piperidines has been researched along with rottlerin* in 3 studies
3 other study(ies) available for piperidines and rottlerin
| Article | Year |
|---|---|
Ginsenoside Re Protects against Serotonergic Behaviors Evoked by 2,5-Dimethoxy-4-iodo-amphetamine in Mice via Inhibition of PKCδ-Mediated Mitochondrial Dysfunction.
It has been recognized that serotonin 2A receptor (5-HT Topics: Acetophenones; Amphetamines; Animals; Behavior, Animal; Benzopyrans; Ginsenosides; Hypothalamus; Male; Mice; Mice, Inbred C57BL; Mice, Knockout; Mitochondria; Oxidative Stress; Piperidines; Protein Kinase C-delta; Protein Kinase Inhibitors; Serotonin; Serotonin Antagonists; Serotonin Receptor Agonists; Serotonin Syndrome | 2021 |
The Group I Pak inhibitor Frax-1036 sensitizes 11q13-amplified ovarian cancer cells to the cytotoxic effects of Rottlerin.
The p21-activated kinases (PAKs) are Cdc42/Rac-activated serine-threonine protein kinases that regulate several key cancer-relevant signaling pathways, such as the Mek/Erk, PI3K/Akt, and Wnt/β-catenin cascades. Pak1 is frequently overexpressed and/or hyperactivated in different human cancers, including breast, ovary, prostate, and brain cancer. PAK1 genomic amplification at 11q13 is the most common mechanism of Pak1 hyperactivation, though Pak1 mRNA and/or protein may be overexpressed in the absence of gene amplification. In previous in vitro and in vivo studies we have shown that ovarian cancer cells with amplified/overexpressed Pak1 were significantly more sensitive to pharmacologic inhibition of Pak1 compared to cells without 11q13 amplification. In the present study we examined if additional signaling pathways might be targeted in tandem with the Group I Pak inhibitor Frax-1036 in ovarian cancer cells. Using the ICCB Known Bioactives Library, we found that the cytotoxic effect of Frax-1036 was significantly higher in combination with the PKCδ inhibitor, Rottlerin, suggesting that Pak inhibitors might be combined with other agents to treat 11q13-amplified ovarian cancer. Topics: Acetophenones; Benzopyrans; Cell Line, Tumor; Chromosomes, Human, Pair 11; Drug Synergism; Female; Humans; Ovarian Neoplasms; p21-Activated Kinases; Piperidines; Protein Kinase Inhibitors; Pyrazines; Pyrimidines; Signal Transduction | 2017 |
Isoform-selectivity of PKC inhibitors acting at the regulatory and catalytic domain of mammalian PKC-alpha, -betaI, -delta, -eta and -zeta.
The aim of the present study was to compare the potency of a series of widely used PKC inhibitors acting either at the regulatory (NPC 15437, tamoxifen and D-sphingosine) or at the catalytic domain (Ro 32-0432, chelerythrine and rottlerin) on individual mammalian PKC isoforms of the classical (alpha and betaI), novel (delta and eta) and atypical (zeta) PKC families, using the yeast phenotypic assay, in order to determine their isoform-selectivity. The PKC inhibitors studied presented differences in their ability to reduce the effect of the appropriate PKC activator (estimated as EC50 ratios) which was interpreted as an index of PKC inhibitory potency. In general, the more marked inhibition was observed on novel PKC isoforms, particularly on PKC-eta. This study indicates promising isoform-selectivity of some PKC inhibitors, namely NPC 15437 for PKC-eta or rottlerin for both novel PKC isoforms. It also suggests that the PKC domain involved in the inhibition does not seem to be relevant for the potency and isoform-selectivity of PKC inhibitors. Topics: Acetophenones; Alkaloids; Animals; Benzophenanthridines; Benzopyrans; Catalysis; Enzyme Inhibitors; Escherichia coli; Indoles; Isoenzymes; Phenanthridines; Piperidines; Protein Kinase C; Protein Kinase C beta; Protein Kinase C-alpha; Protein Kinase C-delta; Pyrroles; Saccharomyces cerevisiae; Sphingosine; Tamoxifen; Yeasts | 2003 |