Database : MEDLINE
Search on : phorbol and esters [Words]
References found : 8167 [refine]
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[PMID]: 29259300
[Au] Autor:Azoitei N; Cobbaut M; Becher A; Van Lint J; Seufferlein T
[Ad] Address:Center for Internal Medicine I, University of Ulm, Ulm, Germany. ninel.azoitei@uni-ulm.de.
[Ti] Title:Protein kinase D2: a versatile player in cancer biology.
[So] Source:Oncogene;37(10):1263-1278, 2018 Mar.
[Is] ISSN:1476-5594
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Protein kinase D2 (PKD2) is a serine/threonine kinase that belongs to the PKD family of calcium-calmodulin kinases, which comprises three isoforms: PKD1, PKD2, and PKD3. PKD2 is activated by many stimuli including growth factors, phorbol esters, and G-protein-coupled receptor agonists. PKD2 participation to uncontrolled growth, survival, neovascularization, metastasis, and invasion has been documented in various tumor types including pancreatic, colorectal, gastric, hepatic, lung, prostate, and breast cancer, as well as glioma multiforme and leukemia. This review discusses the versatile functions of PKD2 from the perspective of cancer hallmarks as described by Hanahan and Weinberg. The PKD2 status, signaling pathways affected in different tumor types and the molecular mechanisms that lead to tumorigenesis and tumor progression are presented. The latest developments of small-molecule inhibitors selective for PKD/PKD2, as well as the need for further chemotherapies that prevent, slow down, or eliminate tumors are also discussed in this review.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1712
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1038/s41388-017-0052-8

  2 / 8167 MEDLINE  
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[PMID]: 29517836
[Au] Autor:Zhao X; Kedei N; Michalowski AM; Lewin NE; Keck GE; Blumberg PM
[Ad] Address:UNITED STATES.
[Ti] Title:Deletion of the C-26 Methyl Substituent from the Bryostatin Analogue Merle 23 has Negligible Impact on Its Biological Profile or Potency.
[So] Source:Chembiochem;, 2018 Mar 08.
[Is] ISSN:1439-7633
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Important strides are being made in understanding the structural features of bryostatin 1, a candidate therapeutic agent for cancer and dementia, conferring its potency for protein kinase C and the unique spectrum of biological responses which it induces. A critical pharmacophoric element in bryostatin 1 is a secondary hydroxyl, whereas a primary hydroxyl group plays the analogous role in binding of the phorbol esters to protein kinase C. Here, we describe the synthesis of a bryostatin homolog where the hydroxyl group is primary, as in the phorbol esters, and show that its biological activity is almost indistinguishable from that of the corresponding compound with the secondary hydroxyl group.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.1002/cbic.201700677

  3 / 8167 MEDLINE  
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[PMID]: 29513138
[Au] Autor:Newton AC
[Ad] Address:a Department of Pharmacology , University of California at San Diego , La Jolla , CA , USA.
[Ti] Title:Protein kinase C: perfectly balanced.
[So] Source:Crit Rev Biochem Mol Biol;53(2):208-230, 2018 Apr.
[Is] ISSN:1549-7798
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Protein kinase C (PKC) isozymes belong to a family of Ser/Thr kinases whose activity is governed by reversible release of an autoinhibitory pseudosubstrate. For conventional and novel isozymes, this is effected by binding the lipid second messenger, diacylglycerol, but for atypical PKC isozymes, this is effected by binding protein scaffolds. PKC shot into the limelight following the discovery in the 1980s that the diacylglycerol-sensitive isozymes are "receptors" for the potent tumor-promoting phorbol esters. This set in place a concept that PKC isozymes are oncoproteins. Yet three decades of cancer clinical trials targeting PKC with inhibitors failed and, in some cases, worsened patient outcome. Emerging evidence from cancer-associated mutations and protein expression levels provide a reason: PKC isozymes generally function as tumor suppressors and their activity should be restored, not inhibited, in cancer therapies. And whereas not enough activity is associated with cancer, variants with enhanced activity are associated with degenerative diseases such as Alzheimer's disease. This review describes the tightly controlled mechanisms that ensure PKC activity is perfectly balanced and what happens when these controls are deregulated. PKC isozymes serve as a paradigm for the wisdom of Confucius: "to go beyond is as wrong as to fall short."
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Data-Review
[do] DOI:10.1080/10409238.2018.1442408

  4 / 8167 MEDLINE  
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[PMID]: 29317197
[Au] Autor:Czikora A; Pany S; You Y; Saini AS; Lewin NE; Mitchell GA; Abramovitz A; Kedei N; Blumberg PM; Das J
[Ad] Address:Laboratory of Cancer Biology and Genetics, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, United States.
[Ti] Title:Structural determinants of phorbol ester binding activity of the C1a and C1b domains of protein kinase C theta.
[So] Source:Biochim Biophys Acta;1860(5):1046-1056, 2018 Jan 06.
[Is] ISSN:0006-3002
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:The PKC isozymes represent the most prominent family of signaling proteins mediating response to the ubiquitous second messenger diacylglycerol. Among them, PKCθ is critically involved in T-cell activation. Whereas all the other conventional and novel PKC isoforms have twin C1 domains with potent binding activity for phorbol esters, in PKCθ only the C1b domain possesses potent binding activity, with little or no activity reported for the C1a domain. In order to better understand the structural basis accounting for the very weak ligand binding of the PKCθ C1a domain, we assessed the effect on ligand binding of twelve amino acid residues which differed between the C1a and C1b domains of PKCθ. Mutation of Pro of the C1a domain of PKCθ to the corresponding Lys found in C1b restored in vitro binding activity for [ H]phorbol 12,13-dibutyrate to 3.6 nM, whereas none of the other residues had substantial effect. Interestingly, the converse mutation in the C1b domain of Lys to Pro only diminished binding affinity to 11.7 nM, compared to 254 nM in the unmutated C1a. In confocal experiments, deletion of the C1b domain from full length PKCθ diminished, whereas deletion of the C1a domain enhanced 5-fold (at 100 nM PMA) the translocation to the plasma membrane. We conclude that the Pro residue in the C1a domain of full length PKCθ plays a critical role in the ligand and membrane binding, while exchanging the residue (Lys ) at the same position in C1b domain of full length PKCθ only modestly reduced the membrane interaction.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180302
[Lr] Last revision date:180302
[St] Status:Publisher

  5 / 8167 MEDLINE  
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[PMID]: 29498277
[Au] Autor:Gomes TG; Hadi SIIA; Costa Alves GS; Mendona S; De Siqueira FG; Miller RNG
[Ad] Address:Instituto de Cincias Biolgicas, Departamento de Biologia Celular, Universidade de Braslia , Campus Universitrio Darcy Ribeiro, Asa Norte, 70910-900, Braslia, DF, Brazil.
[Ti] Title:Current Strategies for the Detoxification of Jatropha curcas Seed Cake: A Review.
[So] Source:J Agric Food Chem;, 2018 Mar 02.
[Is] ISSN:1520-5118
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Jatropha curcas is an important oilseed plant, with considerable potential in the development of biodiesel. Although Jatropha seed cake, the byproduct of oil extraction, is a residue rich in nitrogen, phosphorus, potassium, and carbon, with high protein content suitable for application in animal feed, the presence of toxic phorbol esters limits its application in feed supplements and fertilizers. This review summarizes the current methods available for detoxification of this residue, based upon chemical, physical, biological, or combined processes. The advantages and disadvantages of each process are discussed, and future directions involving genomic and proteomic approaches for advancing our understanding of biodegradation processes involving microorganisms are highlighted.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180302
[Lr] Last revision date:180302
[St] Status:Publisher
[do] DOI:10.1021/acs.jafc.7b05691

  6 / 8167 MEDLINE  
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[PMID]: 29414441
[Au] Autor:Slepchenko KG; Holub JM; Li YV
[Ad] Address:Department of Biomedical Sciences, Heritage College of Osteopathic Medicine, Ohio University, Athens, OH 45701, USA. Electronic address: slepchen@ohio.edu.
[Ti] Title:Intracellular zinc increase affects phosphorylation state and subcellular localization of protein kinase C delta (δ).
[So] Source:Cell Signal;44:148-157, 2018 Apr.
[Is] ISSN:1873-3913
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Protein kinase C delta (PKCδ) is a Ser/Thr-specific kinase involved in many fundamental cellular processes including growth, differentiation and apoptosis. PKCδ is expressed ubiquitously in all known cell types, and can be activated by diacylglycerol, phorbol esters and other kinases. Multiple lines of evidence have indicated that the mode of activation greatly influences the role PKCδ plays in cellular function. Divalent metal ions, such as zinc are released as a response to cellular stress and injury, often resulting in oxidative damage and cell death. In this study, we evaluate the effect increased concentrations of intracellular zinc has on the phosphorylation state and subcellular localization of PKCδ. More specifically, we demonstrate that intracellular zinc inhibits the phosphorylation of PKCδ at Thr in a concentration-dependent manner and facilitates the translocation of PKCδ from the cytosol to the Golgi complex. Analysis of a PKCδ structural model revealed a potential His-Cys3 zinc-binding domain adjacent to residue Thr and suggests that interaction with a Zn ion may preclude phosphorylation at this site. This study establishes zinc as a potent modulator of PKCδ function and suggests a novel mechanism by which PKCδ is able to "sense" changes in the concentration of intracellular zinc. These findings illuminate a new paradigm of metal ion-protein interaction that may have significant implications on a broad spectrum of cellular processes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180227
[Lr] Last revision date:180227
[St] Status:In-Data-Review

  7 / 8167 MEDLINE  
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[PMID]: 29309788
[Au] Autor:Fukushima K; Takahashi K; Kurokawa A; Ishimoto K; Otagaki S; Minami K; Fukushima N; Honoki K; Tsujiuchi T
[Ad] Address:Division of Molecular Oncology, Department of Life Science, Faculty of Science and Engineering, Kindai University, 3-4-1, Kowakae, Higashiosaka, Osaka 577-8502, Japan.
[Ti] Title:Involvement of LPA receptor-5 in the enhancement of cell motile activity by phorbol ester and anticancer drug treatments in melanoma A375 cells.
[So] Source:Biochem Biophys Res Commun;496(1):225-230, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Lysophosphatidic acid (LPA) signaling through six subtypes of LPA receptors (LPA to LPA ) regulates a variety of biological responses in cancer cells. The aim of our study was to evaluate an involvement of LPA receptors in the activation of cell motility by phorbol ester and anticancer drug treatments in melanoma A375 cells. Cells were treated with 12-O-tetradecanoylphorbol- 13-acetate (TPA) and phorbol-12,13-dibutyrate (PDBu) for 3 days. The cell motile activity of TPA treated cells was significantly higher than that of PDBu treated cells, correlating with LPAR5 expression levels. LPA knockdown suppressed the high cell motile activity induced by TPA. To assess whether the cell motile activity of A375 cells is stimulated through LPA induced by anticancer drugs, the long-term cisplatin (CDDP) and dacarbazine (DTIC) treated cells were generated from A375 cells (A375-CDDP and A375-DTIC cells, respectively). The expression levels of LPA receptor genes were changed in A375-CDDP and A375-DTIC cells. In particular, CDDP and DTIC treatment markedly elevated LPAR5 expressions. The cell motile activities of A375-CDDP and A375-DTIC cells were significantly higher than that of untreated cells. These results suggest that the cell motile activity is regulated through the induction of LPA by phorbol ester and anticancer drug treatments in A375 cells.
[Mh] MeSH terms primary: Antineoplastic Agents/administration & dosage
Cell Movement/drug effects
Melanoma/drug therapy
Melanoma/metabolism
Phorbol Esters/administration & dosage
Receptors, Lysophosphatidic Acid/metabolism
Skin Neoplasms/metabolism
[Mh] MeSH terms secundary: Cell Line, Tumor
Cell Proliferation/drug effects
Dose-Response Relationship, Drug
Humans
Skin Neoplasms/drug therapy
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Antineoplastic Agents); 0 (LPAR5 protein, human); 0 (Phorbol Esters); 0 (Receptors, Lysophosphatidic Acid)
[Em] Entry month:1802
[Cu] Class update date: 180215
[Lr] Last revision date:180215
[Js] Journal subset:IM
[Da] Date of entry for processing:180109
[St] Status:MEDLINE

  8 / 8167 MEDLINE  
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[PMID]: 29306054
[Au] Autor:White SH; Sturgeon RM; Gu Y; Nensi A; Magoski NS
[Ad] Address:Department of Biomedical and Molecular Sciences, Physiology and Neuroscience Graduate Programs, Centre for Neuroscience Studies, Queen's University, Kingston, ON K7L 3N6, Canada.
[Ti] Title:Tyrosine Phosphorylation Determines Afterdischarge Initiation by Regulating an Ionotropic Cholinergic Receptor.
[So] Source:Neuroscience;372:273-288, 2018 Feb 21.
[Is] ISSN:1873-7544
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Changes to neuronal activity often involve a rapid and precise transition from low to high excitability. In the marine snail, Aplysia, the bag cell neurons control reproduction by undergoing an afterdischarge, which begins with synaptic input releasing acetylcholine to open an ionotropic cholinergic receptor. Gating of this receptor causes depolarization and a shift from silence to continuous action potential firing, leading to the neuroendocrine secretion of egg-laying hormone and ovulation. At the onset of the afterdischarge, there is a rise in intracellular Ca , followed by both protein kinase C (PKC) activation and tyrosine dephosphorylation. To determine whether these signals influence the acetylcholine ionotropic receptor, we examined the bag cell neuron cholinergic response both in culture and isolated clusters using whole-cell and/or sharp-electrode electrophysiology. The acetylcholine-induced current was not altered by increasing intracellular Ca via voltage-gated Ca channels, clamping intracellular Ca with exogenous Ca buffers, or activating PKC with phorbol esters. However, lowering phosphotyrosine levels by inhibiting tyrosine kinases both reduced the cholinergic current and prevented acetylcholine from triggering action potentials or afterdischarge-like bursts. In other systems, acetylcholine receptors are often modulated by multiple signals, but bag cell neurons appear to be more restrictive in this regard. Prior work finds that, as the afterdischarge proceeds, tyrosine dephosphorylation leads to biophysical alterations that promote persistent firing. Because this firing is subsequent to the cholinergic input, inhibiting the acetylcholine receptor may represent a means of properly orchestrating synaptically induced changes in excitability.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180212
[Lr] Last revision date:180212
[St] Status:In-Data-Review

  9 / 8167 MEDLINE  
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[PMID]: 29248584
[Au] Autor:Patil RH; Naveen Kumar M; Kiran Kumar KM; Nagesh R; Kavya K; Babu RL; Ramesh GT; Chidananda Sharma S
[Ad] Address:Department of Microbiology and Biotechnology, Bangalore University, Jnana Bharathi, Bengaluru 560 056, Karnataka, India; Department of Biotechnology, The Oxford College of Science, HSR Layout, Bengaluru 560102, Karnataka, India. Electronic address: rajeshwarihpatil2@gmail.com.
[Ti] Title:Dexamethasone inhibits inflammatory response via down regulation of AP-1 transcription factor in human lung epithelial cells.
[So] Source:Gene;645:85-94, 2018 Mar 01.
[Is] ISSN:1879-0038
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:The production of inflammatory mediators by epithelial cells in inflammatory lung diseases may represent an important target for the anti-inflammatory effects of glucocorticoids. Activator protein-1 is a major activator of inflammatory genes and has been proposed as a target for inhibition by glucocorticoids. We have used human pulmonary type-II A549 cells to examine the effect of dexamethasone on the phorbol ester (PMA)/Lipopolysaccharide (LPS) induced pro-inflammatory cytokines and AP-1 factors. A549 cells were treated with and without PMA or LPS or dexamethasone and the cell viability and nitric oxide production was measured by MTT assay and Griess reagent respectively. Expression of pro-inflammatory cytokines and AP-1 factors mRNA were measured using semi quantitative RT-PCR. The PMA/LPS treated cells show significant 2-3 fold increase in the mRNA levels of pro-inflammatory cytokines (IL-1, IL-2, IL-6, IL-8 and TNF-α), cyclooxygenase-2 (COX-2) and specific AP-1 factors (c-Jun, c-Fos and Jun-D). Whereas, pretreatment of cells with dexamethasone significantly inhibited the LPS induced nitric oxide production and PMA/LPS induced mRNAs expression of above pro-inflammatory cytokines, COX-2 and AP-1 factors. Cells treated with dexamethasone alone at both the concentrations inhibit the mRNAs expression of IL-1, IL-6 and TNF-α compared to control. Our study reveals that dexamethasone decreased the mRNAs expression of c-Jun and c-Fos available for AP-1 formation suggested that AP-1 is the probable key transcription factor involved in the anti-inflammatory activity of dexamethasone. This may be an important molecular mechanism of steroid action in asthma and other chronic inflammatory lung diseases which may be useful for treatment of lung inflammatory diseases.
[Mh] MeSH terms primary: Anti-Inflammatory Agents/pharmacology
Dexamethasone/pharmacology
Down-Regulation
Lung/drug effects
Transcription Factor AP-1/genetics
[Mh] MeSH terms secundary: A549 Cells
Cell Survival/drug effects
Cytokines/genetics
Epithelial Cells/chemistry
Epithelial Cells/cytology
Epithelial Cells/drug effects
Epithelial Cells/immunology
Gene Expression Regulation/drug effects
Humans
Lipopolysaccharides/adverse effects
Lung/chemistry
Lung/cytology
Lung/immunology
Nitric Oxide/metabolism
Phorbol Esters/adverse effects
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Anti-Inflammatory Agents); 0 (Cytokines); 0 (Lipopolysaccharides); 0 (Phorbol Esters); 0 (Transcription Factor AP-1); 31C4KY9ESH (Nitric Oxide); 7S5I7G3JQL (Dexamethasone)
[Em] Entry month:1801
[Cu] Class update date: 180129
[Lr] Last revision date:180129
[Js] Journal subset:IM
[Da] Date of entry for processing:171218
[St] Status:MEDLINE

  10 / 8167 MEDLINE  
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[PMID]: 29051025
[Au] Autor:Muiwo P; Pandey P; Ahmad HM; Ramachandran SS; Bhattacharya A
[Ad] Address:School of Life Sciences, Jawaharlal Nehru University, New Delhi, India. Electronic address: pamchui36@gmail.com.
[Ti] Title:IsomiR processing during differentiation of myelogenous leukemic cell line K562 by phorbol ester PMA.
[So] Source:Gene;641:172-179, 2018 Jan 30.
[Is] ISSN:1879-0038
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Chronic myelocytic leukemia cell line K562 undergoes differentiation by phorbol esters to megakaryocytes and we have used this system to understand miRNA processing leading to isomiR generation. PMA treatment significantly altered the production of miRNA in K562 cells. Expression of 24.4% of miRNAs were found to be stimulated whereas expression of 10% miRNAs were inhibited by PMA treatment. Our results suggest that miRNA precursors are processed into isomiRs in a deterministic manner. The relative levels of different isomiRs of a miRNA remained mainly unchanged even after PMA treatment irrespective of overall changes in expression (either up-regulation or down-regulation). However, not all miRNAs behave in the same way, about 7% showed a variation of isomiR profiles after PMA treatment. Most of the later class of miRNAs were found to be oncogenic miRNAs. Further, it was also found that number of isomiRs was independent of abundance of a miRNA. Functional importance of different isomiRs was demonstrated using three different isomiRs of miR-22. Our results showed that different isomiRs could inhibit expression of targets genes with different efficiencies. Our study suggests that the heterogeneity of a miRNA population generated during processing is in general regulated and that variation in the generation of an isomiR can be a functionally important regulatory feature.
[Mh] MeSH terms primary: Cell Differentiation/drug effects
Cell Differentiation/genetics
Leukemia, Myeloid/genetics
MicroRNAs/genetics
Phorbol Esters/pharmacology
Phosphorylcholine/analogs & derivatives
Polymethacrylic Acids/pharmacology
[Mh] MeSH terms secundary: Cell Line, Tumor
Genetic Heterogeneity/drug effects
Humans
K562 Cells
Phosphorylcholine/pharmacology
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (MicroRNAs); 0 (Phorbol Esters); 0 (Polymethacrylic Acids); 0 (poly(MPC-co-MA)); 107-73-3 (Phosphorylcholine)
[Em] Entry month:1711
[Cu] Class update date: 171128
[Lr] Last revision date:171128
[Js] Journal subset:IM
[Da] Date of entry for processing:171021
[St] Status:MEDLINE


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