Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells

Cell Calcium ◽  
2007 ◽  
Vol 42 (3) ◽  
pp. 323-331 ◽  
Author(s):  
Annabelle Z. Caron ◽  
Benoit Chaloux ◽  
Guillaume Arguin ◽  
Gaetan Guillemette
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Receptor Type ◽  
Rinm5f Cells ◽  
Apparent Affinity ◽  
Kinase C ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Type 3

Regulation of the phosphorylation of the inositol 1,4,5-trisphosphate receptor by protein kinase C

2004 ◽  
Vol 319 (3) ◽  
pp. 888-893 ◽  
Author(s):  
Elke Vermassen ◽  
Rafael A Fissore ◽  
Nael Nadif Kasri ◽  
Veerle Vanderheyden ◽  
Geert Callewaert ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

scholarly journals Protein kinase C phosphorylates the inositol 1,4,5-trisphosphate receptor type 2 and decreases the mobilization of Ca2+in pancreatoma AR4-2J cells

2007 ◽  
Vol 192 (3) ◽  
pp. 659-668 ◽  
Author(s):  
Guillaume Arguin ◽  
Yannik Regimbald-Dumas ◽  
Marc-Olivier Fregeau ◽  
Annabelle Z Caron ◽  
Gaetan Guillemette
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Types ◽  
Excitable Cells ◽  
Kinase C ◽  
Inositol 1,4,5 Trisphosphate ◽  
Intracellular Ca ◽  
Pre Treatment ◽  
Trisphosphate Receptor

In non-excitable cells, the inositol 1,4,5-trisphosphate receptor channel, which plays a major (IP3R) is an intracellular Ca2+ role in Ca2+ signalling. Three isoforms of IP3R have been identified (IP3R-1, IP3R-2 and IP3R-3) and most cell types express different proportions of each isoform. The differences between the pharmacological and functional properties of the various isoforms of IP3R are poorly understood. AR4-2J cells, which express almost exclusively (~86%) the IP3R-2, represent an interesting model to study this particular isoform. Here, we investigated a regulatory mechanism by which protein kinase C (PKC) influences IP3R-2-mediated Ca2+ release. Using an immunoprecipitation approach, we confirmed that AR4-2J cells express almost exclusively the IP3R-2 isoform. Using an in vitro phosphorylation assay, we showed that the immunopurified IP3R-2 was efficiently phosphorylated by exogenous PKC. In intact AR4-2J cells metabolically labelled with 32Pi, we showed that phorbol-12-myristate-13-acetate (PMA) and Ca2+ mobilizing agonists cause the phosphorylation of IP3R-2. In saponin-permeabilized AR4-2J cells, IP3-induced Ca2+ release was reduced after a pre-treatment with PMA or with exogenous PKC. PMA also reduced the Ca2+ response of intact AR4-2J cells stimulated with carbachol and epidermal growth factor, two agonists that use different receptor types to activate phospholipase C. These results demonstrate that PKC decreases the Ca2+mobilizing activity of IP3R-2 and thus exerts a negative feedback on the agonists-induced Ca2+ response of AR4-2J cells.

Differential modulation of inositol 1,4,5-trisphosphate receptor type 1 and type 3 by ATP

Cell Calcium ◽  
2000 ◽  
Vol 27 (5) ◽  
pp. 257-267 ◽  
Author(s):  
K. Maes ◽  
L. Missiaen ◽  
P. De Smet ◽  
S. Vanlingen ◽  
G. Callewaert ◽  
...  
Keyword(s):  
Receptor Type ◽  
Differential Modulation ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Type 3
Sign in / Sign up

Export Citation Format

Share Document