scholarly journals Histamine H4 receptor activation enhances LPS-induced IL-6 production in mast cells via ERK and PI3K activation

2011 ◽  
Vol 41 (6) ◽  
pp. 1764-1773 ◽  
Author(s):  
Pragnya Desai ◽  
Robin L. Thurmond
Keyword(s):  
Mast Cells ◽  
Receptor Activation ◽  
Histamine H4 Receptor ◽  
Pi3k Activation ◽  
H4 Receptor

scholarly journals Sequential Engagement of FcεRI on Mast Cells and Basophil Histamine H4 Receptor and FcεRI in Allergic Rhinitis

2012 ◽  
Vol 190 (2) ◽  
pp. 539-548 ◽  
Author(s):  
Yoshiki Shiraishi ◽  
Yi Jia ◽  
Joanne Domenico ◽  
Anthony Joetham ◽  
Hajime Karasuyama ◽  
...  
Keyword(s):  
Allergic Rhinitis ◽  
Mast Cells ◽  
Histamine H4 Receptor ◽  
H4 Receptor

Cloning and characterization of dominant negative splice variants of the human histamine H4 receptor

2008 ◽  
Vol 414 (1) ◽  
pp. 121-131 ◽  
Author(s):  
Richard M. van Rijn ◽  
André van Marle ◽  
Paul L. Chazot ◽  
Ellen Langemeijer ◽  
Yongjun Qin ◽  
...  
Keyword(s):  
Mast Cells ◽  
Mammalian Cells ◽  
Splice Variants ◽  
Inflammatory Diseases ◽  
Dominant Negative ◽  
Full Length ◽  
Dominant Negative Effect ◽  
Histamine H4 Receptor ◽  
Negative Effect ◽  
H4 Receptor

The H4R (histamine H4 receptor) is the latest identified member of the histamine receptor subfamily of GPCRs (G-protein-coupled receptors) with potential functional implications in inflammatory diseases and cancer. The H4R is primarily expressed in eosinophils and mast cells and has the highest homology with the H3R. The occurrence of at least twenty different hH3R (human H3R) isoforms led us to investigate the possible existence of H4R splice variants. In the present paper, we report on the cloning of the first two alternatively spliced H4R isoforms from CD34+ cord blood-cell-derived eosinophils and mast cells. These H4R splice variants are localized predominantly intracellularly when expressed recombinantly in mammalian cells. We failed to detect any ligand binding, H4R–ligand induced signalling or constitutive activity for these H4R splice variants. However, when co-expressed with full-length H4R [H4R(390) (H4R isoform of 390 amino acids)], the H4R splice variants have a dominant negative effect on the surface expression of H4R(390). We detected H4R(390)–H4R splice varianthetero-oligomers by employing both biochemical (immunoprecipitation and cell-surface labelling) and biophysical [time-resolved FRET (fluorescence resonance energy transfer)] techniques. mRNAs encoding the H4R splice variants were detected in various cell types and expressed at similar levels to the full-length H4R(390) mRNA in, for example, pre-monocytes. We conclude that the H4R splice variants described here have a dominant negative effect on H4R(390) functionality, as they are able to retain H4R(390) intracellularly and inactivate a population of H4R(390), presumably via hetero-oligomerization.

Histamine H4 receptor mediates chemotaxis of human lung mast cells

2018 ◽  
Vol 837 ◽  
pp. 38-44 ◽  
Author(s):  
Linda J. Kay ◽  
S.Kim Suvarna ◽  
Peter T. Peachell
Keyword(s):  
Mast Cells ◽  
Human Lung ◽  
Histamine H4 Receptor ◽  
H4 Receptor

In Silico Characterization of Ligand Binding Modes in the Human Histamine H4 Receptor and their Impact on Receptor Activation

ChemBioChem ◽  
2010 ◽  
Vol 11 (13) ◽  
pp. 1850-1855 ◽  
Author(s):  
Tim Werner ◽  
Kerstin Sander ◽  
Yusuf Tanrikulu ◽  
Tim Kottke ◽  
Ewgenij Proschak ◽  
...  
Keyword(s):  
Ligand Binding ◽  
In Silico ◽  
Receptor Activation ◽  
Binding Modes ◽  
Histamine H4 Receptor ◽  
H4 Receptor ◽  
In Silico Characterization ◽  
Human Histamine

scholarly journals Histamine H4 Receptor Mediates Chemotaxis and Calcium Mobilization of Mast Cells

2003 ◽  
Vol 305 (3) ◽  
pp. 1212-1221 ◽  
Author(s):  
Claudia L. Hofstra ◽  
Pragnya J. Desai ◽  
Robin L. Thurmond ◽  
Wai-Ping Fung-Leung
Keyword(s):  
Mast Cells ◽  
Calcium Mobilization ◽  
Histamine H4 Receptor ◽  
H4 Receptor

Histamine H4 receptor activation alleviates neuropathic pain through differential regulation of ERK, JNK, and P38 MAPK phosphorylation

Pain ◽  
2015 ◽  
Vol 156 (12) ◽  
pp. 2492-2504 ◽  
Author(s):  
Maria D. Sanna ◽  
Holger Stark ◽  
Laura Lucarini ◽  
Carla Ghelardini ◽  
Emanuela Masini ◽  
...  
Keyword(s):  
Neuropathic Pain ◽  
P38 Mapk ◽  
Receptor Activation ◽  
Differential Regulation ◽  
Histamine H4 Receptor ◽  
Mapk Phosphorylation ◽  
H4 Receptor

scholarly journals TRPV1 and PLC Participate in Histamine H4 Receptor-Induced Itch

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Tunyu Jian ◽  
Niuniu Yang ◽  
Yan Yang ◽  
Chan Zhu ◽  
Xiaolin Yuan ◽  
...  
Keyword(s):  
Intracellular Signaling ◽  
Underlying Mechanism ◽  
Receptor Activation ◽  
Ruthenium Red ◽  
Drg Neurons ◽  
Histamine H4 Receptor ◽  
Signaling Mechanism ◽  
Downstream Signaling ◽  
Intracellular Ca ◽  
H4 Receptor

Histamine H4 receptor has been confirmed to play a role in evoking peripheral pruritus. However, the ionic and intracellular signaling mechanism of activation of H4 receptor on the dorsal root ganglion (DRG) neurons is still unknown. By using cell culture and calcium imaging, we studied the underlying mechanism of activation of H4 receptor on the DRG neuron. Immepip dihydrobromide (immepip)—a histamine H4 receptor special agonist under cutaneous injection—obviously induced itch behavior of mice. Immepip-induced scratching behavior could be blocked by TRPV1 antagonist AMG9810 and PLC pathway inhibitor U73122. Application of immepip (8.3–50 μM) could also induce a dose-dependent increase in intracellular Ca2+(Ca2+i) of DRG neurons. We found that 77.8% of the immepip-sensitized DRG neurons respond to the TRPV1 selective agonist capsaicin. U73122 could inhibit immepip-induced Ca2+responses. In addition, immepip-inducedCa2+iincrease could be blocked by ruthenium red, capsazepine, and AMG9810; however it could not be blocked by TRPA1 antagonist HC-030031. These results indicate that TRPV1 but not TRPA1 is the important ion channel to induce the DRG neurons’ responses in the downstream signaling pathway of histamine H4 receptor and suggest that TRPV1 may be involved in the mechanism of histamine-induced itch response by H4 receptor activation.

Role of the second and third extracellular loops of the histamine H4 receptor in receptor activation

2011 ◽  
Vol 384 (3) ◽  
pp. 301-317 ◽  
Author(s):  
Irena Brunskole ◽  
Andrea Strasser ◽  
Roland Seifert ◽  
Armin Buschauer
Keyword(s):  
Receptor Activation ◽  
Histamine H4 Receptor ◽  
Extracellular Loops ◽  
H4 Receptor

Functional characterization of histamine H4 receptor on human mast cells

2014 ◽  
Vol 62 (1) ◽  
pp. 19-28 ◽  
Author(s):  
E. Angel Jemima ◽  
A. Prema ◽  
E. Berla Thangam
Keyword(s):  
Mast Cells ◽  
Functional Characterization ◽  
Histamine H4 Receptor ◽  
Human Mast Cells ◽  
H4 Receptor
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