Calcium Signals in Rat Basophilic Leukemia (RBL-2H3) Cells Primed with the Neuropeptide Substance P.

Furukawa, Yôko; Furuno, Tadahide; Teshima, Reiko; Nakanishi, Mamoru

doi:10.1248/bpb.24.1060

Cited by 3 publications

(2 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For treatment with MβCD, cells were incubated with MβCD for 30 min with Fura2/AM. Ratio values were converted to Ca 2+ concentration by the procedure reported previously (21).…”

Section: Methodsmentioning

confidence: 99%

Cholesterol Depletion Inhibits Store-Operated Calcium Currents and Exocytotic Membrane Fusion in RBL-2H3 Cells

2003

Self Cite

View full text Add to dashboard Cite

The effects of cholesterol depletion from the plasma membrane with methyl-beta-cyclodextrin (MbetaCD) on exocytotic processes were investigated in rat basophil leukemia cells (RBL-2H3 cells). Pretreatment of the cells with MbetaCD inhibited antigen-evoked exocytotic release dose-dependently. To elucidate the mechanism of this inhibition, we performed experiments on the effects of MbetaCD on exocytotic membrane fusion and mobilization of Ca(2+) and on the localization of the tyrosine kinase Lyn. Inhibition of degranulation by MbetaCD was observed even under stimulation with the phorbol ester and calcium ionophore. Therefore, MbetaCD affected a process downstream of Ca(2+) influx, or membrane fusion between the granule and the plasma membrane. Intracellular calcium measurements revealed that MbetaCD inhibited the Ca(2+) increase induced by antigen. Furthermore, we found that MbetaCD significantly inhibited Ca(2+) influx from the extracellular medium through the store-operated calcium channel (SOC) but did not affect Ca(2+) release from the intracellular Ca(2+) store. Fluorescent image analysis of cells expressing Lyn-YFP showed that treatment with MbetaCD scarcely affected the localization and lateral mobility of Lyn in the plasma membrane. These results suggest that cholesterol depletion by MbetaCD decreases degranulation mainly by inhibiting the SOC and membrane fusion between the secretory granules and the plasma membrane in mast cells.

show abstract

“…For treatment with MβCD, cells were incubated with MβCD for 30 min with Fura2/AM. Ratio values were converted to Ca 2+ concentration by the procedure reported previously (21).…”

Section: Methodsmentioning

confidence: 99%

Cholesterol Depletion Inhibits Store-Operated Calcium Currents and Exocytotic Membrane Fusion in RBL-2H3 Cells

2003

Self Cite

View full text Add to dashboard Cite

show abstract

“…However, the detailed role of NK1R in allergic disorders remains unclear. Given that previous reports have demonstrated that NK1R is expressed in the RBL-2H3 cell line, a rat mast cell line with the properties of mucosal mast cells [22, 23], determining whether NK1R plays a role in FcεRΙ-induced activation of RBL-2H3 cells, will be of significance.…”

Section: Introductionmentioning

confidence: 99%

An involvement of neurokinin-1 receptor in FcεRΙ-mediated RBL-2H3 mast cell activation

Fang

Xie

et al. 2012

Inflamm. Res.

View full text Add to dashboard Cite

Objective and designTo determine whether the neurokinin-1 receptor (NK1R) plays a role in the activation of RBL-2H3 mast cells after FcεRΙ aggregation.Materials and methodsNK1R expression in RBL-2H3 cells was inhibited by small hairpin RNA (shRNA) against NK1R, and determined by western blotting. For activation, both NK1R knockdown and control RBL-2H3 cells were sensitized by dinitrophenol (DNP)-specific IgE and stimulated with the antigen DNP-bovine serum albumin (BSA). Following the activation of RBL-2H3 cells, monocyte chemoattractant protein (MCP-1) production and intracellular calcium flux were monitored by ELISA and confocal microscopy assay, respectively. For investigation of the signaling mechanism, phosphorylation of mitogen-activated protein kinases (MAPKs) after RBL-2H3 cell activation was assessed by western blotting.ResultsshRNA-NK1R mediated an effective inhibition of NK1R expression in RBL-2H3 cells. Protein production of MCP-1 was reduced by more than 55 % in NK1R knockdown RBL-2H3 cells compared with control RBL-2H3 cells. In addition, both calcium mobilization and phosphorylation levels of MAPKs (Erk1/2, JNK, and p38) after DNP-BSA stimulation (via FcεRΙ) were decreased due to the inhibition of NK1R expression.ConclusionNK1R is required for the activation of RBL-2H3 cells following FcεRΙ engagement and involved in the regulation of MAPK signaling pathways.Electronic supplementary materialThe online version of this article (doi:10.1007/s00011-012-0523-x) contains supplementary material, which is available to authorized users.

show abstract

Leukemias

Mravec

2024

Neurobiology of Cancer

View full text Add to dashboard Cite

Calcium Signals in Rat Basophilic Leukemia (RBL-2H3) Cells Primed with the Neuropeptide Substance P.

Cited by 3 publications

References 22 publications

Cholesterol Depletion Inhibits Store-Operated Calcium Currents and Exocytotic Membrane Fusion in RBL-2H3 Cells

Cholesterol Depletion Inhibits Store-Operated Calcium Currents and Exocytotic Membrane Fusion in RBL-2H3 Cells

An involvement of neurokinin-1 receptor in FcεRΙ-mediated RBL-2H3 mast cell activation

Leukemias

Contact Info

Product

Resources

About