Cch. Petersen et Mj. Berridge, G-PROTEIN REGULATION OF CAPACITATIVE CALCIUM-ENTRY MAY BE MEDIATED BYPROTEIN-KINASE-A AND PROTEIN-KINASE-C IN XENOPUS OOCYTES, Biochemical journal, 307, 1995, pp. 663-668
Inositol 2,4,5-trisphosphate irreversibly activated capacitative calci
um entry in Xenopus oocytes, whereas guanosine thiotriphosphate (GTP[S
]) and AlF4- only activated capacitative calcium entry transiently. Bo
th GTP[S] and AIF(4)(-) 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 heterotri
meric GTP-binding proteins in the regulation of capacitative calcium e
ntry. Activation of protein kinase C or cyclic-AMP-dependent protein k
inase had profound effects on capacitative calcium entry, which were c
onsistent with the hypothesis that the effects of GTP[S] and AlF4- on
capacitative calcium entry may be mediated via heterotrimeric GTP-bind
ing protein stimulation of kinases. Further evidence for this hypothes
is was derived from the result that the effects of GTP[S] on calcium e
ntry could be inhibited by the application of the protein kinase inhib
itor staurosporine.