scholarly journals Role of the Phospholipase C-Inositol 1,4,5-Trisphosphate Pathway in Calcium Release-activated Calcium Current and Capacitative Calcium Entry

2001 ◽  
Vol 276 (19) ◽  
pp. 15945-15952 ◽  
Author(s):  
Lisa M. Broad ◽  
Franz-Josef Braun ◽  
Jean-Philippe Lievremont ◽  
Gary St. J. Bird ◽  
Tomohiro Kurosaki ◽  
...  
2006 ◽  
Vol 1757 (5-6) ◽  
pp. 380-387 ◽  
Author(s):  
Jerzy Duszyński ◽  
Rafał Kozieł ◽  
Wojciech Brutkowski ◽  
Joanna Szczepanowska ◽  
Krzysztof Zabłocki

2020 ◽  
Vol 9 (4) ◽  
pp. 1096
Author(s):  
Jessica Gambardella ◽  
Angela Lombardi ◽  
Marco Bruno Morelli ◽  
John Ferrara ◽  
Gaetano Santulli

Inositol 1,4,5-trisphosphate receptors (ITPRs) are intracellular calcium release channels located on the endoplasmic reticulum of virtually every cell. Herein, we are reporting an updated systematic summary of the current knowledge on the functional role of ITPRs in human disorders. Specifically, we are describing the involvement of its loss-of-function and gain-of-function mutations in the pathogenesis of neurological, immunological, cardiovascular, and neoplastic human disease. Recent results from genome-wide association studies are also discussed.


Reproduction ◽  
2001 ◽  
pp. 839-846 ◽  
Author(s):  
K Swann ◽  
J Parrington ◽  
KT Jones

An increase in intracellular Ca2+ at fertilization is the trigger for egg activation in all species that have been studied. Exactly how sperm-egg interaction leads to this Ca2+ increase has not been established. There is increasing support for the hypothesis that the spermatozoon introduces a Ca2+-releasing protein into the egg cytoplasm after gamete membrane fusion. This review discusses the merits of this 'sperm factor' hypothesis and presents evidence indicating that the sperm factor, at least in mammals, consists of a phospholipase C with distinctive properties. This evidence leads us to propose that, after gamete fusion, a sperm-derived phospholipase C causes production of inositol 1,4,5- trisphosphate, which then generates Ca2+ waves from within the egg cytoplasm.


1994 ◽  
Vol 304 (3) ◽  
pp. 679-682 ◽  
Author(s):  
B Verjans ◽  
C C Petersen ◽  
M J Berridge

Ins(1,4,5)P3 3-kinase is a key enzyme in the regulation of Ins(1,4,5)P3. Overexpression of Ins(1,4,5)P3 3-kinase inhibited agonist-evoked and Ins(1,3,4,5)P4-evoked Ca2+ entry in Xenopus oocytes, but did not inhibit Ca2+ entry evoked by thapsigargin or non-metabolizable Ins(1,4,5)P3 analogues. The data suggest that Ins(1,4,5)P3 alone plays the crucial role in the activation of capacitative Ca2+ entry by emptying intracellular stores.


2005 ◽  
Vol 289 (3) ◽  
pp. C625-C632 ◽  
Author(s):  
Eamonn Bradley ◽  
Mark A. Hollywood ◽  
Noel G. McHale ◽  
Keith D. Thornbury ◽  
Gerard P. Sergeant

The aim of the present study was to investigate the properties and role of capacitative Ca2+ entry (CCE) in interstitial cells (IC) isolated from the rabbit urethra. Ca2+ entry in IC was larger in cells with depleted intracellular Ca2+ stores compared with controls, consistent with influx via a CCE pathway. The nonselective Ca2+ entry blockers Gd3+ (10 μM), La3+ (10 μM), and Ni2+ (100 μM) reduced CCE by 67% ( n = 14), 65% ( n = 11), and 55% ( n = 9), respectively. These agents did not inhibit Ca2+ entry when stores were not depleted. Conversely, CCE in IC was resistant to SKF-96365 (10 μM), wortmannin (10 μM), and nifedipine (1 μM). Spontaneous transient inward currents were recorded from IC voltage-clamped at −60 mV. These events were not significantly affected by Gd3+ (10 μM) or La3+ (10 μM) and were only slightly decreased in amplitude by 100 μM Ni2+. The results from this study demonstrate that freshly dispersed IC from the rabbit urethra possess a CCE pathway. However, influx via this pathway does not appear to contribute to spontaneous activity in these cells.


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