Chloroquine, quinine and quinidine inhibit calcium release from macrophage intracellular stores by blocking inositol 1,4,5‐trisphosphate binding to its receptor
Identifieur interne : 002952 ( Main/Exploration ); précédent : 002951; suivant : 002953Chloroquine, quinine and quinidine inhibit calcium release from macrophage intracellular stores by blocking inositol 1,4,5‐trisphosphate binding to its receptor
Auteurs : Uma Kant Misra [États-Unis] ; Govind Gawdi [États-Unis] ; Salvatore V. Pizzo [États-Unis]Source :
- Journal of Cellular Biochemistry [ 0730-2312 ] ; 1997-02.
English descriptors
- Teeft :
- Antimalarial, Biochem, Biol, Capacitative, Capacitative entry, Chem, Chloroquine, Endocytosis, Epidermal growth factor, Ginsburg, Inositol, Internal stores, Intracellular, Ligand, Macrophage, Microsomal, Microsomal preparation, Microsomal preparations, Misra, Phagocytic vesicles, Plasmodium species, Quinidine, Quinine, Receptor, Thapsigargin.
Abstract
The binding of many ligands to cellular receptors induces a signaling cascade which generates inositol 1,4,5‐trisphosphate (IP3). IP3 binding to its receptors in various internal compartments causes a rapid Ca2+ efflux into the cytosol. We now demonstrate that chloroquine blocks ligand‐induced Ca2+ mobilization without affecting IP3 synthesis. The effect is independent of the ligand employed and occurred with five unrelated ligands; namely, α2‐macroglobulin‐methylamine, angiotensin II, bradykinin, carbachol, and epidermal growth factor. Chloroquine, quinidine, and quinine, however, block binding of [3H]IP3 to its receptors by 90%, 88%, and 71%, respectively. These observations suggest a previously undetected mechanism by which these agents may in part function as antimalarials. J. Cell. Biochem. 64:225–232. © 1997 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/(SICI)1097-4644(199702)64:2<225::AID-JCB6>3.0.CO;2-Z
Affiliations:
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IP3 binding to its receptors in various internal compartments causes a rapid Ca2+ efflux into the cytosol. We now demonstrate that chloroquine blocks ligand‐induced Ca2+ mobilization without affecting IP3 synthesis. The effect is independent of the ligand employed and occurred with five unrelated ligands; namely, α2‐macroglobulin‐methylamine, angiotensin II, bradykinin, carbachol, and epidermal growth factor. Chloroquine, quinidine, and quinine, however, block binding of [3H]IP3 to its receptors by 90%, 88%, and 71%, respectively. These observations suggest a previously undetected mechanism by which these agents may in part function as antimalarials. J. Cell. 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