Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-19772
Biochem J 1995 May 01;307 ( Pt 3):663-8.
Show Gene links Show Anatomy links

G-protein regulation of capacitative calcium entry may be mediated by protein kinases A and C in Xenopus oocytes.

Petersen CC , Berridge MJ .


???displayArticle.abstract???
Inositol 2,4,5-trisphosphate irreversibly activated capacitative calcium entry in Xenopus oocytes, whereas guanosine thiotriphosphate (GTP[S]) and AIF4- only activated capacitative calcium entry transiently. Both GTP[S] and AIF4- inhibited capacitative calcium entry activated by thapsigargin pretreatment, but guanosine thiodiphosphate (GDP[S]), inositol 2,4,5-trisphosphate and dibutyryl cyclic GMP did not affect capacitative calcium entry. This suggests the involvement of heterotrimeric GTP-binding proteins in the regulation of capacitative calcium entry. Activation of protein kinase C or cyclic-AMP-dependent protein kinase had profound effects on capacitative calcium entry, which were consistent with the hypothesis that the effects of GTP[S] and AIF4- on capacitative calcium entry may be mediated via heterotrimeric GTP-binding protein stimulation of kinases. Further evidence for this hypothesis was derived from the result that the effects of GTP[S] on calcium entry could be inhibited by the application of the protein kinase inhibitor staurosporine.

???displayArticle.pubmedLink??? 7741694
???displayArticle.pmcLink??? PMC1136702
???displayArticle.link??? Biochem J
???displayArticle.grants??? [+]


References [+] :
Bahnson, Cyclic GMP modulates depletion-activated Ca2+ entry in pancreatic acinar cells. 1993, Pubmed