scholarly journals Overexpression of inositol 1,4,5-trisphosphate 3-kinase in Xenopus oocytes inhibits agonist-evoked capacitative calcium entry

1994 ◽  
Vol 304 (3) ◽  
pp. 679-682 ◽  
Author(s):  
B Verjans ◽  
C C Petersen ◽  
M J Berridge
Keyword(s):  
Crucial Role ◽  
Xenopus Oocytes ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Inositol 1,4,5 Trisphosphate ◽  
Key Enzyme

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.

scholarly journals Molecular cloning and immunolocalization of a novel vertebrate trp homologue from Xenopus

1999 ◽  
Vol 340 (3) ◽  
pp. 593-599 ◽  
Author(s):  
Laura K. BOBANOVIĆ ◽  
Mika LAINE ◽  
Carl C. H. PETERSEN ◽  
Deborah L. BENNETT ◽  
Michael J. BERRIDGE ◽  
...  
Keyword(s):  
Antisense Oligonucleotides ◽  
Xenopus Oocytes ◽  
Transient Receptor Potential ◽  
Polyclonal Antibodies ◽  
Sequence Similarity ◽  
Receptor Potential ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Sequence Structure ◽  
Transient Receptor

We report the sequence, structure and distribution of a novel transient receptor potential (trp) homologue from Xenopus, Xtrp, determined by screening an oocyte cDNA library. On the basis of sequence similarity and predicted structure, Xtrp appears to be a homologue of mammalian trp1 proteins. Two polyclonal antibodies raised against distinct regions of the Xtrp sequence revealed Xtrp expression in various Xenopus tissues, and the localization of Xtrp at the plasma membrane of Xenopus oocytes and HeLa cells. Since capacitative calcium entry into Xenopus oocytes has been shown previously to be substantially inhibited by trp1 antisense oligonucleotides [Tomita, Kaneko, Funayama, Kondo, Satoh and Akaike (1998) Neurosci. Lett. 248, 195-198] we suggest that Xtrp may underlie capacitative calcium entry in Xenopus tissues.

Caffeine exerts a dual effect on capacitative calcium entry in Xenopus oocytes

2000 ◽  
Vol 12 (1) ◽  
pp. 31-35 ◽  
Author(s):  
Frédéric Hague ◽  
Fabrice Matifat ◽  
Gérard Brûlé ◽  
Thibault Collin
Keyword(s):  
Xenopus Oocytes ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Dual Effect

scholarly journals Putative capacitative calcium entry channels: expression of Drosophila trp and evidence for the existence of vertebrate homologues

1995 ◽  
Vol 311 (1) ◽  
pp. 41-44 ◽  
Author(s):  
C C Petersen ◽  
M J Berridge ◽  
M F Borgese ◽  
D L Bennett
Keyword(s):  
Intracellular Calcium ◽  
Xenopus Oocytes ◽  
Transient Receptor Potential ◽  
Calcium Entry ◽  
Calcium Stores ◽  
Pcr Cloning ◽  
Capacitative Calcium Entry ◽  
Homologous Proteins ◽  
Major Pathway ◽  
Intracellular Calcium Stores

Capacitative calcium entry is a major pathway through which intracellular calcium stores are refilled after stimulation. It has been suggested that the protein encoded by the transient receptor potential (trp) gene expressed in Drosophila photoreceptors may be homologous with capacitative calcium entry channels. Expression of the trp gene product in Xenopus oocytes led to significant increases in calcium entry only when the intracellular calcium stores were depleted. Previous investigations have found trp to be uniquely expressed in Drosophila photoreceptors, but PCR cloning shows that homologous proteins exist in Calliphora, mouse brain and Xenopus oocytes. It is thus possible that capacitative calcium entry in Xenopus oocytes is mediated by a homologue of trp.

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 ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Calcium Current ◽  
Calcium Release ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Inositol 1,4,5 Trisphosphate

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

1995 ◽  
Vol 307 (3) ◽  
pp. 663-668 ◽  
Author(s):  
C C H Petersen ◽  
M J Berridge
Keyword(s):  
Protein Kinase ◽  
Xenopus Oocytes ◽  
Kinase Inhibitor ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Gtp Binding ◽  
Dependent Protein ◽  
Stimulation Of

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.

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