DEPLETION OF INSP3 STORES ACTIVATES A CA2+ AND K+ CURRENT BY MEANS OF A PHOSPHATASE AND A DIFFUSIBLE MESSENGER
DEPLETION OF INSP3 STORES ACTIVATES A CA2+ AND K+ CURRENT BY MEANS OF A PHOSPHATASE AND A DIFFUSIBLE MESSENGER
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DOI:
10.1038/364814a0
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发表时间:
1993-08-26
期刊:
影响因子:
64.8
通讯作者:
STUHMER, W
中科院分区:
文献类型:
--
作者:
PAREKH, AB;TERLAU, H;STUHMER, W
IN non-excitable cells, release of Ca2+ from the inositol 1,4,5-trisphosphate (InsP3)-sensitive store can activate Ca2+ entry1-3. Very little is known about the signal mechanism relating store emptying to plasma membrane Ca2+ influx. It has been suggested that the signal may be either a diffusible messenger like an inositol phosphate4, or the InsP3 receptor itself, which, by physically coupling to some component of Ca2+ entry in the plasma membrane, may link store release to Ca2+ entry5. The nature of the Ca2+ entry pathway is also unclear. Only in mast cells has a very selective Ca2+ current been observed after store emptying6. Activation of exogenous 5-hydroxytryptamine (5-HT) receptors expressed in Xenopus oocytes or direct injection of InsP3 evokes Ca2+ entry activated by InsP3 pool depletion7. Here we investigate the nature of this influx pathway and find a current activated by pool depletion. This has an unusual selectivity in that it is more permeable to Ca2+ ions than to other divalent cations (Ba2+, Sr2+ or Mn2+). Moreover, a K+ permeability is also stimulated after pool depletion. The activation of this store depletion current involves both a phosphatase and an unidentified diffusible messenger. Both the Ca2+ entry pathway and the activating factors found here may be relevant to pool-depleted Ca2+ entry in a variety of non-excitable cells.