Compounds > sphingosine-phosphorylcholine

sphingosine-phosphorylcholine and pyrazolanthrone

sphingosine-phosphorylcholine has been researched along with pyrazolanthrone* in 1 studies

Other Studies

1 other study(ies) available for sphingosine-phosphorylcholine and pyrazolanthrone

Article	Year
Novel participation of transglutaminase-2 through c-Jun N-terminal kinase activation in sphingosylphosphorylcholine-induced keratin reorganization of PANC-1 cells. Biochimica et biophysica acta, 2011, Volume: 1811, Issue:12 Sphingosylphosphorylcholine (SPC) is found at increased levels in the malignant ascites of tumor patients and induces perinuclear reorganization of keratin 8 (K8) filaments that contribute to the viscoelasticity of metastatic cancer cells. In this study, we investigated the role and molecular mechanisms of Tgase-2 in SPC-induced K8 phosphorylation and perinuclear reorganization in PANC-1 cells (PAN(WT)), and in PANC-1 cells that stably expressed shTgase-2 or Tgase-2 (PAN(shTg2) and PAN(Tg2)). SPC induces the expression of Tgase-2 in a time- and dose-dependent manner. Gene silencing of Tgase-2 or cystamine suppressed the SPC-induced phosphorylation and perinuclear reorganization of K8 and suppressed the SPC-induced migration of PANC-1 cells. An inhibitor of c-Jun N-terminal kinase (JNK), SP600125, suppressed the SPC-induced phosphorylation of serine 431 in K8 and keratin reorganization. Next, we examined the effect of Tgase-2 on JNK activation of serine 431 phosphorylation in K8. Tgase-2 gene silencing suppressed the expression of active form JNK (pJNK). Constitutive or tetracyclin-induced conditional expression of Tgase-2 increased the levels of pJNK. Tgase-2 was coimmunoprecipitated with K8 and JNK. In addition, K8 was coimmunoprecipitated with Tgase-2 and JNK. JNK was also coimmunoprecipitated with K8 and Tgase-2. Overall, these results suggest that Tgase-2 is involved in SPC-induced phosphorylation and perinuclear reorganization of K8 by activating JNK and forming a triple complex with K8 and JNK. Therefore, SPC-induced Tgase-2 might be a new target for modulating keratin reorganization, metastasis of cancer cells and JNK activation. Topics: Anthracenes; Cell Line, Tumor; Cell Movement; Cystamine; Cytoskeleton; Gene Expression Regulation, Neoplastic; Gene Silencing; GTP-Binding Proteins; Humans; Immunoprecipitation; JNK Mitogen-Activated Protein Kinases; Keratin-8; MAP Kinase Signaling System; Pancreatic Neoplasms; Phosphorylation; Phosphorylcholine; Protein Glutamine gamma Glutamyltransferase 2; Protein Kinase Inhibitors; RNA, Small Interfering; Serine; Sphingosine; Transglutaminases	2011

Article

Year

Novel participation of transglutaminase-2 through c-Jun N-terminal kinase activation in sphingosylphosphorylcholine-induced keratin reorganization of PANC-1 cells.

Biochimica et biophysica acta, 2011, Volume: 1811, Issue:12

Sphingosylphosphorylcholine (SPC) is found at increased levels in the malignant ascites of tumor patients and induces perinuclear reorganization of keratin 8 (K8) filaments that contribute to the viscoelasticity of metastatic cancer cells. In this study, we investigated the role and molecular mechanisms of Tgase-2 in SPC-induced K8 phosphorylation and perinuclear reorganization in PANC-1 cells (PAN(WT)), and in PANC-1 cells that stably expressed shTgase-2 or Tgase-2 (PAN(shTg2) and PAN(Tg2)). SPC induces the expression of Tgase-2 in a time- and dose-dependent manner. Gene silencing of Tgase-2 or cystamine suppressed the SPC-induced phosphorylation and perinuclear reorganization of K8 and suppressed the SPC-induced migration of PANC-1 cells. An inhibitor of c-Jun N-terminal kinase (JNK), SP600125, suppressed the SPC-induced phosphorylation of serine 431 in K8 and keratin reorganization. Next, we examined the effect of Tgase-2 on JNK activation of serine 431 phosphorylation in K8. Tgase-2 gene silencing suppressed the expression of active form JNK (pJNK). Constitutive or tetracyclin-induced conditional expression of Tgase-2 increased the levels of pJNK. Tgase-2 was coimmunoprecipitated with K8 and JNK. In addition, K8 was coimmunoprecipitated with Tgase-2 and JNK. JNK was also coimmunoprecipitated with K8 and Tgase-2. Overall, these results suggest that Tgase-2 is involved in SPC-induced phosphorylation and perinuclear reorganization of K8 by activating JNK and forming a triple complex with K8 and JNK. Therefore, SPC-induced Tgase-2 might be a new target for modulating keratin reorganization, metastasis of cancer cells and JNK activation.

Topics: Anthracenes; Cell Line, Tumor; Cell Movement; Cystamine; Cytoskeleton; Gene Expression Regulation, Neoplastic; Gene Silencing; GTP-Binding Proteins; Humans; Immunoprecipitation; JNK Mitogen-Activated Protein Kinases; Keratin-8; MAP Kinase Signaling System; Pancreatic Neoplasms; Phosphorylation; Phosphorylcholine; Protein Glutamine gamma Glutamyltransferase 2; Protein Kinase Inhibitors; RNA, Small Interfering; Serine; Sphingosine; Transglutaminases

2011