Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Jean-François Coquil"'
Publikováno v:
Biology of the Cell. 101:469-480
Background information. Interconnections between the Ca2+ and cAMP signalling pathways can determine the specificity and diversity of the cellular effects mediated by these second messengers. Most cAMP effects are mediated by PKA (protein kinase A),
Publikováno v:
Biochemical Journal. 381:423-428
In the present study we investigated the effects of K+ and other univalent cations on [3H]InsP3 {[3H]Ins(1,4,5)P3} binding to sheep cerebellar microsomes. In equilibrium binding experiments performed over 4 s at pH 7.1 and 20 °C, the addition of K+
Publikováno v:
Biochemical Pharmacology. 59:131-139
The inositol 1,4,5-trisphosphate (InsP 3 ) receptor is essential for Ca 2+ release from intracellular stores. There are three InsP 3 receptor types which are targets for several types of regulation. Ca 2+ , phosphorylation, and protein–protein inte
Publikováno v:
Biochemical Journal. 341:697-704
We have characterized in detail the Ca2+-dependent inhibition of [3H]Ins(1,4,5)P3 ([3H]InsP3) binding to sheep cerebellar microsomes, over a short duration (3 s), with the use of a perfusion protocol. This procedure prevented artifacts previously ide
Publikováno v:
Journal of Biological Chemistry. 271:3568-3574
Incubation of cerebellar microsomes with d-myo-inositol 1,4,5-trisphosphate (InsP3) (0.01 1 microM), at 4 or 20 degrees C in a cytosolic-like medium devoid of Ca2+ and Mg2+, followed by InsP3 removal, induced an increase in InsP3 binding determined w
Autor:
C Schteingart, N Chomiki, Jean-François Coquil, Serge Erlinger, P Jourdon, Michel Claret, Laurent Combettes, Brigitte Berthon
Publikováno v:
Biochemical Journal. 273:153-160
The monohydroxy bile acid taurolithocholate permeabilizes the endoplasmic reticulum to Ca2+ in rat liver cells. To assess whether this action on the endoplasmic reticulum was restricted to this tissue, the effects of bile acid were investigated in tw
Publikováno v:
Cell calcium. 23(5)
Ca2+ mobilisation by inositol 1,4,5-trisphosphate (InsP3) is a complex phenomenon which involves positive and negative feedback regulation by cytosolic Ca2+. It has been shown that Ca2+ increased the affinity of [3H]-InsP3 binding to liver membranes
Autor:
Zalika Hannaert-Merah, Jean-Pierre Mauger, Michel Claret, Stéphane Swillens, Laurent Combettes, Philippe Champeil, Jean-François Coquil
Publikováno v:
Cell calcium. 18(5)
Using sheep cerebellum microsomes previously loaded with 45 Ca 2+ or 90 Sr 2+ , we measured the dependence of inositol 1,4,5-trisphosphate (InsP 3 )-induced efflux of these ions on Ca 2+ or Sr 2+ on the cytosolic side. At a low InsP 3 concentration,
Autor:
Michel Claret, Laurent Combettes, Zalika Hannaert-Merah, Jean-François Coquil, Caroline Rousseau, Stéphane Swillens, Philippe Champeil
Publikováno v:
The Journal of biological chemistry. 269(26)
Using microsomal membrane vesicles derived from sheep cerebellum, we measured the rate of inositol 1,4,5-trisphosphate (InsP3)-dependent 45Ca2+ efflux from 45Ca(2+)-loaded compartments during rapid perfusion with a medium containing InsP3 and various
Autor:
Jean-Pierre Mauger, Jean-Philippe Lièvremont, France Piétri-Rouxel, Mauricette Hilly, Jean-François Coquil
Publikováno v:
Molecular and cellular endocrinology. 98(2)
Inositol 1,4,5-trisphosphate (InsP3) is a second messenger responsible for the mobilization of intracellular Ca2+ after receptor-mediated hydrolysis of phosphatidylinositol 4,5-bisphosphate. InsP3 binds to a specific receptor located on the membrane