Title : Serine phosphorylation of glutathione S-transferase P1 (GSTP1) by PKCα enhances GSTP1-dependent cisplatin metabolism and resistance in human glioma cells.

Pub. Date : 2010 Nov 1

PMID : 20654585






15 Functional Relationships(s)
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Protein Name
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1 Serine phosphorylation of glutathione S-transferase P1 (GSTP1) by PKCalpha enhances GSTP1-dependent cisplatin metabolism and resistance in human glioma cells. Cisplatin glutathione S-transferase pi 1 Homo sapiens
2 Serine phosphorylation of glutathione S-transferase P1 (GSTP1) by PKCalpha enhances GSTP1-dependent cisplatin metabolism and resistance in human glioma cells. Cisplatin glutathione S-transferase pi 1 Homo sapiens
3 Serine phosphorylation of glutathione S-transferase P1 (GSTP1) by PKCalpha enhances GSTP1-dependent cisplatin metabolism and resistance in human glioma cells. Cisplatin glutathione S-transferase pi 1 Homo sapiens
4 In this study, we investigated the contribution of this post-translational modification of GSTP1 to tumor cisplatin resistance. Cisplatin glutathione S-transferase pi 1 Homo sapiens
5 Using two malignant glioma cell lines, MGR1 and MGR3, the ability of PKCalpha-phosphorylated GSTP1 to catalyze the conjugation of cisplatin to glutathione was assessed and correlated with cisplatin sensitivity and cisplatin-induced DNA interstrand cross-links and apoptosis of the cells. Cisplatin glutathione S-transferase pi 1 Homo sapiens
6 Using two malignant glioma cell lines, MGR1 and MGR3, the ability of PKCalpha-phosphorylated GSTP1 to catalyze the conjugation of cisplatin to glutathione was assessed and correlated with cisplatin sensitivity and cisplatin-induced DNA interstrand cross-links and apoptosis of the cells. Cisplatin glutathione S-transferase pi 1 Homo sapiens
7 Using two malignant glioma cell lines, MGR1 and MGR3, the ability of PKCalpha-phosphorylated GSTP1 to catalyze the conjugation of cisplatin to glutathione was assessed and correlated with cisplatin sensitivity and cisplatin-induced DNA interstrand cross-links and apoptosis of the cells. Cisplatin glutathione S-transferase pi 1 Homo sapiens
8 The results showed PKCalpha activation and associated phosphorylation of GSTP1 to correlate significantly with increased glutathionylplatinum formation, decreased DNA interstrand cross-link formation and increased cisplatin resistance. Cisplatin glutathione S-transferase pi 1 Homo sapiens
9 In both cell lines, siRNA-mediated GSTP1 or PKCalpha transcriptional suppression similarly decreased cisplatin IC(50) and was associated with decreased intracellular levels of glutathionylplatinum metabolite. Cisplatin glutathione S-transferase pi 1 Homo sapiens
10 Combined inhibition/transcriptional suppression of both PKCalpha and GSTP1 was synergistic in enhancing cisplatin sensitivity. Cisplatin glutathione S-transferase pi 1 Homo sapiens
11 Although, cisplatin-induced apoptosis was associated with the translocation of Bax to mitochondria, release of cytochrome c and caspase-3/7 activation, the levels of relocalized Bax and cytochrome c were significantly greater following GSTP1 knockdown. Cisplatin glutathione S-transferase pi 1 Homo sapiens
12 These results support a mechanism of cisplatin resistance mediated by the PKCalpha-dependent serine phosphorylation of GSTP1 and its associated increased cisplatin metabolism, and suggest the potential of simultaneous targeting of GSTP1 and PKCalpha to improve the efficacy of cisplatin therapy. Cisplatin glutathione S-transferase pi 1 Homo sapiens
13 These results support a mechanism of cisplatin resistance mediated by the PKCalpha-dependent serine phosphorylation of GSTP1 and its associated increased cisplatin metabolism, and suggest the potential of simultaneous targeting of GSTP1 and PKCalpha to improve the efficacy of cisplatin therapy. Cisplatin glutathione S-transferase pi 1 Homo sapiens
14 These results support a mechanism of cisplatin resistance mediated by the PKCalpha-dependent serine phosphorylation of GSTP1 and its associated increased cisplatin metabolism, and suggest the potential of simultaneous targeting of GSTP1 and PKCalpha to improve the efficacy of cisplatin therapy. Cisplatin glutathione S-transferase pi 1 Homo sapiens
15 These results support a mechanism of cisplatin resistance mediated by the PKCalpha-dependent serine phosphorylation of GSTP1 and its associated increased cisplatin metabolism, and suggest the potential of simultaneous targeting of GSTP1 and PKCalpha to improve the efficacy of cisplatin therapy. Cisplatin glutathione S-transferase pi 1 Homo sapiens