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231223s2009 xx |||||o 00| ||eng c |
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|a 10.1016/j.clim.2009.05.003
|2 doi
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|a pubmed24n0630.xml
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|a (DE-627)NLM188860738
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|a (NLM)19477690
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Saini, Sarbjit S
|e verfasserin
|4 aut
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|a Cultured peripheral blood mast cells from chronic idiopathic urticaria patients spontaneously degranulate upon IgE sensitization
|b Relationship to expression of Syk and SHIP-2
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|c 2009
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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 01.09.2009
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|a Date Revised 20.10.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Recently, signaling changes in the FcvarepsilonRI pathway involving inositol lipid phosphatases have been identified in the basophils of chronic idiopathic urticaria (CIU) subjects. Based on the profile of basophil FcvarepsilonRI-mediated histamine degranulation, we have segregated CIU subjects into two groups, CIU Responder (CIU R) or CIU Nonresponder (CIU NR). In the present study, we compared expression of SHIP-1, SHIP-2, and Syk protein to histamine release (HR) from mast cells (MC) cultured from the peripheral blood of CIU R, CIU NR, and normal subjects. The MC of CIU R donors contained significantly increased Syk and decreased SHIP-2 as compared to CIU NR (Syk: p=0.038, SHIP-2: p=0.038) and normals (Syk: p=0.042, SHIP-2: p=0.027). Spontaneous HR from CIU donors was increased two-fold compared to normals (p=0.04). In summary, our results suggest a possible predilection for urticarial MC to spontaneously degranulate upon IgE sensitization contributing to the increased pruritus associated with CIU
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|a Journal Article
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|a Research Support, N.I.H., Extramural
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|a Research Support, Non-U.S. Gov't
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|a Antibodies
|2 NLM
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|a Intracellular Signaling Peptides and Proteins
|2 NLM
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|a Receptors, IgE
|2 NLM
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|a Immunoglobulin E
|2 NLM
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|a 37341-29-0
|2 NLM
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|a Histamine
|2 NLM
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|a 820484N8I3
|2 NLM
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|a Protein-Tyrosine Kinases
|2 NLM
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|a EC 2.7.10.1
|2 NLM
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|a Proto-Oncogene Proteins c-kit
|2 NLM
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|a EC 2.7.10.1
|2 NLM
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|a SYK protein, human
|2 NLM
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|a EC 2.7.10.2
|2 NLM
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|a Syk Kinase
|2 NLM
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|a EC 2.7.10.2
|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 INPPL1 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 Paterniti, Miya
|e verfasserin
|4 aut
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|a Vasagar, Kavitha
|e verfasserin
|4 aut
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|a Gibbons, Scott P
|c Jr
|e verfasserin
|4 aut
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|a Sterba, Patricia M
|e verfasserin
|4 aut
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|a Vonakis, Becky M
|e verfasserin
|4 aut
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|i Enthalten in
|t Clinical immunology (Orlando, Fla.)
|d 1999
|g 132(2009), 3 vom: 01. Sept., Seite 342-8
|w (DE-627)NLM098196855
|x 1521-7035
|7 nnns
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|g volume:132
|g year:2009
|g number:3
|g day:01
|g month:09
|g pages:342-8
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|u http://dx.doi.org/10.1016/j.clim.2009.05.003
|3 Volltext
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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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 132
|j 2009
|e 3
|b 01
|c 09
|h 342-8
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