scholarly journals Blockade of ankyrin repeat-rich membrane spanning protein modulates extracellular signal-regulated kinase expression and inhibits allergic inflammation in ovalbumin-sensitized mice

2013 ◽  
Vol 1 (4) ◽  
pp. 674-678 ◽  
Author(s):  
XIUQIN NI ◽  
XING LI ◽  
SHUHUA TAO ◽  
MINGHUI XU ◽  
HONGMEI MA ◽  
...  
Keyword(s):  
Allergic Inflammation ◽  
Ankyrin Repeat ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Membrane Spanning ◽  
Kinase Expression

scholarly journals Extracellular Signal-Regulated Kinase Mediates Ebastine-Induced Human Follicle Dermal Papilla Cell Proliferation

2019 ◽  
Vol 2019 ◽  
pp. 1-9
Author(s):  
Fu-Ming Tsai ◽  
Chao-Hsu Li ◽  
Lu-Kai Wang ◽  
Mao-Liang Chen ◽  
Ming-Cheng Lee ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Allergic Inflammation ◽  
Dermal Papilla ◽  
Dermal Papilla Cells ◽  
Expression Levels ◽  
Extracellular Signal Regulated Kinase ◽  
Hair Regrowth ◽  
Extracellular Signal ◽  
Elevated Expression ◽  
H1 Receptor Antagonist

Ebastine is a second-generation histamine H1 receptor antagonist that is used to attenuate allergic inflammation. Ebastine has also shown to affect hair loss; however, the immunoregulatory effect of ebastine cannot completely exclude the possibility of spontaneous hair regrowth in ebastine-treated mice. In this study, we examined the effects of ebastine on the growth of human follicle dermal papilla cells (HFDPC) using a WST-1 cell proliferation assay and a bromodeoxyuridine incorporation assay. Ebastine was shown to significantly increase the proliferation of HFDPC. The expression levels of cell-cycle regulatory proteins and an antiapoptotic protein were increased in ebastine-treated HFDPC. Furthermore, elevated expression levels of phospho-AKT and phospho-p44/42 extracellular signal-regulated kinase (ERK) were observed in ebastine-treated HFDPC. Ebastine-mediated HFDPC growth was completely reversed by blocking ERK kinase. The results from our present study suggest that the regulation of HFDPC proliferation by ebastine might be directly involved in hair regrowth through the ERK signaling pathway.

scholarly journals Multifaceted roles of β-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling

2003 ◽  
Vol 375 (3) ◽  
pp. 503-515 ◽  
Author(s):  
Sudha K. SHENOY ◽  
Robert J. LEFKOWITZ
Keyword(s):  
G Protein ◽  
Receptor Internalization ◽  
Adapter Proteins ◽  
Adapter Protein ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Membrane Spanning ◽  
G Protein Coupled ◽  
Adp Ribosylation Factor

β-Arrestins are cytosolic proteins that bind to activated and phosphorylated G-protein-coupled receptors [7MSRs (seven-membrane-spanning receptors)] and uncouple them from G-protein-mediated second messenger signalling pathways. The binding of β-arrestins to 7MSRs also leads to new signals via activation of MAPKs (mitogen-activated protein kinases) such as JNK3 (c-Jun N-terminal kinase 3), ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38 MAPKs. By binding to endocytic proteins [clathrin, AP2 (adapter protein 2), NSF (N-ethylmaleimide-sensitive fusion protein) and ARF6 (ADP-ribosylation factor 6)], β-arrestins also serve as adapters to link the receptors to the cellular trafficking machinery. Agonist-promoted ubiquitination of β-arrestins is a prerequisite for their role in receptor internalization, as well as a determinant of the differing trafficking patterns of distinct classes of receptors. Recently, β-arrestins have also been implicated as playing novel roles in cellular chemotaxis and apoptosis. By virtue of their ability to bind, in a stimulus-dependent fashion, to 7MSRs as well as to different classes of cellular proteins, β-arrestins serve as versatile adapter proteins that regulate the signalling and trafficking of the receptors.

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