Inositol 1,4,5-trisphosphate (IP3) receptor type1 (IP3R1) modulates the acquisition of cisplatin resistance in bladder cancer cell lines

Tsunoda, Toshiyuki; Koga, Hirofumi; Yokomizo, Akira; Tatsugami, Katsunori; Eto, Masatoshi; Inokuchi, Junichi; Hirata, Akira; Masuda, Katsuaki; Okumura, Koji; Naito, Seiji

doi:10.1038/sj.onc.1208313

Cited by 65 publications

(59 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Studies in DT40 and Jurkat cells have established that genetic ablation of IP 3 R isoforms induces resistance to apoptotic stimuli (9,29). In bladder cancer cell lines, the small interfering RNA-induced suppression of type I IP 3 R prevented apoptosis mediated by cisplatin (39). It has been generally assumed that these findings reflect a requirement for intracellular Ca 2ϩ release for one or more steps in the apoptotic cascade.…”

Section: Discussionmentioning

confidence: 98%

Akt Kinase Phosphorylation of Inositol 1,4,5-Trisphosphate Receptors

Khan

Wagner

Yule

et al. 2006

Journal of Biological Chemistry

138

107

View full text Add to dashboard Cite

Inositol 1,4,5-trisphosphate receptors (IP 3 R) 2 are a family of intracellular release channels that play an essential role in evoking Ca 2ϩ signals triggered by the occupation of numerous types of cell-surface receptors that are coupled to enhanced inositol-lipid turnover (1). Three different IP 3 R isoforms have been identified, and most cells appear to express multiple isoforms (2, 3). IP 3 receptors have been shown to be substrates for several different protein kinases in vivo and/or in vitro. These include protein kinase A (4, 5), protein kinase G (6, 7), protein kinase C (8), CaM kinase-II (8), Fyn tyrosine kinase (9, 10) and cdk1/CyB (11). By far the best-characterized of these effects are those of protein kinases A and G. Two serine residues have been identified as potential sites of phosphorylation in the type I IP 3 R isoform (12). Mutagenesis studies in a DT40 IP 3 R expression system suggest that both protein kinases A and G act to enhance IP 3 -mediated Ca 2ϩ release (13). However, the preferred sites of phosphorylation and functional effects on IP 3 R channel function may differ in different cell types and between alternatively spliced variants (6, 13-15). The regulatory role of the other protein kinases phosphorylating IP 3 Rs are poorly understood.The serine/threonine protein kinase Akt/protein kinase B is the cellular homologue of the viral oncogene v-Akt and is activated by various growth factors and cytokines. The membrane translocation and initial activation of the enzyme is dependent on the production of 3-phosphorylated inositol lipids catalyzed by PI 3-kinase. The activated Akt kinase then phosphorylates a number of key substrates involved in the stimulation of intermediary metabolism and promotion of cell survival, proliferation, and growth (reviewed in ). An examination of the sequence of all three IP 3 R isoforms indicates the presence of a consensus RXRXX(S/T) sequence for phosphorylation by Akt kinase (19). In the present study, we have shown for the first time that IP 3 Rs are substrates for activated Akt kinase in vivo and have investigated several possible functional consequences of this phosphorylation on Ca 2ϩ signaling.

show abstract

Section: Discussionmentioning

confidence: 98%

Akt Kinase Phosphorylation of Inositol 1,4,5-Trisphosphate Receptors

Khan

Wagner

Yule

et al. 2006

Journal of Biological Chemistry

138

107

View full text Add to dashboard Cite

show abstract

“…the procedure of cDnA microarray analysis was performed as described previously (18). Briefly, cDNA generation, hybridization, and data collection for cDnA microarray analyses were performed by the Incyte corporation (palo Alto, cA, UsA).…”

Section: Methodsmentioning

confidence: 99%

Ectonucleoside triphosphate diphosphohydrolase 6 expression in testis and testicular cancer and its implication in cisplatin resistance

Tada

Yokomizo

Shiota³

et al. 2011

Oncol Rep

Self Cite

View full text Add to dashboard Cite

Abstract. the development of resistance to cisplatin during treatment of testicular cancer constitutes a major obstacle to the cure of testicular cancer. to resolve its mechanism will provide useful information for making clinical decisions. We found 4 and 15 gene expressions were, respectively, up-regulated and down-regulated in cisplatin-resistant testicular cancer nec-8/DDp cells compared with their parental nec-8 cells (about 2.5-fold) using cDnA microarray analysis. After screening, we selected the entpD6 among these 19 genes. entpD6 was less expressed in cancerous region compared with that in non-cancerous lesion. In addition, entpD6 expression in seminoma was higher than that in other testicular tumors. entpD6 expression was involved in cellular sensitivity to cisplatin through an interaction with e-cadherin. entpD6 is a promising molecular biomarker of cisplatin resistance in testicular cancer, and also a novel therapeutical target modulating cisplatin resistance in testicular cancer.

show abstract

“…We have been investigating mechanisms of a resistance to anticancer drug and aiming to overcome anticancer-drug resistance (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11). We previously established doxorubicin-resistant cells of urothelial cancer (4).…”

Section: Resultsmentioning

confidence: 99%

“…Although anticancer agents decrease patient tumor burdens and expand life expectancy, nonresponsiveness or development of chemotherapy resistance are major obstacles for effective cancer treatment. We have previously investigated mechanisms of resistance to anticancer drugs including cisplatin, vincristine, etoposide and doxorubicin (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11). Doxorubicin has been administered for many types of solid tumors including breast cancer, hepatocellular cancer and urothelial cancer.…”

Section: Introductionmentioning

confidence: 99%