Academic literature on the topic 'Rottlerin'
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Journal articles on the topic "Rottlerin"
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Chen, Xu‐Ling, Yu Dong, and Ji‐Yu Wang. "The Practical Total Synthesis of Rottlerin and Rottlerone." ChemistrySelect 5, no. 29 (August 4, 2020): 9206–9. http://dx.doi.org/10.1002/slct.202002245.
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Kim, Hyun Kyung, Eun Young Kang, and Gwang-woong Go. "Rottlerin, a Polyphenolic Compound, Alleviate Body Adiposity by Enhancing Lipolysis and Thermogenesis in Diet-Induced Obesity Mice." Current Developments in Nutrition 5, Supplement_2 (June 2021): 1222. http://dx.doi.org/10.1093/cdn/nzab055_032.
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Abstract Objectives Rottlerin (mallotoxin) is a polyphenolic compound in Mallotus philippensis. The anti-tumor, anti-inflammation, and mitochondrial uncoupling regulation effects of rottlerin have been known. However, the anti-obesity effect was not reported yet. Thus, we hypothesized that rottlerin would suppress body fat accumulation in obesity-induced mice. Methods Five-week-old male C57BL/6 mice were fed a high-fat diet (HFD) (60% kcal from fat) ad libitum for 8 weeks. Mice were randomly assigned to five groups as follows: 1) normal diet (18% kcal from fat), 2) negative control (60% kcal from fat), 3) rottlerin 10 (HFD + rottlerin 10 mg/kg bw), 4) rottlerin 20 (HFD + 20 mg/kg bw), 5) positive control (HFD + metformin 150 mg/kg bw). Rottlerin was daily supplemented by oral gavage. Body weight and feed intake were measured each week. Results Body weight and weight gain were reduced in rottlerin 20 compared to the control (P < 0.001). Body fat mass was also significantly decreased by rottlerin (P < 0.05). Total feed intake and lean mass were similar among HFD groups. Furthermore, energy expenditure was dose-dependently facilitated by rottlerin. RNA-sequencing results supported these findings that rottlerin 20 up-regulated fatty acid beta-oxidation, heat generation, and brown cell differentiation in white-adipose tissues. Rottlerin promoted a catabolic pathway such as lipolysis, thermogenesis, and oxidation in white adipose tissues. Moreover, non-esterified fatty acid levels were decreased by rottlerin (P < 0.05), and hepatic triglyceride contents tended to decline in rottlerin 20 without hepatotoxicity. Non-shivering thermogenesis enzymes, PRDM16 (P = 0.06) and UCP1 (P < 0.01), were stimulated by rottlerin. Conclusions Rottlerin supplementation altered body adiposity accumulation via enhancing fat utilization, lipolysis, and thermogenesis in obese mice. We suggest that rottlerin is a potent nutraceutical for anti-obesity. Funding Sources This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (Ministry of Science and ICT; MSIT).
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Shivshankar, Pooja, Lei Lei, Jie Wang, and Guangming Zhong. "Rottlerin Inhibits Chlamydial Intracellular Growth and Blocks Chlamydial Acquisition of Sphingolipids from Host Cells." Applied and Environmental Microbiology 74, no. 4 (December 14, 2007): 1243–49. http://dx.doi.org/10.1128/aem.02151-07.
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ABSTRACT We report that rottlerin, a plant-derived compound known to inhibit various mammalian kinases, profoundly inhibited chlamydial growth in cell culture with a minimal inhibition concentration of 1 μM. The inhibition was effective even when rottlerin was added as late as the middle stage of chlamydial infection cycle, against multiple Chlamydia species, and in different host cell lines. Pretreatment of host cells with rottlerin prior to infection also blocked chlamydial growth, suggesting that rottlerin targets host factors. Moreover, rottlerin did not alter the chlamydial infection rate and did not directly target chlamydial protein synthesis and secretion. The rottlerin-mediated inhibition of chlamydial replication and inclusion expansion correlated well with the rottlerin-induced blockade of host cell sphingolipid trafficking from the Golgi apparatus into chlamydial inclusions. These studies not only allowed us to identify a novel antimicrobial activity for rottlerin but also allowed us to uncover a potential mechanism for rottlerin inhibition of chlamydial growth.
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Kim, Ye Jin, and Gwang-woong !Go. "Rottlerin Suppresses Fat Accumulation by Inhibiting Adipogenesis and De Novo Lipogenesis in 3T3-L1 Adipocytes." Current Developments in Nutrition 5, Supplement_2 (June 2021): 1224. http://dx.doi.org/10.1093/cdn/nzab055_034.
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Abstract Objectives Rottlerin is isolated from Mallotus japonicus, a rich-in polyphenol. Rottlerin is a PKC delta inhibitor known for an uncoupler of oxidative phosphorylation and anti-neoplastic agent. However, the effect of anti-obesity is not conclusive. This study hypothesized that rottlerin inhibits lipid accumulation in adipocytes. Methods 3T3-L1 cells were maintained with DMEM containing 10% BCS and 1% penicillin. The cells were seeded in a 6-well plate with a density of 8 × 104 followed by cultured for 4 days until reaching 120% confluency and incubated in a differentiation medium for 6 days. Rottlerin was incubated with differentiation media (0, 1, 2, and 4 µM). Cells were harvested after treatment for measurement of Oil Red O stating, immunoblotting, and RT-PCR. Results Differentiated 3T3-L1 adipocytes were stained using the Oil Red O, which stains triglycerides into the red. Lipid accumulation was significantly inhibited in 4 µM of rottlerin (P < 0.001). In protein levels, PPARγ, an adipogenesis marker, was reduced dose-dependently decreased (P < 0.001), indicating lipid droplet formation reduced. FAS and SCD1 were diminished by rottlerin treated groups (all P < 0.001). ACC-pS79/ACC was increased by rottlerin (P = 0.02). In mRNA gene expressions, C/EBPα was reduced by rottlerin in a dose-dependent manner (P < 0.001), and PPARγ tend to be decreased by rottlerin (P = 0.06). FAS and SREBP1 were inhibited by rottlerin (P < 0.01). SCD1 was dramatically reduced by rottlerin (P < 0.001). Conclusions We found that rottlerin reduces lipid accumulation by inhibiting adipogenesis in differentiated 3T3-L1 adipocytes. This suggests that rottlerin is a potential nutraceutical for treating dyslipidemia, non-alcoholic fatty liver disease, and obesity. Funding Sources This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (Ministry of Science and ICT; MSIT).
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Ohno, Izumi, Guido Eibl, Irina Odinokova, Mouad Edderkaoui, Robert D. Damoiseaux, Moussa Yazbec, Ravinder Abrol, et al. "Rottlerin stimulates apoptosis in pancreatic cancer cells through interactions with proteins of the Bcl-2 family." American Journal of Physiology-Gastrointestinal and Liver Physiology 298, no. 1 (January 2010): G63—G73. http://dx.doi.org/10.1152/ajpgi.00257.2009.
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Rottlerin is a polyphenolic compound derived from Mallotus philipinensis . In the present study, we show that rottlerin decreased tumor size and stimulated apoptosis in an orthotopic model of pancreatic cancer with no effect on normal tissues in vivo. Rottlerin also induced apoptosis in pancreatic cancer (PaCa) cell lines by interacting with mitochondria and stimulating cytochrome c release. Immunoprecipitation results indicated that rottlerin disrupts complexes of prosurvival Bcl-xL with Bim and Puma. Furthermore, siRNA knockdown showed that Bim and Puma are necessary for rottlerin to stimulate apoptosis. We also showed that rottlerin and Bcl-2 and Bcl-xL inhibitor BH3I-2′ stimulate apoptosis through a common mechanism. They both directly interact with mitochondria, causing increased cytochrome c release and mitochondrial depolarization, and both decrease sequestration of BH3-only proteins by Bcl-xL. However, the effects of rottlerin and BH3I-2′ on the complex formation between Bcl-xL and BH3-only proteins are different. BH3I-2′ disrupts complexes of Bcl-xL with Bad but not with Bim or Puma, whereas rottlerin had no effect on the Bcl-xL interaction with Bad. Also BH3I-2′, but not rottlerin, required Bad to stimulate apoptosis. In conclusion, our results demonstrate that rottlerin has a potent proapoptotic and antitumor activity in pancreatic cancer, which is mediated by disrupting the interaction between prosurvival Bcl-2 proteins and proapoptotic BH3-only proteins. Thus rottlerin represents a promising novel agent for pancreatic cancer treatment.
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Maioli, Emanuela, Lucedio Greci, Karel Soucek, Martina Hyzdalova, Alessandra Pecorelli, Vittoria Fortino, and Giuseppe Valacchi. "Rottlerin Inhibits ROS Formation and Prevents NFκB Activation in MCF-7 and HT-29 Cells." Journal of Biomedicine and Biotechnology 2009 (2009): 1–7. http://dx.doi.org/10.1155/2009/742936.
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Rottlerin, a polyphenol isolated from Mallotus Philippinensis, has been recently used as a selective inhibitor of PKCδ, although it can inhibit many kinases and has several biological effects. Among them, we recently found that Rottlerin inhibits the Nuclear FactorκB (NFκB), activated by either phorbol esters orH2O2. Because of the redox sensitivity of NFκB and on the basis of Rottlerin antioxidant property, we hypothesized that Rottlerin could prevent NFκB activation acting as a free radicals scavenger, as other natural polyphenols. The current study confirms the antioxidant property of Rottlerin against the 2,2-diphenyl-1-picrylhydrazyl radical (DPPH) in vitro and against oxidative stress induced byH2O2and by menadione in culture cells. We also demonstrate that Rottlerin prevents TNFα-dependent NFκB activation in MCF-7 cells and in HT-29 cells transfected with the NFκB-driven plasmid pBIIX-LUC, suggesting that Rottlerin can inhibit NFκB via several pathways and in several cell types.
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Molina, Yessenia L., David García-Seisdedos, Bohdan Babiy, Milagros Lerma, Javier Martínez-Botas, María J. Casarejos, María T. Vallejo, et al. "Rottlerin Stimulates Exosome/Microvesicle Release Via the Increase of Ceramide Levels Mediated by Ampk in an In Vitro Model of Intracellular Lipid Accumulation." Biomedicines 10, no. 6 (June 3, 2022): 1316. http://dx.doi.org/10.3390/biomedicines10061316.
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Exosomes/microvesicles originate from multivesicular bodies that allow the secretion of endolysosome components out of the cell. In the present work, we investigated the effects of rottlerin, a polyphenol, on exosome/microvesicle secretion in a model of intracellular lipid trafficking impairment, and elucidated the mechanism of action. In a model of lipid trafficking impairment in C6 glia cells, rottlerin increased ceramide levels, while decreasing hexosylceramide content. This was accompanied by increased exosome/microvesicle secretion, thereby reducing the concentration of lipids in the endolysosomal compartment. The reduction of hexosylceramide levels by rottlerin was attributed to the increase of β-glucosidase (glucosylceramidase) activity, and the effects of rottlerin were abrogated by β-glucosidase inhibitors such as isofagomine D-tartrate and AMP-deoxynojirimycin. Moreover, treatment with ML-266, a potent activator of the β-glucosidase enzyme, recapitulated the effects of rottlerin on the sphingolipid profile and exosome/microvesicle secretion. Finally, inhibition of AMPK (AMP-activated protein kinase) using compound C prevented both exosome/microvesicle secretion and the elimination of endolysosome lipids, which were promoted by rottlerin. The results showed that the decrease in intracellular lipid deposition induced by rottlerin was mediated by β-glucosidase activation and exosome/microvesicle release via the AMPK pathway. Rottlerin consumption could represent an additional health benefit in lysosomal deposition diseases.
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Mischitelli, Morena, Mohamed Jemaà, Mustafa Almasry, Caterina Faggio, and Florian Lang. "Stimulation of Suicidal Erythrocyte Death by Rottlerin." Cellular Physiology and Biochemistry 40, no. 3-4 (2016): 558–66. http://dx.doi.org/10.1159/000452569.
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Background/Aims: The phytochemical polyphenol rottlerin is a potent activator of diverse Ca2+ -sensitive K+ channels. Those channels play a decisive role in the execution of eryptosis, the suicidal death of erythrocytes, which is characterized by cell shrinkage and cell membrane scrambling with phosphatidylserine translocation to the erythrocyte surface. Signaling involved in the stimulation of eryptosis includes increase of cytosolic Ca2+ activity ([Ca2+]i) and ceramide. The present study explored, whether rottlerin induces eryptosis and, if so, to test for the involvement of Ca2+ entry and ceramide. Methods: Flow cytometry was employed to estimate phosphatidylserine exposure at the cell surface from annexin-V-binding, cell volume from forward scatter, [Ca2+]i from Fluo3-fluorescence, and ceramide abundance utilizing specific antibodies. Hemolysis was quantified by determination of haemoglobin concentration in the supernatant. Results: A 48 hours exposure of human erythrocytes to rottlerin (1 - 5 µM) significantly increased the percentage of annexin-V-binding cells, an effect paralleled by significant decrease of forward scatter. Up to 5 µM rottlerin failed to significantly increase average Fluo3-fluorescence. Rottlerin (5 µM) did, however, significantly increase the ceramide abundance. Rottlerin (5 µM) further significantly increased hemolysis. The effect of rottlerin (5 µM) on annexin-V-binding was virtually abolished by removal of extracellular Ca2+. Conclusions: Rottlerin stimulates eryptosis with erythrocyte shrinkage and phospholipid scrambling of the erythrocyte cell membrane, an effect paralleled by and at least in part due to Ca2+ entry and ceramide.
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Matschke, Veronika, Ilaria Piccini, Janina Schubert, Eva Wrobel, Florian Lang, Johann Matschke, Elsie Amedonu, et al. "The Natural Plant Product Rottlerin Activates Kv7.1/KCNE1 Channels." Cellular Physiology and Biochemistry 40, no. 6 (2016): 1549–58. http://dx.doi.org/10.1159/000453205.
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Background/Aims: Acquired as well as inherited channelopathies are disorders that are caused by altered ion channel function. A family of channels whose malfunction is associated with different channelopathies is the Kv7 K+ channel family; and restoration of normal Kv7 channel function by small molecule modulators is a promising approach for treatment of these often fatal diseases. Methods: Here, we show the modulation of Kv7 channels by the natural compound Rottlerin heterologously expressed in Xenopus laevis oocytes and on iPSC cardiomyocytes overexpressing Kv7.1 channels. Results: We show that currents carried by Kv7.1 (EC50 = 1.48 μM), Kv7.1/KCNE1 (EC50 = 4.9 μM), and Kv7.4 (EC50 = 0.148 μM) are strongly enhanced by the compound, whereas Kv7.2, Kv7.2/Kv7.3, and Kv7.5 are not sensitive to Rottlerin. Studies on Kv7.1/KCNE1 mutants and in silico modelling indicate that Rottlerin binds to the R-L3-activator site. Rottlerin mediated activation of Kv7.1/KCNE1 channels might be a promising approach in long QT syndrome. As a proof of concept, we show that Rottlerin shortens cardiac repolarisation in iPSC-derived cardiomyocytes expressing Kv7.1.Conclusion: Rottlerin or an optimized derivative holds a potential as QT interval correcting drug.
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Klinger, James R., Josh D. Murray, Brian Casserly, Diego F. Alvarez, Judy A. King, Steven S. An, Gaurav Choudhary, Akua N. Owusu-Sarfo, Rod Warburton, and Elizabeth O. Harrington. "Rottlerin causes pulmonary edema in vivo: a possible role for PKCδ." Journal of Applied Physiology 103, no. 6 (December 2007): 2084–94. http://dx.doi.org/10.1152/japplphysiol.00695.2007.
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In the present study, we assessed the effects of chemical inhibitors shown to be selective for protein kinase C (PKC) isoforms on lung barrier function both in vitro and in vivo. Rottlerin, a purported inhibitor of PKCδ, but not other chemical inhibitors, dose dependently promoted barrier dysfunction in lung endothelial cells in vitro. This barrier dysfunction correlated with structural changes in focal adhesions and stress fibers, which were consistent with functional changes in cell stiffness. To determine whether the effects noted in vitro correlated with changes in intact lungs, we tested the effects of rottlerin in the formation of pulmonary edema in rats using both ex vivo and in vivo models. Isolated, perfused lungs demonstrated a significant increase in filtration coefficients on exposure to rottlerin, compared with vehicle-treated lungs, an effect that correlated with increased extravasation of Evan's blue dye (EBD)-conjugated albumin. Additionally, compared with vehicle, the ratio of the wet lung weights to dry lung weights was significantly greater on exposure of animals to rottlerin; rottlerin also produced a dose-dependent increase in EBD extravasation into the lungs. These effects on lung edema occurred without any increase in right ventricular pressures. Microscopic assessment of edema in the ex vivo lungs demonstrated perivascular cuffing, with no evidence of septal capillary leak, in rottlerin-exposed lungs. Taken together, rottlerin increases barrier dysfunction in pulmonary endothelial cell monolayers and causes pulmonary edema in rats; results suggestive of an important role for PKCδ in maintaining lung endothelial barrier function.
Dissertations / Theses on the topic "Rottlerin"
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Lama, Zoé. "Étude fonctionnelle d'inhibiteurs de kinases réprimant la réplication du virus de la rage." Thesis, Université Paris-Saclay (ComUE), 2017. http://www.theses.fr/2017SACLS490.
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Alors que les étapes du cycle du virus de la rage sont plutôt bien décrites, les interactions du virus avec la machinerie cellulaire restent mal connues. Le but de ce projet de thèse a été d’identifier et caractériser les voies de signalisation cellulaires impliquées dans le déroulement du cycle viral. Les kinases cellulaires jouent un rôle majeur dans la régulation de ces voies et certaines protéines rabiques ont déjà été décrites comme cibles de ces enzymes. Afin d’identifier les kinases impliquées dans le déroulement du cycle viral, nous avons réalisé un criblage d’une banque d’inhibiteur de kinases. L’analyse a été effectuée par cytométrie en flux dans des cellules infectées avec un virus rabique recombinant exprimant la protéine fluorescente GFP. Nous avons ainsi pu isoler deux inhibiteurs de kinases bloquant l’infection : La Tyrphostin 9,un inhibiteur de l’autophosphorylation du récepteur au PDGF (platelet-derived growth factor) (PDGF.R), et la Rottlerin, un inhibiteur de la PKCδ et découplant mitochondrial. Nous avons confirmé leur activité anti-virale dans différents types cellulaires (fibroblaste, glioblastome,neuroblastome et neurones primaires) et sur deux souches rabiques (CVS et SAD-B19). Par diverses approches expérimentales, nous avons identifié l’étape du cycle viral ciblée par chacun de ces inhibiteurs. Les résultats obtenus montrent que la Tyrphostin 9 perturbe une étape très précoce de l’infection : la fusion virale et plus particulièrement l’acidification endosomale. Nous avons observé que la Tyrphostin 9 provoquait également une désagrégation de l’appareil de Golgi. L’inhibition de l’acidification endosomale pourrait donc découler de cet effet. En présence de Rottlerin, le cycle viral est également inhibé au niveau d’une étape précoce : la réplication. A l’aide de siRNA, nous avons montré que cet effet de la Rottlerin est indépendant de la PKCδ. Les expériences réalisées avec un découplant mitochondrial bien caractérisé, le CCCP, tendent à montrer que l’effet de la Rottlerin est dû à sa fonction de découplant mitochondrial, qui induit une diminution du niveau d’ATP intracellulaire. Ce travail a permis d’identifier deux inhibiteurs de kinases inhibant des étapes précoces du cycle rabique. Les cibles cellulaires précisément impactées ainsi que l’effet sur le fonctionnement cellulaire lors de l’infection virale restent à déterminer. Des études in vivo pourraient valider leur utilisation en tant qu’agents antivirauxHowever the rabies viral cycle is fairly well described, the interactions with the cellular machinery are not. This thesis project aimed at identifying and characterizing the cellular signaling pathways involved in the establishment and progress of the viral cycle through the study of cellular kinases. Indeed, kinases are the main actors of these pathways and their effects on certain rabies proteins have already been reported. In order to identify kinases involved in the viral cycle, we screened a kinase inhibitor library for anti-viral activity using a recombinant rabies virus expressing the GFP fluorescent protein. This assay allowed us to isolate two kinase inhibitors that block rabies virus infection: Tyrphostin 9, an inhibitor of the receptor tyrosine kinase platelet-derived growth factor receptor (PDGF.R), and Rottlerin, a PKCδ inhibitor and mitochondrial uncoupler. We confirmed their anti-viral action in different cell types (fibroblast, glioblastoma, neuroblastoma, as well as primary neurons) and on different rabies strains (CVS and SAD-B19). Using various experimental approaches, we found that each inhibitor impairs an early stage of the viral cycle: the viral fusion and more specifically the endosomal acidification by Tyrphostin 9 and the viral replication step by Rottlerin. We observed that Tyrphostin 9 also caused disintegration of the Golgi apparatus. The inhibition of endosomal acidification could therefore result from this effect. Seeking for the mechanisms involved in Rottlerin’s effect, we evidenced that it is independent of PKCδ. Experiments with a well characterized mitochondrial uncoupler (CCCP), revealed that the Rottlerin anti-viral effect is rather due to its mitochondrial uncoupling function, which leads to a decrease of the cellular ATP level. This study allowed the identification of two kinase inhibitors with anti-viral effects acting on early stages of the rabies cycle. The cellular targets as well as the effect on the cellular functions during viral infection remain to be determined. In vivo studies could validate their use in therapeutics as anti-rabies agents
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Sivanathan, Sivatharushan [Verfasser]. "Synthese enantiomerenreiner α-Hydroxycarbonsäuren, neuer Cyclooctadepsipeptide sowie Studien zur Totalsynthese von Rottlerin / Sivatharushan Sivanathan." Wuppertal : Universitätsbibliothek Wuppertal, 2015. http://d-nb.info/1076930166/34.
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Heineck, Lukas [Verfasser], and Christian [Akademischer Betreuer] Kurts. "Der Einfluss von Rottlerin auf T-Zellpräsentation und -aktivierung / Lukas Heineck ; Betreuer: Christian Kurts." Marburg : Philipps-Universität Marburg, 2019. http://d-nb.info/1199537519/34.
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Juneja, Manisha. "Novel insights into MACC1 transcriptional regulation for identifying small molecule MACC1 inhibitors to restrict colorectal cancer progression." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://dx.doi.org/10.18452/17038.
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MACC1 wurde als prognostischer Biomarker für die Tumorprogression und das Metastasen-freie Überleben im KRK sowie in anderen soliden Tumoren beschrieben. Das Gen induziert Zellmotilität und Proliferation in Zellkultur sowie die Metastasierung im Mausmodell. Damit stellt MACC1 ein vielversprechendes Ziel für die Intervention bei Tumorprogression und –metastasierung und damit für die Behandlung von KRK-Patienten dar. Unser Ziel war es, die Transkription von MACC1 zu inhibieren. Hierfür identifizierten wir zunächst die Promoter-Region von MACC1 und untersuchten MACC1s transkriptionelles Regulationsnetzwerk. Durch ortsgerichtete Mutagenese, Chromatin Immunopräzipitation und Electrophoretic Mobility Shift Assay ermittelten wir, dass Transkriptionsfaktoren wie Ap-1, Sp1, C/EBPs und GIPC1 an den MACC1-Promoter binden und die Transkription des MACC1-Gens kontrollieren. Darüberhinaus konnten wir durch Hochdurchsatz-Screening die bisher ersten Inhibitoren gegen MACC1 identifizieren: Rottlerin und Lovastatin. Wir zeigten, dass diese spezifisch auf den endogenen MACC1-Promoter wirken, was eine zeit- und konzentrationsabhängige Reduktion der MACC1-Expression zur Folge hatte. Beide Inhibitoren begrenzten das Expressionsniveau von Sp1 und interferierten mit der Bindung von c-Jun mit dem MACC1-Promoter, was in einer Inhibition der MACC1-Transkription resultierte. Ferner führte die tägliche Behandlung von Xenograft-Mausmodellen mit Rottlerin zu einer Inhibition der MACC1-Expression im Primärtumor und einer damit einhergehenden Begrenzung des Tumorwachstums. Zusammenfassend lässt sich festhalten, dass in der vorliegenden Arbeit zum ersten Mal der MACC1-Promoter und seine transkriptionelle Regulation beleuchtet wurden. Die neuen Erkenntnisse wurden zur Identifizierung der ersten Inhibitoren gegen MACC1 genutzt. Zur Behandlung von KRK-Patienten mit einem hohen Risiko für MACC1-induzierte Metastasierung könnten diese Inhibitoren Potential für die klinische Anwendung beherbergen.MACC1 has been reported as a prognostic biomarker for tumor progression and metastasis-free survival in CRC along with other solid tumors. It induces cell motility and proliferation in cell culture and metastasis in mouse models. Consequently, targeting MACC1 to intervene in tumor progression and metastasis formation holds a promising approach to treat CRC patients. We designed a strategy to inhibit MACC1 via targeting its transcription. We first identified MACC1 gene promoter by creating various promoter-luciferase constructs. We then established that transcription factors such as Ap-1, Sp1, C/EBPs and GIPC1 bind to the MACC1 promoter and govern MACC1 transcription, expression and thus motility in vitro and in CRC patients. Using a high throughput screening targeting the MACC1 promoter, we identified small molecule MACC1 inhibitors, Rottlerin and Lovastatin. These inhibitors specifically restricted endogenous MACC1 promoter leading to reduced MACC1 expression in a time- and concentration-dependent manner. In vitro functional assays demonstrated the impact of the small molecule inhibitors on retarding cell proliferation and motility. Both inhibitors restricted Sp1 levels and interfered with the binding of c-Jun to the MACC1 promoter, thereby inhibiting MACC1 transcription. The study further described the effect of Rottlerin on a CRC-xenografted mouse model. Daily treatment of xenografted mice with Rottlerin resulted in the inhibition of MACC1 expression in the primary tumor accompanied with the restricted tumor growth. To summarize, this is the first study unraveling the MACC1 promoter, its transcriptional regulation and identification of newly identified MACC1 inhibitors. In clinical settings, inhibition of MACC1 expression using these inhibitors might provide immense potential for the treatment of CRC patients who are at high risk for MACC1-induced metastasis linked to shorter survival.
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Cordeiro, Thuany de Moura. "Efeitos da rottlerin na esquizogonia eritrocitária de Plasmodium falciparum e implementação e avaliação de teste in vitro por fluorescência de atividade antiplasmodial." reponame:Repositório Institucional da UnB, 2014. http://repositorio.unb.br/handle/10482/15666.
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Dissertação (mestrado)—Universidade de Brasília, Faculdade de Medicina, Programa de Pós-Graduação em Patologia Molecular, 2014.Submitted by Alaíde Gonçalves dos Santos (alaide@unb.br) on 2014-04-29T12:50:20Z No. of bitstreams: 1 2014_ThuanydeMouraCordeiro.pdf: 3960809 bytes, checksum: 4b394c3182d7b2be77db6f48e1225c6d (MD5)
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A malária é uma doença infecciosa causada por protozoários Plasmodium spp. O P. falciparum é considerado o mais severo por ser o responsável pela maioria dos casos de morte causados pela doença. Devido ao rápido surgimento de cepas de P. falciparum resistentes às drogas antimalariais dá-se a importância de realizar um screening de compostos da biodiversidade, além de elucidar os mecanismos de ação de substâncias com comprovada ação antiplasmodial, como por exemplo, a rottlerin, um inibidor da proteína quinase C. As proteínas quinases desempenham um papel essencial em muitas funções celulares, o que as tornam alvos muito atraentes para o desenvolvimento de novas drogas. A metodologia considerada padrão ouro para avaliar a atividade antimalárica de drogas é o ensaio com incorporação de hipoxantina tritiada. No entanto, o alto custo, a adoção de medidas de segurança e a produção de lixo radioativo limitam a utilização desta técnica. Desta forma, os objetivos deste trabalho foram à implementação do teste de atividade antiplasmodial baseado em fluorescência com SYBR Green I®, avaliação da atividade antimalárica das subfrações cromatográficas de sílica-gel do extrato de acetato de etila de Qualea grandiflora, uma planta típica do Cerrado brasileiro, e avaliação dos efeitos da rottlerin no ciclo intra-eritrocitário do P. falciparum por métodos bioquímicos e citofluorimétricos. Três subfrações de Q. grandiflora apresentaram atividade antiplasmodial moderada, sem atividade citotóxica e hemolítica aparentes. Foi demonstrado o efeito da rottlerin, um potencial efetor da autofagia, sobre o ciclo eritrocitário de P. falciparum por citometria de fluxo. De fato, a análise da população enriquecida de esquizonte de P. falciparum em cultura tratada por rottlerin comparada com a não tratada revelou que houve inibição da diferenciação dos merozoítos, acarretando na morte rápida do parasito. A fim de entender quais eram os alvos proteicos de ação desta molécula, foi realizada uma análise proteômica comparativa preliminar por eletroforese bidimensional. Três proteínas, Heat Shock Protein 90 (HSP90), 3-fosfoglicerato quinase (3-PGK) e lactato desidrogenase (LDH), superexpressas na população de esquizontes não tratada com a rottlerin foram identificadas. Estas proteínas pertencem à classe de proteínas quinases ou possuem um domínio de interação com quinase. A HSP90 está envolvida no processo de enovelamento proteico com um papel fundamental no crescimento e desenvolvimento do parasito e, consequentemente, estudada como potencial alvo de droga antiplasmodial. A LDH e a 3-PGK são enzimas do metabolismo da glicose, e assim, potenciais alvos bem conhecidos para compostos antimaláricos devido à dependência deste parasito à glicólise para produção de energia. O estudo da biodiversidade do Cerrado pode contribuir para a descoberta de compostos antimalariais e a conservação deste bioma ameaçado. A não detecção das proteínas identificadas na presença de rottlerin pode estar relacionada à indução da autofagia na esquizogonia eritrocitária e constituem potenciais alvos de drogas antimaláricas. _______________________________________________________________________________________ ABSTRACT
Malaria is an infectious disease caused by Plasmodium spp protozoa. The P. falciparum is considered the most severe, since it is responsible for the majority of deaths related to this disease. Due to the rapid emergence of resistant strains of P. falciparum against antimalarial drugs, a great importance can be given to the screening of biodiversity compounds in addition to elucidate the mechanisms of action of substances with demonstrated antiplasmodial action such as rottlerin, an inhibitor of protein kinase C. Protein kinases play a pivotal role in many cellular functions, which make them very attractive targets for the development of new drugs. The methodology considered the gold standard for assessing antimalarial drug activity is the [3H]hypoxanthine incorporation assay. However, the high cost, adoption of safety regulations and the production of radioactive waste limit the application of this technique. Therefore, the objectives of this study were to implement the antiplasmodial activity test based on SYBR® Green I fluorescence, assessment of antimalarial activity of silica gel chromatographic subfractions of Qualea grandiflora ethyl acetate extract, a typical plant of the Brazilian Cerrado, and assessment of the rottlerin‟s effects in erythrocytic cycle of P. falciparum by biochemical and cytofluorimetric methods. Three subfractions of Q.grandiflora showed moderate antiplasmodial activity without apparent cytotoxic and hemolytic activities. It was demonstrated the effect of rottlerin, a potencial autophagy effector, on P. falciparum erythrocytic cycle by flow cytometry. In fact, analysis of the schizont enriched population of P. falciparum in rottlerin-treated culture compared to untreated ones revealed that there was an inhibition of merozoites differentiation, resulting in the rapid death of the parasite. In order to elucidate which proteins were the targets of rottlerin action, a preliminary comparative proteomic analysis by two-dimensional electrophoresis was performed. Three proteins, heat shock protein 90 (HSP90), 3- phosphoglycerate kinase (PGK-3) and lactate dehydrogenase (LDH), upregulated in schizont population non treated with rottlerin were identified. These proteins belong to the class of protein kinases or possess domains that interact with them. The HSP90 is involved in the protein folding process with a critic role in parasite growth and development, thus being studied as a potential target for antiplasmodial drugs. The 3- PGK and LDH are enzymes of glucose metabolism, hence well known potential targets for antimalarial compounds due to parasite dependence on glycolysis to produce energy. The study of Cerrado biodiversity can contribute to the discovery of antimalarial compounds and to the conservation of this threatened biome. The not detection of these proteins identified in the presence of rottlerin may be related to autophagy induction in erythrocytic schizogony and constitute potential targets for antimalarial drugs.
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Nguyen, Khoa Thuy Diem. "Energy metabolism in the brain and rapid distribution of glutamate transporter GLAST in astrocytes." Thesis, The University of Sydney, 2008. http://hdl.handle.net/2123/3996.
Full textAbstract:
Glutamate transporters play a role in removing extracellular excitatory neurotransmitter, L-glutamate into the cells. The rate of the uptake depends on the density of the transporters at the membrane. Some studies claimed that glutamate transporters could transit between the cytoplasm and the membrane on a time-scale of minutes. The present study examined the distribution of glutamate transporter GLAST predominantly expressed in rat cortical cultured astrocytes between the membrane and the cytoplasm by using deconvolution microscopy and then analyzing the images. The regulation of the distribution of GLAST was studied in the presence of glutamate transporter substrate (D-aspartate), purinergic receptor activators (α,β-methylene ATP, adenosine), neuroleptic drugs (clozapine, haloperidol), ammonia (hyperammonia) and Na+/K+-ATPase inhibitors (ouabain, digoxin and FCCP). It was demonstrated that the translocation of GLAST towards the plasma membrane was induced by D-aspartate, α,β-methylene ATP, adenosine, clozapine and ammonia (at 100 μM and very high concentrations of 10 mM). However, the inhibition of Na+/K+-ATPase activity had an opposite effect, resulting in redistribution of GLAST away from the membrane. It has previously been claimed that the membrane-cytoplasm trafficking of GLAST was regulated by phosphorylation catalysed by protein kinase C delta (PKC-delta). Involvement of this mechanism has, however, been put to doubt when rottlerin, a PKC-delta inhibitor, used to test the hypothesis showed to inhibit Na+/K+-ATPase-mediated uptake of Rb+, suggesting that rottlerin influenced the activity of Na+/K+-ATPase. As Na+/K+-ATPase converts ATP to energy and pumps Na+, K+ ions, thus helping to maintain normal electrochemical and ionic gradients across the cell membrane. Its inhibition also reduced D-aspartate transport and could impact on the cytoplasm-to-membrane traffic of GLAST molecules. Furthermore, rottlerin decreased the activity of Na+/K+-ATPase by acting as a mitochondrial inhibitor. The present study has focused on the inhibition of Na+/K+-ATPase activity by rottlerin, ouabain and digoxin in homogenates prepared from rat kidney and cultured astrocytes. The activity of Na+/K+-ATPase was measured by the absorption of inorganic phosphate product generated from the hydrolysis of ATP and the fluorescent transition of the dye RH421 induced by the movement of Na+/K+-ATPase. This approach has a potential to test whether the rottlerin effect on Na+/K+-ATPase is a direct inhibition of the enzyme activity. Rottlerin has been found to block the activity of Na+/K+-ATPase in a dose-dependent manner in both rat kidney and astrocyte homogenates. Therefore, rottlerin inhibited the activity of Na+/K+-ATPase directly in a cell-free preparation, thus strongly indicating that the effect was direct on the enzyme. In parallel experiments, ouabain and digoxin produced similar inhibitions of Na+/K+-ATPase activity in rat kidney while digoxin blocked the activity of Na+/K+-ATPase to a greater extent than ouabain in rat cortical cultured astrocytes. In a separate set of experiments, Na+/K+-ATPase in the astrocytic membrane was found to be unsaturated in E1(Na+)3 conformation in the presence of Na+ ions and this could explain the differences between the effects of digoxin and ouabain on the activity of Na+/K+-ATPase in rat astrocytes. In addition, it was found that at low concentrations of rottlerin, the activity of Na+/K+-ATPase was increased rather than inhibited. This effect was further investigated by studying rottlerin interactions with membrane lipids. The activity of Na+/K+-ATPase has been reported to be regulated by membrane lipids. The enzyme activity can be enhanced by increasing fluidity of the lipid membrane. I have, therefore, proposed that rottlerin binds to the membrane lipids and the effects of rottlerin on Na+/K+-ATPase are mediated by changes in the properties (fluidity) of the membrane. The hypothesis was tested by comparing rottlerin and a detergent, DOC (sodium deoxycholate), for their binding to the lipids by using a DMPC (1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine) monolayer technique. DOC has been shown to both increase and inhibit activity of Na+/K+-ATPase in a manner similar to that displayed by rottlerin. The effects of rottlerin and DOC on the DMPC monolayers were studied by measuring the surface pressure of DMPC monolayers and surface area per DMPC molecule. I established that both rottlerin and DOC decreased the surface pressure of DMPC monolayers and increased the surface area per DMPC molecule. This indicates that both rottlerin and DOC penetrated into the DMPC monolayers. If rottlerin can interact with the lipids, changes in fluidity of the lipid membrane cannot be ruled out and should be considered as a possible factor contributing to the effects of rottlerin on the activity of Na+/K+-ATPase. Overall, the study demonstrates that rottlerin is not only a PKC-delta inhibitor but can have additional effects, both on the enzyme activities (Na+/K+-ATPase) and/or on lipid-containing biological structures such as membranes. The findings have implication not only for studies where rottlerin was used as a supposedly specific PKC-delta inhibitor but also for mechanisms of its toxicity.
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Nguyen, Khoa Thuy Diem. "Energy metabolism in the brain and rapid distribution of glutamate transporter GLAST in astrocytes." University of Sydney, 2008. http://hdl.handle.net/2123/3996.
Full textAbstract:
Doctor of Philosophy (Medicine)Glutamate transporters play a role in removing extracellular excitatory neurotransmitter, L-glutamate into the cells. The rate of the uptake depends on the density of the transporters at the membrane. Some studies claimed that glutamate transporters could transit between the cytoplasm and the membrane on a time-scale of minutes. The present study examined the distribution of glutamate transporter GLAST predominantly expressed in rat cortical cultured astrocytes between the membrane and the cytoplasm by using deconvolution microscopy and then analyzing the images. The regulation of the distribution of GLAST was studied in the presence of glutamate transporter substrate (D-aspartate), purinergic receptor activators (α,β-methylene ATP, adenosine), neuroleptic drugs (clozapine, haloperidol), ammonia (hyperammonia) and Na+/K+-ATPase inhibitors (ouabain, digoxin and FCCP). It was demonstrated that the translocation of GLAST towards the plasma membrane was induced by D-aspartate, α,β-methylene ATP, adenosine, clozapine and ammonia (at 100 μM and very high concentrations of 10 mM). However, the inhibition of Na+/K+-ATPase activity had an opposite effect, resulting in redistribution of GLAST away from the membrane. It has previously been claimed that the membrane-cytoplasm trafficking of GLAST was regulated by phosphorylation catalysed by protein kinase C delta (PKC-delta). Involvement of this mechanism has, however, been put to doubt when rottlerin, a PKC-delta inhibitor, used to test the hypothesis showed to inhibit Na+/K+-ATPase-mediated uptake of Rb+, suggesting that rottlerin influenced the activity of Na+/K+-ATPase. As Na+/K+-ATPase converts ATP to energy and pumps Na+, K+ ions, thus helping to maintain normal electrochemical and ionic gradients across the cell membrane. Its inhibition also reduced D-aspartate transport and could impact on the cytoplasm-to-membrane traffic of GLAST molecules. Furthermore, rottlerin decreased the activity of Na+/K+-ATPase by acting as a mitochondrial inhibitor. The present study has focused on the inhibition of Na+/K+-ATPase activity by rottlerin, ouabain and digoxin in homogenates prepared from rat kidney and cultured astrocytes. The activity of Na+/K+-ATPase was measured by the absorption of inorganic phosphate product generated from the hydrolysis of ATP and the fluorescent transition of the dye RH421 induced by the movement of Na+/K+-ATPase. This approach has a potential to test whether the rottlerin effect on Na+/K+-ATPase is a direct inhibition of the enzyme activity. Rottlerin has been found to block the activity of Na+/K+-ATPase in a dose-dependent manner in both rat kidney and astrocyte homogenates. Therefore, rottlerin inhibited the activity of Na+/K+-ATPase directly in a cell-free preparation, thus strongly indicating that the effect was direct on the enzyme. In parallel experiments, ouabain and digoxin produced similar inhibitions of Na+/K+-ATPase activity in rat kidney while digoxin blocked the activity of Na+/K+-ATPase to a greater extent than ouabain in rat cortical cultured astrocytes. In a separate set of experiments, Na+/K+-ATPase in the astrocytic membrane was found to be unsaturated in E1(Na+)3 conformation in the presence of Na+ ions and this could explain the differences between the effects of digoxin and ouabain on the activity of Na+/K+-ATPase in rat astrocytes. In addition, it was found that at low concentrations of rottlerin, the activity of Na+/K+-ATPase was increased rather than inhibited. This effect was further investigated by studying rottlerin interactions with membrane lipids. The activity of Na+/K+-ATPase has been reported to be regulated by membrane lipids. The enzyme activity can be enhanced by increasing fluidity of the lipid membrane. I have, therefore, proposed that rottlerin binds to the membrane lipids and the effects of rottlerin on Na+/K+-ATPase are mediated by changes in the properties (fluidity) of the membrane. The hypothesis was tested by comparing rottlerin and a detergent, DOC (sodium deoxycholate), for their binding to the lipids by using a DMPC (1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine) monolayer technique. DOC has been shown to both increase and inhibit activity of Na+/K+-ATPase in a manner similar to that displayed by rottlerin. The effects of rottlerin and DOC on the DMPC monolayers were studied by measuring the surface pressure of DMPC monolayers and surface area per DMPC molecule. I established that both rottlerin and DOC decreased the surface pressure of DMPC monolayers and increased the surface area per DMPC molecule. This indicates that both rottlerin and DOC penetrated into the DMPC monolayers. If rottlerin can interact with the lipids, changes in fluidity of the lipid membrane cannot be ruled out and should be considered as a possible factor contributing to the effects of rottlerin on the activity of Na+/K+-ATPase. Overall, the study demonstrates that rottlerin is not only a PKC-delta inhibitor but can have additional effects, both on the enzyme activities (Na+/K+-ATPase) and/or on lipid-containing biological structures such as membranes. The findings have implication not only for studies where rottlerin was used as a supposedly specific PKC-delta inhibitor but also for mechanisms of its toxicity.
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Contreras, Xavier. "Rôle des voies PKC et calcium dans les productions de TNF-alpha et d'IL-10 induites par la protéine Tat du Virus de l'immuodéficience humaine chez le monocyte humain et dans la réplication de virus R5-tropiques dans le macrophage." Toulouse 3, 2005. http://www.theses.fr/2005TOU30012.
Full textAbstract:
Les objectifs de cette thèse sont d’une part la caractérisation des voies de signalisation impliquées dans la production de TNF-a et d’IL-10 par les monocytes/macrophages humains stimulés par la protéine Tat du VIH-1 et d’autre part l’évaluation du rôle de ces voies de signalisation dans la réplication virale. Ainsi, la protéine Tat active la voie calcique et la voie de la PKC dans le monocyte/macrophage pour stimuler la production du TNF-a et de l’IL-10 via son domaine N-terminal 1-45. Le domaine 20-45 stimule l’entrée du calcium dans le monocyte via les canaux calciques DHP sensibles. Tat induit l’activation des isoformes de PKC a, bI, bII, d, et e, mais seule l’activation des PKC d et bII est essentielle pour la production de l’IL-10. L’inhibition sélective de l’activation de la PKC d par la rottlerin bloque la réplication du virus CCR5-tropique HIV-1 BaL dans le macrophage humain en agissant probablement au niveau d’une étape précoce du cycle viral impliquant le cytosqueletteThe goals of this study are on the one hand the characterization of signaling pathways involved in TNF-a and IL-10 productions by human monocytes/macrophages stimulated by Tat protein of HIV-1 and on the other hand the evaluation of the role of these signaling pathways in viral replication. Thus, Tat protein activates the calcium and PKC pathways in the monocyte/macrophage to stimulate TNF-a and IL-10 productions via its 1-45 N-terminal domain. The 20-45 region stimulates calcium entry in monocytes via DHP-sensitive calcium channels. Tat induces the activation of a, bI, bII, d, and e PKC isozymes, but only d and bII PKC isozymes activation is essential for IL-10 production. The selective inhibition of PKC d activation by rottlerin blocks CCR5-tropic HIV-1 BaL virus replication in human macrophage by acting probably at the level of an early step of the virus life cycle involving the cytoskeleton
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Koterba, Kristen L. "Regulation of Autophagy and Cell Death in Breast Carcinoma Cells." University of Toledo Health Science Campus / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=mco1276005638.
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Rottler, Andreas [Verfasser]. "Investigation of Radial Metamaterials / Andreas Rottler." München : Verlag Dr. Hut, 2013. http://d-nb.info/1037286847/34.
Full textBooks on the topic "Rottlerin"
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Misaca, Constantin. How I escaped from Communist Romania, or... the Story of My Rottlen Life. Lulu Press, Inc., 2010.
Find full textBook chapters on the topic "Rottlerin"
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Bhandari, Khadka B., Suresh Subedi, Ripu M. Kunwar, Rainer W. Bussmann, and Narel Y. Paniagua-Zambrana. "Grewia disperma Rottler ex Spreng. Malvaceae." In Ethnobotany of the Himalayas, 1–13. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45597-2_112-1.
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Bhandari, Khadka B., Suresh Subedi, Ripu M. Kunwar, Rainer W. Bussmann, and Narel Y. Paniagua-Zambrana. "Grewia disperma Rottler ex Spreng. Malvaceae." In Ethnobotany of the Himalayas, 1001–13. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57408-6_112.
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"ROTTLERA." In Directory Of Plants Containing Secondary Metabolites, 1034. CRC Press, 1991. http://dx.doi.org/10.1201/b12561-426.
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"Kachri (Cucumis callosus [Rottler] Cogn.)." In Handbook of Cucurbits, 519–32. CRC Press, 2016. http://dx.doi.org/10.1201/b19233-48.
Full textConference papers on the topic "Rottlerin"
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Goldklang, Monica P., Nazish Sayed, Takwi Nkyimbeng, Jordis Trischler, Tina Zelonina, A. J. Dabo, Sergey Zakharov, et al. "Rottlerin Suppresses Airway Hyperreactivity And Inflammation In Mouse Models Of Experimental Asthma." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3580.
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Su, Hsin-Yuan, Richard Waldron, Raymond Gong, Stephen Pandol, and Aurelia Lugea. "Abstract 1769: Rottlerin induces ER stress-mediated cell death in pancreatic stellate cells." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1769.
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Joeckel, Matthias W., Elke Schneider, Frederik C. Roos, Christian Hampel, Joachim W. Thueroff, and Walburgis Brenner. "Abstract 1041: Sorafenib in combination with rottlerin show an additive effects in renal cell carcinoma (RCC) cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1041.
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Kumar, Dhruv. "Abstract 329: Rottlerin induced autophagy by targeting multiple sites that leads to the apoptosis in cancer stem cells." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-329.
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Prudnikova, Tatiana, and Jonathan Chernoff. "Abstract LB-011: PAK1 inhibitor FRAX1036 sensitizes ovarian cancer cells with amplified 11q13 to cytotoxic effect of rottlerin." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-lb-011.
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Ashour, Ahmed A., Abdel-Aziz H. Abdel-Aziz, Ahmed M. Mansour, Sultan N. Alpay, Kevin Dalby, and Bulent Ozpolat. "Abstract 848: Inhibition of eukaryotic elongation factor-2 kinase mediates Rottlerin induced effects in apoptosis and cell proliferation inhibition in human pancreatic cancer cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-848.
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