorylation sites in Gab2 that prevent the recruitment of the p85 regulatory subunit of PI3K. Using bone marrow-derived mast cells to study Gab2-dependent signaling, we found that the inhibition of ERK1/2 activity promotes Akt signaling in response to Kit and the high-affinity IgE receptor. Together, our results indicate that ERK1/2 participates in a negative-feedback loop that attenuates PI3K/Akt signaling in response to various agonists.

scholarly journals A Minor Catalytic Activity of Src Family Kinases Is Sufficient for Maximal Activation of Mast Cells via the High-Affinity IgE Receptor

2009 ◽  
Vol 184 (1) ◽  
pp. 84-93 ◽  
Author(s):  
Michael Poderycki ◽  
Yoshiaki Tomimori ◽  
Tomoaki Ando ◽  
Wenbin Xiao ◽  
Mari Maeda-Yamamoto ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Mast Cells ◽  
Src Family Kinases ◽  
Ige Receptor ◽  
High Affinity ◽  
Maximal Activation ◽  
A Minor ◽  
High Affinity Ige Receptor

scholarly journals Measurement for Canine IgE Using Canine Recombinant High Affinity IgE Receptor ^|^alpha; Chain (Fc^|^epsilon;RI^|^alpha;)

2012 ◽  
Vol 74 (7) ◽  
pp. 851-856 ◽  
Author(s):  
Toshihiro TSUKUI ◽  
Masahiro SAKAGUCHI ◽  
Keigo KURATA ◽  
Sadatoshi MAEDA ◽  
Keitaro OHMORI ◽  
...  
Keyword(s):  
Ige Receptor ◽  
Receptor Alpha ◽  
Alpha Chain ◽  
High Affinity ◽  
High Affinity Ige Receptor ◽  
Receptor Alpha Chain

scholarly journals Regulation of the Tyrosine Phosphorylation of Phospholipid Scramblase 1 in Mast Cells That Are Stimulated through the High-Affinity IgE Receptor

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e109800 ◽  
Author(s):  
Asma Kassas ◽  
Ivan C. Moura ◽  
Yumi Yamashita ◽  
Jorg Scheffel ◽  
Claudine Guérin-Marchand ◽  
...  
Keyword(s):  
Mast Cells ◽  
Tyrosine Phosphorylation ◽  
Ige Receptor ◽  
Phospholipid Scramblase ◽  
High Affinity ◽  
High Affinity Ige Receptor ◽  
Phospholipid Scramblase 1

scholarly journals High-affinity IgE receptor-β chain expression in human mast cells

2008 ◽  
Vol 336 (2) ◽  
pp. 229-234 ◽  
Author(s):  
Akira Matsuda ◽  
Yoshimichi Okayama ◽  
Nobuyuki Ebihara ◽  
Norihiko Yokoi ◽  
Peisong Gao ◽  
...  
Keyword(s):  
Mast Cells ◽  
Ige Receptor ◽  
High Affinity ◽  
Human Mast Cells ◽  
High Affinity Ige Receptor ◽  
Β Chain

scholarly journals Substance P downregulates expression of the high affinity IgE receptor (FcεRI) by human mast cells

2010 ◽  
Vol 220 (1-2) ◽  
pp. 17-24 ◽  
Author(s):  
Christine McCary ◽  
Brian P. Tancowny ◽  
Adriana Catalli ◽  
Leslie C. Grammer ◽  
Kathleen E. Harris ◽  
...  
Keyword(s):  
Mast Cells ◽  
Substance P ◽  
Ige Receptor ◽  
High Affinity ◽  
Human Mast Cells ◽  
High Affinity Ige Receptor

Post-translational suppression of the high affinity IgE receptor expression on mast cells by an intestinal bacterium

Immunobiology ◽  
2021 ◽  
Vol 226 (2) ◽  
pp. 152056
Author(s):  
Sakino Fukatsu ◽  
Hikari Horinouchi ◽  
Shiho Nagata ◽  
Risa Kamei ◽  
Daichi Tanaka ◽  
...  
Keyword(s):  
Mast Cells ◽  
Receptor Expression ◽  
Intestinal Bacterium ◽  
Ige Receptor ◽  
High Affinity ◽  
High Affinity Ige Receptor ◽  
Translational Suppression

scholarly journals Regulation of Trafficking and Signaling of the High Affinity IgE Receptor by FcεRIβ and the Potential Impact of FcεRIβ Splicing in Allergic Inflammation

2022 ◽  
Vol 23 (2) ◽  
pp. 788
Author(s):  
Greer K. Arthur ◽  
Glenn Cruse
Keyword(s):  
Mast Cells ◽  
Cell Function ◽  
Allergic Inflammation ◽  
Receptor Complex ◽  
Ige Receptor ◽  
Preferential Expression ◽  
High Affinity ◽  
Proinflammatory Mediators ◽  
Ige Mediated ◽  
High Affinity Ige Receptor

Mast cells are tissue-resident immune cells that function in both innate and adaptive immunity through the release of both preformed granule-stored mediators, and newly generated proinflammatory mediators that contribute to the generation of both the early and late phases of the allergic inflammatory response. Although mast cells can be activated by a vast array of mediators to contribute to homeostasis and pathophysiology in diverse settings and contexts, in this review, we will focus on the canonical setting of IgE-mediated activation and allergic inflammation. IgE-dependent activation of mast cells occurs through the high affinity IgE receptor, FcεRI, which is a multimeric receptor complex that, once crosslinked by antigen, triggers a cascade of signaling to generate a robust response in mast cells. Here, we discuss FcεRI structure and function, and describe established and emerging roles of the β subunit of FcεRI (FcεRIβ) in regulating mast cell function and FcεRI trafficking and signaling. We discuss current approaches to target IgE and FcεRI signaling and emerging approaches that could target FcεRIβ specifically. We examine how alternative splicing of FcεRIβ alters protein function and how manipulation of splicing could be employed as a therapeutic approach. Targeting FcεRI directly and/or IgE binding to FcεRI are promising approaches to therapeutics for allergic inflammation. The characteristic role of FcεRIβ in both trafficking and signaling of the FcεRI receptor complex, the specificity to IgE-mediated activation pathways, and the preferential expression in mast cells and basophils, makes FcεRIβ an excellent, but challenging, candidate for therapeutic strategies in allergy and asthma, if targeting can be realized.

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