%0 Journal Article
%9 ACL : Articles dans des revues avec comité de lecture répertoriées par l'AERES
%A Jaimovich, E.
%A Mattei, C.
%A Liberona, J. L.
%A Cardenas, C.
%A Estrada, M.
%A Barbier, J.
%A Debitus, Cécile
%A Laurent, Dominique
%A Molgo, J.
%T Xestospongin B, a competitive inhibitor of IP3-mediated Ca2+ signalling in cultured rat myotubes, isolated myonuclei, and neuroblastoma (NG108-15) cells
%D 2005
%L fdi:010038253
%G ENG
%J Febs Letters
%@ 0014-5793
%K INVERTEBRE AQUATIQUE ; SUBSTANCE NATURELLE ; ALCALOIDE ; STRUCTURE CHIMIQUE ; ACTIVITE BIOLOGIQUE ; INTERET PHARMACOLOGIQUE ; CULTURE CELLULAIRE ; TEST
%K XESTOSPONGIN B ; EPONGE
%K xestospongin B ; inositol 1,4,5 trisphosphate ; intracellular Ca2+ signals ; bradykinin ; neuroblastoma NG108 15 cell ; rat skeletal myotubes ; cerebellar membranes ; isolated myonuclei ; calcium ATPase
%K NOUVELLE CALEDONIE
%M CC:0002283107-0006
%N 10
%P 2051-2057
%R 10.1016/j.febslet.2005.02.053
%U https://www.documentation.ird.fr/hor/fdi:010038253
%> https://horizon.documentation.ird.fr/exl-doc/pleins_textes/2024-12/010038253.pdf
%V 579
%W Horizon (IRD)
%X Xestospongin B, a macrocyclic bis-1-oxaquinolizidine alkaloid extracted from the marine sponge Xestospongia exigua, was highly purified and tested for its ability to block inositol 1,4,5-trisphosphate (IP3)-induced Ca2+ release. In a concentration-dependent manner xestospongin B displaced [H-3]IP3 from both rat cerebellar membranes and rat skeletal myotube homogenates with an EC50 of 44.6 +/- 1.1 mu M and 27.4 +/- 1.1 mu M, respectively. Xestospongin B, depending on the dose, suppressed bradykinin-induced Ca2+ signals in neuroblastoma (NG108-15) cells, and also selectively blocked the slow intracellular Ca2+ signal induced by membrane depolarization with high external K+ (47mM) in rat skeletal myotubes. This slow Ca2+ signal is unrelated to muscle contraction, and involves IP3 receptors. In highly purified isolated nuclei from rat skeletal myotubes, Xestospongin B reduced, or suppressed IP3-induced Ca2+ oscillations with an EC50 = 18.9 +/- 1.35 mu M. In rat my rotubes exposed to a Ca2+-free medium, Xestospongin B neither depleted sarcoplasmic reticulum Ca2+ stores, nor modified thapsigargin action and did not affect capacitative Ca2+ entry after thapsigargin-induced depletion of Ca2+ stores. Ca2+-ATPase activity measured in skeletal myrotube homogenates remained unaffected by Xestospongin B. It is concluded that xestospongin B is an effective cell-permeant. competitive inhibitor of IP3 receptors in cultured rat myotubes, isolated myonuclei, and neuroblastoma (NG108-15) cells. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
%$ 035SUBSAN02