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231223s2008 xx |||||o 00| ||eng c |
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|a 10.1016/j.clim.2008.07.003
|2 doi
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|a pubmed24n0605.xml
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|a (DE-627)NLM181557665
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|a (NLM)18700185
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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1 |
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|a Matsui, Takashi
|e verfasserin
|4 aut
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|a Functionality of the IgA Fc receptor (FcalphaR, CD89) is down-regulated by extensive engagement of FcepsilonRI
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|c 2008
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 07.10.2008
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|a Date Revised 24.11.2016
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Besides mast cells and basophils, the high-affinity IgE Fc receptor (FcepsilonRI) is exclusively expressed on certain FcalphaR (IgA Fc receptor)-expressing immune cells such as neutrophils in allergic patients. Transfected rat basophilic leukemia cell line (RBL-2H3) co-expressing FcepsilonRI and FcalphaR was analyzed for effects of simultaneous receptor engagement by their specific antibodies on degranulation and signaling. Whereas supraoptimal FcepsilonRI engagement decreased degranulation, which is known as a bell-shaped dose-response curve, such inhibitory effect was not observed with FcalphaR engagement. However, simultaneous engagement of FcepsilonRI and FcalphaR showed that supraoptimal FcepsilonRI engagement down-regulates FcalphaR-mediated degranulation. This inhibition was associated with extensive phosphorylation of inositol polyphosphate 5'-phosphatase SHIP1 and FcepsilonRIbeta, and reversed by adding actin-depolymerizing drug, latrunculin B. The results suggest an endogenous mechanism by which FcalphaR functionality is down-regulated in an 'allergic environment' where FcepsilonRI is co-expressed and extensively cross-linked on FcalphaR-expressing effector cells
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Actins
|2 NLM
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|a Antigens, CD
|2 NLM
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|a Bridged Bicyclo Compounds, Heterocyclic
|2 NLM
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|a Fc(alpha) receptor
|2 NLM
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|a Receptors, Fc
|2 NLM
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|a Receptors, IgE
|2 NLM
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|a Thiazolidines
|2 NLM
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|a Phosphoric Monoester Hydrolases
|2 NLM
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|a EC 3.1.3.2
|2 NLM
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|a Inositol Polyphosphate 5-Phosphatases
|2 NLM
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|a EC 3.1.3.56
|2 NLM
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|a INPP5D protein, human
|2 NLM
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|a EC 3.1.3.86
|2 NLM
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|a Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
|2 NLM
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|a EC 3.1.3.86
|2 NLM
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|a latrunculin B
|2 NLM
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|a LW7U308U7U
|2 NLM
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1 |
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|a Nunomura, Satoshi
|e verfasserin
|4 aut
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1 |
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|a Shimokawa, Toshibumi
|e verfasserin
|4 aut
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1 |
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|a Yoshimaru, Tetsuro
|e verfasserin
|4 aut
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1 |
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|a Ra, Chisei
|e verfasserin
|4 aut
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773 |
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|i Enthalten in
|t Clinical immunology (Orlando, Fla.)
|d 1999
|g 129(2008), 1 vom: 16. Okt., Seite 155-62
|w (DE-627)NLM098196855
|x 1521-7035
|7 nnns
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1 |
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|g volume:129
|g year:2008
|g number:1
|g day:16
|g month:10
|g pages:155-62
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|u http://dx.doi.org/10.1016/j.clim.2008.07.003
|3 Volltext
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_ILN_11
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|a GBV_ILN_24
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|a GBV_ILN_350
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|a AR
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|d 129
|j 2008
|e 1
|b 16
|c 10
|h 155-62
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