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[PMID]: 25091693
[Au] Autor:Havrilesky LJ; Alvarez Secord A; Ehrisman JA; Berchuck A; Valea FA; Lee PS; Gaillard SL; Samsa GP; Cella D; Weinfurt KP; Abernethy AP; Reed SD
[Ad] Address:Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Duke University Medical Center, Durham, North Carolina; Duke Cancer Institute, Duke University Medical Center, Durham, North Carolina.
[Ti] Title:Patient preferences in advanced or recurrent ovarian cancer.
[So] Source:Cancer;120(23):3651-9, 2014 Dec 1.
[Is] ISSN:1097-0142
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: The objective of this study was to elucidate relative preferences of women with ovarian cancer for symptoms, treatment-related side effects, and progression-free survival (PFS) relevant to choosing a treatment regimen. METHODS: Women with advanced or recurrent ovarian cancer participated in a survey that included 3 methods to measure patient preferences (ratings, rankings, and a discrete-choice experiment) for 7 attributes: mode of administration, visit frequency, peripheral neuropathy, nausea and vomiting, fatigue, abdominal discomfort, and PFS. Participants were asked to choose between 2 unlabeled treatment scenarios that were characterized using the 7 attributes. Each participant completed 12 choice questions in which attribute levels were assigned according to an experimental design and a fixed-choice question representing 2 chemotherapy regimens for ovarian cancer. RESULTS: In total, 95 women completed the survey. Participants' ratings and rankings revealed greater concern and importance for PFS than for any other attribute (P < .0001 for all). The discrete-choice experiment revealed that the relative odds that a participant would choose a scenario with 18 months, 21 months, and 24 months of PFS versus 15 months of PFS were 1.5 (P = .01), 3.4 (P < .001), and 7.5 (P < .001), respectively. However, participants' choices indicated that they were willing to accept a shorter PFS to avoid severe side effects: 6.7 months to reduce nausea and vomiting from severe to mild, 5.0 months to reduce neuropathy from severe to mild, and 3.7 months to reduce abdominal symptoms from severe to moderate. CONCLUSIONS: PFS is the predominant driver of patient preferences for chemotherapy regimens. However, women in the current study were willing to trade significant PFS time for reductions in treatment-related toxicity.
[Mh] MeSH terms primary: Antineoplastic Agents/adverse effects
Choice Behavior
Neoplasm Recurrence, Local/therapy
Ovarian Neoplasms/drug therapy
Patient Preference
[Mh] MeSH terms secundary: Aged
Disease-Free Survival
Fatigue/chemically induced
Female
Humans
Middle Aged
Nausea/chemically induced
Neoplasm Recurrence, Local/pathology
Neoplasm Recurrence, Local/psychology
Neoplasm Staging
Ovarian Neoplasms/pathology
Ovarian Neoplasms/psychology
Peripheral Nervous System Diseases/chemically induced
Vomiting/chemically induced
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Name of substance:0 (Antineoplastic Agents)
[Em] Entry month:1501
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:141121
[St] Status:MEDLINE
[do] DOI:10.1002/cncr.28940

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[PMID]: 25128228
[Au] Autor:Park K; Chen Z; MacDonald TY; Siddiqui J; Ye H; Erbersdobler A; Shevchuk MM; Robinson BD; Sanda MG; Chinnaiyan AM; Beltran H; Rubin MA; Mosquera JM
[Ad] Address:Department of Pathology and Laboratory Medicine, Weill Medical College of Cornell University, New York, NY 10065....
[Ti] Title:Prostate cancer with Paneth cell-like neuroendocrine differentiation has recognizable histomorphology and harbors AURKA gene amplification.
[So] Source:Hum Pathol;45(10):2136-43, 2014 Oct.
[Is] ISSN:1532-8392
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Aurora kinase A (AURKA) gene amplification has been documented in 67% of hormone-naive prostate cancer cases that progress to a highly aggressive variant of castrate-resistant disease, clinically referred to as "neuroendocrine" prostate cancer, "small cell" prostate carcinoma, or "anaplastic" prostate cancer. Therefore, AURKA amplification is a potential prognostic biomarker that may help to identify patients with prostate cancer who are at high risk for developing castrate-resistant disease with clinical features of small cell carcinoma. Furthermore, AURKA inhibitors are currently being tested in clinical trials. In a previous study, we found AURKA amplification in 6 cases of prostate cancer with Paneth cell-like cells. This morphologic pattern has been suggested to represent low-grade neuroendocrine differentiation (NED) with generally favorable prognosis. We sought to investigate the frequency of AURKA amplification and the histologic characteristics of prostate cancer with Paneth cell-like NED. Twenty-five cases from 172 prostatectomies were evaluated for the presence of 18 morphologic features and AURKA amplification. Most prostate cancers with Paneth cell-like NED had macronucleoli (92%), basophilic appearance (88%), perineural invasion (72%), and nuclear stratification (76%). The frequency of AURKA amplification was 45%, present throughout the examined tumor nodule including areas without Paneth cell-like cells. When histologically similar cases with and without AURKA amplification were compared, this gene alteration was associated with larger extent of Paneth cell-like NED identified at magnification ×20 (P = .015), higher percentage of Paneth cell-like NED throughout the tumor nodule (P = .033), ductal features (P = .02), and higher overall Gleason grade (P = .039). AURKA amplification was not associated with age, serum prostate specific antigen, or tumor stage. The high frequency of AURKA amplification (45%) in localized prostate cancer with Paneth cell-like NED and its potential prognostic significance warrant further investigation.
[Mh] MeSH terms primary: Adenocarcinoma/genetics
Adenocarcinoma/pathology
Aurora Kinase A/genetics
Prostatic Neoplasms/genetics
Prostatic Neoplasms/pathology
[Mh] MeSH terms secundary: Aged
Aged, 80 and over
Cell Differentiation
Female
Gene Amplification
Humans
In Situ Hybridization, Fluorescence
Male
Middle Aged
Paneth Cells/pathology
Tumor Markers, Biological/analysis
Tumor Markers, Biological/genetics
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Name of substance:0 (Tumor Markers, Biological); EC 2.7.11.1 (AURKA protein, human); EC 2.7.11.1 (Aurora Kinase A)
[Em] Entry month:1412
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:141013
[St] Status:MEDLINE

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[PMID]: 25189339
[Au] Autor:Kamson DO; Lee TJ; Varadarajan K; Robinette NL; Muzik O; Chakraborty PK; Snyder M; Barger GR; Mittal S; Juhász C
[Ad] Address:PET Center and Translational Imaging Laboratory, Children's Hospital of Michigan, Detroit, Michigan Department of Pediatrics, Wayne State University, Detroit, Michigan....
[Ti] Title:Clinical significance of tryptophan metabolism in the nontumoral hemisphere in patients with malignant glioma.
[So] Source:J Nucl Med;55(10):1605-10, 2014 Oct.
[Is] ISSN:1535-5667
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:UNLABELLED: α-(11)C-methyl-L-tryptophan (AMT) PET allows evaluation of brain serotonin synthesis and can also track upregulation of the immunosuppressive kynurenine pathway in tumor tissue. Increased AMT uptake is a hallmark of World Health Organization grade III-IV gliomas. Our recent study also suggested decreased frontal cortical AMT uptake in glioma patients contralateral to the tumor. The clinical significance of extratumoral tryptophan metabolism has not been established. In the present study, we investigated clinical correlates of tryptophan metabolic abnormalities in the nontumoral hemisphere of glioma patients. METHODS: Standardized AMT uptake values (SUVs) and the uptake rate constant of AMT (K [mL/g/min], a measure proportional to serotonin synthesis in nontumoral gray matter) were quantified in the frontal and temporal cortex and thalamus in the nontumoral hemisphere in 77 AMT PET scans of 66 patients (41 men, 25 women; mean age ± SD, 55 ± 15 y) with grade III-IV gliomas. These AMT values were determined before treatment in 35 and after treatment in 42 patients and were correlated with clinical variables and survival. RESULTS: AMT uptake in the thalamus showed a moderate age-related increase before treatment (SUV, r = 0.39, P = 0.02) but decrease after treatment (K, r = -0.33, P = 0.057). Women had higher thalamic SUVs before treatment (P = 0.037) and higher thalamic (P = 0.013) and frontal cortical K values (P = 0.023) after treatment. In the posttreatment glioma group, high thalamic SUVs and high thalamocortical SUV ratios were associated with short survival in Cox regression analysis. The thalamocortical ratio remained strongly prognostic (P < 0.01) when clinical predictors, including age, glioma grade, and time since radiotherapy, were entered in the regression model. Long interval between radiotherapy and posttreatment AMT PET as well as high radiation dose affecting the thalamus were associated with lower contralateral thalamic or cortical AMT uptake values. CONCLUSION: These observations provide evidence for altered tryptophan uptake in contralateral cortical and thalamic brain regions in glioma patients after initial therapy, suggesting treatment effects on the serotonergic system. Low thalamic tryptophan uptake appears to be a strong, independent predictor of long survival in patients with previous glioma treatment.
[Mh] MeSH terms primary: Brain Neoplasms/metabolism
Glioma/metabolism
Tryptophan/metabolism
[Mh] MeSH terms secundary: Adult
Aged
Brain/pathology
Brain/radionuclide imaging
Female
Humans
Kynurenine/metabolism
Magnetic Resonance Imaging/methods
Male
Middle Aged
Positron-Emission Tomography/methods
Prognosis
Proportional Hazards Models
Serotonin/metabolism
Tryptophan/analogs & derivatives
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:333DO1RDJY (Serotonin); 343-65-7 (Kynurenine); 7303-49-3 (tryptophan methyl ester); 8DUH1N11BX (Tryptophan)
[Em] Entry month:1412
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:141002
[St] Status:MEDLINE
[do] DOI:10.2967/jnumed.114.141002

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[PMID]: 25118570
[Au] Autor:Queisser MA; Dada LA; Deiss-Yehiely N; Angulo M; Zhou G; Kouri FM; Knab LM; Liu J; Stegh AH; DeCamp MM; Budinger GR; Chandel NS; Ciechanover A; Iwai K; Sznajder JI
[Ad] Address:1 Division of Pulmonary and Critical Care Medicine.
[Ti] Title:HOIL-1L functions as the PKCζ ubiquitin ligase to promote lung tumor growth.
[So] Source:Am J Respir Crit Care Med;190(6):688-98, 2014 Sep 15.
[Is] ISSN:1535-4970
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:RATIONALE: Protein kinase C zeta (PKCζ) has been reported to act as a tumor suppressor. Deletion of PKCζ in experimental cancer models has been shown to increase tumor growth. However, the mechanisms of PKCζ down-regulation in cancerous cells have not been previously described. OBJECTIVES: To determine the molecular mechanisms that lead to decreased PKCζ expression and thus increased survival in cancer cells and tumor growth. METHODS: The levels of expression of heme-oxidized IRP2 ubiquitin ligase 1L (HOIL-1L), HOIL-1-interacting protein (HOIP), Shank-associated RH domain-interacting protein (SHARPIN), and PKCζ were analyzed by Western blot and/or quantitative real-time polymerase chain reaction in different cell lines. Coimmunoprecipitation experiments were used to demonstrate the interaction between HOIL-1L and PKCζ. Ubiquitination was measured in an in vitro ubiquitination assay and by Western blot with specific antibodies. The role of hypoxia-inducible factor (HIF) was determined by gain/loss-of-function experiments. The effect of HOIL-1L expression on cell death was investigated using RNA interference approaches in vitro and on tumor growth in mice models. Increased HOIL-1L and decreased PKCζ expression was assessed in lung adenocarcinoma and glioblastoma multiforme and documented in several other cancer types by oncogenomic analysis. MEASUREMENTS AND MAIN RESULTS: Hypoxia is a hallmark of rapidly growing solid tumors. We found that during hypoxia, PKCζ is ubiquitinated and degraded via the ubiquitin ligase HOIL-1L, a component of the linear ubiquitin chain assembly complex (LUBAC). In vitro ubiquitination assays indicate that HOIL-1L ubiquitinates PKCζ at Lys-48, targeting it for proteasomal degradation. In a xenograft tumor model and lung cancer model, we found that silencing of HOIL-1L increased the abundance of PKCζ and decreased the size of tumors, suggesting that lower levels of HOIL-1L promote survival. Indeed, mRNA transcript levels of HOIL-1L were elevated in tumor of patients with lung adenocarcinoma, and in a lung adenocarcinoma tissue microarray the levels of HOIL-1L were associated with high-grade tumors. Moreover, we found that HOIL-1L expression was regulated by HIFs. Interestingly, the actions of HOIL-1L were independent of LUBAC. CONCLUSIONS: These data provide first evidence of a mechanism of cancer cell adaptation to hypoxia where HIFs regulate HOIL-1L, which targets PKCζ for degradation to promote tumor survival. We provided a proof of concept that silencing of HOIL-1L impairs lung tumor growth and that HOIL-1L expression predicts survival rate in cancer patients suggesting that HOIL-1L is an attractive target for cancer therapy.
[Mh] MeSH terms primary: Adenocarcinoma/metabolism
Adenocarcinoma/pathology
Cell Line, Tumor/metabolism
Glioblastoma/metabolism
Lung Neoplasms/metabolism
Lung Neoplasms/pathology
Protein Kinase C/metabolism
Ubiquitin-Protein Ligases/metabolism
[Mh] MeSH terms secundary: Animals
Cell Hypoxia/physiology
Cell Proliferation/physiology
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Neoplastic
Humans
Mice
Protein Kinase C/genetics
Ubiquitination/physiology
Xenograft Model Antitumor Assays
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:EC 2.7.11.1 (protein kinase C zeta); EC 2.7.11.13 (Protein Kinase C); EC 6.3.2.19 (HOIL-1 protein, human); EC 6.3.2.19 (Ubiquitin-Protein Ligases)
[Em] Entry month:1411
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:140916
[St] Status:MEDLINE
[do] DOI:10.1164/rccm.201403-0463OC

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[PMID]: 25177973
[Au] Autor:Wu CH; Sokolov K
[Ad] Address:Department of Biomedical Engineering, University of Texas at Austin; Department of Imaging Physics, University of Texas M.D. Anderson Cancer Center.
[Ti] Title:Synthesis of immunotargeted magneto-plasmonic nanoclusters.
[So] Source:J Vis Exp;(90), 2014.
[Is] ISSN:1940-087X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Magnetic and plasmonic properties combined in a single nanoparticle provide a synergy that is advantageous in a number of biomedical applications including contrast enhancement in novel magnetomotive imaging modalities, simultaneous capture and detection of circulating tumor cells (CTCs), and multimodal molecular imaging combined with photothermal therapy of cancer cells. These applications have stimulated significant interest in development of protocols for synthesis of magneto-plasmonic nanoparticles with optical absorbance in the near-infrared (NIR) region and a strong magnetic moment. Here, we present a novel protocol for synthesis of such hybrid nanoparticles that is based on an oil-in-water microemulsion method. The unique feature of the protocol described herein is synthesis of magneto-plasmonic nanoparticles of various sizes from primary blocks which also have magneto-plasmonic characteristics. This approach yields nanoparticles with a high density of magnetic and plasmonic functionalities which are uniformly distributed throughout the nanoparticle volume. The hybrid nanoparticles can be easily functionalized by attaching antibodies through the Fc moiety leaving the Fab portion that is responsible for antigen binding available for targeting.
[Mh] MeSH terms primary: Immunoconjugates/chemistry
Immunoglobulin Fab Fragments/chemistry
Immunoglobulin Fc Fragments/chemistry
Magnetite Nanoparticles/chemistry
[Mh] MeSH terms secundary: Antibodies, Monoclonal/chemistry
Breast Neoplasms/immunology
Cell Line, Tumor
Humans
Magnetics
Receptor, Epidermal Growth Factor/immunology
Skin Neoplasms/pathology
Spectrophotometry, Ultraviolet
Spectroscopy, Near-Infrared
Surface Plasmon Resonance
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; VIDEO-AUDIO MEDIA
[Nm] Name of substance:0 (Antibodies, Monoclonal); 0 (Immunoconjugates); 0 (Immunoglobulin Fab Fragments); 0 (Immunoglobulin Fc Fragments); 0 (Magnetite Nanoparticles); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[Em] Entry month:1501
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:140902
[St] Status:MEDLINE
[do] DOI:10.3791/52090

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[PMID]: 24731055
[Au] Autor:Warram JM; Sorace AG; Mahoney M; Samuel S; Harbin B; Joshi M; Martin A; Whitworth L; Hoyt K; Zinn KR
[Ad] Address:Department of Radiology and.
[Ti] Title:Biodistribution of P-selectin targeted microbubbles.
[So] Source:J Drug Target;22(5):387-94, 2014 Jun.
[Is] ISSN:1029-2330
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:PURPOSE: To evaluate binding of P-selectin targeted microbubbles (MB) in tumor vasculature; a whole-body imaging and biodistribution study was performed in a tumor bearing mouse model. METHODS: Antibodies were radiolabeled with Tc-99 m using the HYNIC method. Tc-99 m labeled anti-P-selectin antibodies were avidin-bound to lipid-shelled, perfluorocarbon gas-filled MB and intravenously injected into mice bearing MDA-MB-231 breast tumors. Whole-body biodistribution was performed at 5 min (n = 12) and 60 min (n = 4) using a gamma counter. Tc-99 m-labeled IgG bound IgG-control-MB group (n = 12 at 5 min; n = 4 at 60 min), Tc-99 m-labeled IgG-control-Ab group (n = 5 at 5 min; n = 3 at 60 min) and Tc-99 m-labeled anti P-selectin-Ab group (n = 5 at 5 min; n = 3 at 60 min) were also evaluated. Planar gamma camera imaging was also performed at each time point. RESULTS: Targeted-MB retention in tumor (60 min: 1.8 ± 0.3% ID/g) was significantly greater (p = 0.01) than targeted-MB levels in adjacent skeletal muscle at both time points (5 min: 0.7 ± 0.2% ID/g; 60 min: 0.2 ± 0.1% ID/g) while there was no significant difference (p = 0.17) between muscle and tumor retention for the IgG-control-MB group at 5 min. CONCLUSIONS: P-selectin targeted MBs were significantly higher in tumor tissue, as compared with adjacent skeletal tissue or tumor retention of IgG-control-MB.
[Mh] MeSH terms primary: Angiogenesis Inhibitors/pharmacokinetics
Antibodies, Monoclonal/pharmacokinetics
Mammary Neoplasms, Experimental/drug therapy
Microbubbles
P-Selectin/antagonists & inhibitors
[Mh] MeSH terms secundary: Angiogenesis Inhibitors/administration & dosage
Angiogenesis Inhibitors/therapeutic use
Animals
Antibodies, Monoclonal/administration & dosage
Antibodies, Monoclonal/adverse effects
Antibodies, Monoclonal/therapeutic use
Cell Line, Tumor
Contrast Media
Female
Humans
Mammary Neoplasms, Experimental/blood supply
Mammary Neoplasms, Experimental/metabolism
Mammary Neoplasms, Experimental/radionuclide imaging
Mice
Mice, Nude
P-Selectin/genetics
Technetium
Tissue Distribution
Xenograft Model Antitumor Assays
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Angiogenesis Inhibitors); 0 (Antibodies, Monoclonal); 0 (Contrast Media); 0 (P-Selectin); 7440-26-8 (Technetium)
[Em] Entry month:1412
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:140514
[St] Status:MEDLINE
[do] DOI:10.3109/1061186X.2013.869822

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[PMID]: 24674886
[Au] Autor:Wu Q; Kohli M; Bergen HR; Cheville JC; Karnes RJ; Cao H; Young CY; Tindall DJ; McNiven MA; Donkena KV
[Ad] Address:Authors' Affiliations: Departments of Urology, Oncology, and Biochemistry and Molecular Biology; and Division of Anatomic Pathology, Mayo Clinic, Rochester, Minnesota.
[Ti] Title:Preclinical evaluation of the supercritical extract of azadirachta indica (neem) leaves in vitro and in vivo on inhibition of prostate cancer tumor growth.
[So] Source:Mol Cancer Ther;13(5):1067-77, 2014 May.
[Is] ISSN:1538-8514
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Azadirachta indica, commonly known as neem, has gained worldwide prominence because of its medical properties, namely antitumor, antiviral, anti-inflammatory, antihyperglycemic, antifungal, and antibacterial activities. Despite these promising results, gaps remain in our understanding of the molecular mechanism of action of neem compounds and their potential for use in clinical trials. We investigated supercritical extract of neem leaves (SENL) for the following: molecular targets in vitro, in vivo efficacy to inhibit tumor growth, and bioactive compounds that exert antitumor activity. Treatment of LNCaP-luc2 prostate cancer cells with SENL suppressed dihydrotestosterone-induced androgen receptor and prostate-specific antigen levels. SENL inhibited integrin ß1, calreticulin, and focal adhesion kinase activation in LNCaP-luc2 and PC3 prostate cancer cells. Oral administration of SENL significantly reduced LNCaP-luc2 xenograft tumor growth in mice with the formation of hyalinized fibrous tumor tissue, reduction in the prostate-specific antigen, and increase in AKR1C2 levels. To identify the active anticancer compounds, we fractionated SENL by high-pressure liquid chromatography and evaluated 16 peaks for cytotoxic activity. Four of the 16 peaks exhibited significant cytotoxic activity against prostate cancer cells. Mass spectrometry of the isolated peaks suggested the compounds with cytotoxic activity were nimbandiol, nimbolide, 2',3'-dihydronimbolide, and 28-deoxonimbolide. Analysis of tumor tissue and plasma samples from mice treated with SENL indicated 28-deoxonimbolide and nimbolide as the bioactive compounds. Overall, our data revealed the bioactive compounds in SENL and suggested that the anticancer activity could be mediated through alteration in androgen receptor and calreticulin levels in prostate cancer.
[Mh] MeSH terms primary: Antineoplastic Agents/pharmacology
Azadirachta/chemistry
Plant Extracts/pharmacology
Plant Leaves/chemistry
Prostatic Neoplasms/pathology
[Mh] MeSH terms secundary: Animals
Antineoplastic Agents/pharmacokinetics
Antineoplastic Agents/toxicity
Apoptosis/drug effects
Cell Line, Tumor
Cell Proliferation/drug effects
Disease Models, Animal
Focal Adhesions/drug effects
Humans
Inhibitory Concentration 50
Male
Mice
Plant Extracts/pharmacokinetics
Plant Extracts/toxicity
Prostate-Specific Antigen/metabolism
Prostatic Neoplasms/drug therapy
Prostatic Neoplasms/metabolism
Receptors, Androgen/metabolism
Tumor Burden/drug effects
Xenograft Model Antitumor Assays
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Name of substance:0 (Antineoplastic Agents); 0 (Plant Extracts); 0 (Receptors, Androgen); EC 3.4.21.77 (Prostate-Specific Antigen)
[Em] Entry month:1501
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:140507
[St] Status:MEDLINE
[do] DOI:10.1158/1535-7163.MCT-13-0699

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[PMID]: 24667300
[Au] Autor:Bedikian AY; Garbe C; Conry R; Lebbe C; Grob JJ; Genasense Melanoma Study Group
[Ad] Address:aDepartment of Melanoma Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas bDivision of Hematology/Oncology, University of Alabama at Birmingham, Birmingham, Alabama, USA cDermatology Polyclinic, Saint Louis Hospital, Paris dDepartment of Dermatology, Aix-Marseille University, Marseille, France eDepartment of Dermatology, University Medical Centre, Tubingen, Germany.
[Ti] Title:Dacarbazine with or without oblimersen (a Bcl-2 antisense oligonucleotide) in chemotherapy-naive patients with advanced melanoma and low-normal serum lactate dehydrogenase: 'The AGENDA trial'.
[So] Source:Melanoma Res;24(3):237-43, 2014 Jun.
[Is] ISSN:1473-5636
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:In a previous large randomized, open-label study, retrospective subset analysis revealed that the addition of the Bcl-2 antisense oligonucleotide oblimersen to dacarbazine (Dac) significantly improved overall survival, progression-free survival, and the response rate in chemotherapy-naive patients with advanced melanoma and normal baseline serum lactate dehydrogenase (LDH) levels. To confirm and expand on this observation, we conducted a prospective double-blind, placebo-controlled study to determine whether oblimersen augmented the efficacy of Dac in advanced melanoma patients with low-normal baseline LDH levels. A total of 314 chemotherapy-naive patients were randomly assigned to receive Dac (1000 mg/m(2)) preceded by a 5-day continuous intravenous infusion of either oblimersen sodium (7 mg/kg/day) or placebo every 21 days for less than eight cycles. Co-primary efficacy endpoints were overall survival and progression-free survival. Response and progression of the disease were assessed by independent blinded review of computed tomography scan images. No difference in overall nor progression-free survival was observed between the Dac-oblimersen and Dac-placebo groups. Although the overall (17.2 vs. 12.1%) and durable (10.8 vs. 7.6%) response rates numerically favored Dac-oblimersen over Dac-placebo, they did not differ significantly (P=0.19 and 0.32, respectively). The incidence of hematologic adverse events, particularly thrombocytopenia and neutropenia, was higher in the Dac-oblimersen group than in the Dac-placebo group. Withdrawals from the study because of treatment-related adverse events were low (i.e. <2.5%) in both groups. The addition of oblimersen to Dac did not significantly improve overall survival nor progression-free survival in patients with advanced melanoma and low-normal levels of LDH at baseline.
[Mh] MeSH terms primary: Antineoplastic Combined Chemotherapy Protocols/therapeutic use
Melanoma/drug therapy
Proto-Oncogene Proteins c-bcl-2/genetics
Skin Neoplasms/drug therapy
[Mh] MeSH terms secundary: Aged
Antineoplastic Agents, Alkylating/administration & dosage
Antineoplastic Combined Chemotherapy Protocols/adverse effects
Dacarbazine/administration & dosage
Disease-Free Survival
Double-Blind Method
Drug Administration Schedule
Female
Gene Expression Regulation, Neoplastic
Humans
Infusions, Intravenous
Male
Melanoma/genetics
Melanoma/metabolism
Melanoma/mortality
Melanoma/radiography
Middle Aged
Oligonucleotides, Antisense/administration & dosage
Prospective Studies
Skin Neoplasms/genetics
Skin Neoplasms/mortality
Skin Neoplasms/radiography
Thionucleotides/administration & dosage
Time Factors
Tomography, X-Ray Computed
Treatment Outcome
[Pt] Publication type:CLINICAL TRIAL, PHASE III; JOURNAL ARTICLE; MULTICENTER STUDY; RANDOMIZED CONTROLLED TRIAL
[Nm] Name of substance:0 (Antineoplastic Agents, Alkylating); 0 (Oligonucleotides, Antisense); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (Thionucleotides); 7GR28W0FJI (Dacarbazine); 85J5ZP6YSL (oblimersen)
[Em] Entry month:1412
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:140429
[St] Status:MEDLINE
[do] DOI:10.1097/CMR.0000000000000056

  9 / 1938960 MEDLINE  
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[PMID]: 24565984
[Au] Autor:Islam M; Datta J; Lang JC; Teknos TN
[Ad] Address:Department of Otolaryngology-Head and Neck Surgery, The Ohio State University, Wexner Medical Center, Columbus, OH, USA; Arthur G. James Cancer Hospital and Richard J. Solove Research Institute, The Ohio State University, Wexner Medical Center, Columbus, OH, USA. Electronic address: Mozaffarul.Islam...
[Ti] Title:Down regulation of RhoC by microRNA-138 results in de-activation of FAK, Src and Erk1/2 signaling pathway in head and neck squamous cell carcinoma.
[So] Source:Oral Oncol;50(5):448-56, 2014 May.
[Is] ISSN:1879-0593
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:OBJECTIVE: RhoC a pro-metastatic oncogene is constitutively active in many head and neck squamous cell carcinomas. MicroRNA-138 which possesses a documented tumor suppressor function can bind to the 3'UTR of RhoC mRNA and inhibit its activity. We hypothesize that miR-138 can inhibit the function of RhoC and consequently the activation of downstream target molecules involve in the signaling cascade. For this reason we investigated the role of miR-138 in HNSCC. METHODS: In vitro studies were carried out to evaluate the role of miR-138 in HNSCC cell lines and in primary tumors obtained from HNSCC patients. Real time RT-PCR, Western blot, cell motility, invasion and colony formation assays were performed according to standard procedures. RESULTS: Data obtained by G-LISA and real time PCR shows an inverse correlation between RhoC expression and miR-138 in HNSCC cell lines. Additionally, we obtained a similar pattern of RhoC and miR-138 expression in primary tumors from HNSCC patients. Over expression of miR-138 in HNSCC lines showed down regulation of RhoC, as well as a decrease in cell motility, invasion colony and stress fiber formation. Furthermore, a significant down regulation was observed for FAK, Src and Erk(1/2) upon miR-138 overexpression. CONCLUSION: These findings strongly suggest that the inhibition of RhoC can be achieved by over expressing miR-138, which further attenuates the downstream signaling cascade leading to cancer progression and survival. Moreover, this study for the first time shows that down regulation of FAK, Src and Erk(1/2) by miR-138 overexpression is due to inhibition of RhoC in HNSCC.
[Mh] MeSH terms primary: Carcinoma, Squamous Cell/metabolism
Down-Regulation
Head and Neck Neoplasms/metabolism
MicroRNAs/physiology
Signal Transduction
rho GTP-Binding Proteins/metabolism
[Mh] MeSH terms secundary: 3' Untranslated Regions
Carcinoma, Squamous Cell/enzymology
Carcinoma, Squamous Cell/pathology
Cell Line, Tumor
Focal Adhesion Protein-Tyrosine Kinases/metabolism
Head and Neck Neoplasms/enzymology
Head and Neck Neoplasms/pathology
Humans
MAP Kinase Signaling System
Proto-Oncogene Proteins pp60(c-src)
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (3' Untranslated Regions); 0 (MIRN138 microRNA, human); 0 (MicroRNAs); 0 (RHOC protein, human); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); EC 2.7.10.2 (Proto-Oncogene Proteins pp60(c-src)); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Entry month:1412
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:140414
[St] Status:MEDLINE

  10 / 1938960 MEDLINE  
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[PMID]: 24478380
[Au] Autor:Borger DR; Goyal L; Yau T; Poon RT; Ancukiewicz M; Deshpande V; Christiani DC; Liebman HM; Yang H; Kim H; Yen K; Faris JE; Iafrate AJ; Kwak EL; Clark JW; Allen JN; Blaszkowsky LS; Murphy JE; Saha SK; Hong TS; Wo JY; Ferrone CR; Tanabe KK; Bardeesy N; Straley KS; Agresta S; Schenkein DP; Ellisen LW; Ryan DP; Zhu AX
[Ad] Address:Authors' Affiliations: Massachusetts General Hospital Cancer Center, Harvard Medical School, Boston; Agios Pharmaceuticals, Cambridge, Massachusetts; and Queen Mary Hospital, The University of Hong Kong, Hong Kong, China.
[Ti] Title:Circulating oncometabolite 2-hydroxyglutarate is a potential surrogate biomarker in patients with isocitrate dehydrogenase-mutant intrahepatic cholangiocarcinoma.
[So] Source:Clin Cancer Res;20(7):1884-90, 2014 Apr 1.
[Is] ISSN:1078-0432
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:PURPOSE: Mutations in the IDH1 and IDH2 (IDH1/2) genes occur in approximately 20% of intrahepatic cholangiocarcinoma and lead to accumulation of 2-hydroxyglutarate (2HG) in the tumor tissue. However, it remains unknown whether IDH1/2 mutations can lead to high levels of 2HG circulating in the blood and whether serum 2HG can be used as a biomarker for IDH1/2 mutational status and tumor burden in intrahepatic cholangiocarcinoma. EXPERIMENTAL DESIGN: We initially measured serum 2HG concentration in blood samples collected from 31 patients with intrahepatic cholangiocarcinoma in a screening cohort. Findings were validated across 38 resected patients with intrahepatic cholangiocarcinoma from a second cohort with tumor volume measures. Circulating levels of 2HG were evaluated relative to IDH1/2 mutational status, tumor burden, and a number of clinical variables. RESULTS: Circulating levels of 2HG in the screening cohort were significantly elevated in patients with IDH1/2-mutant (median, 478 ng/mL) versus IDH1/2-wild-type (median, 118 ng/mL) tumors (P < 0.001). This significance was maintained in the validation cohort (343 ng/mL vs. 55 ng/mL, P < 0.0001) and levels of 2HG directly correlated with tumor burden in IDH1/2-mutant cases (P < 0.05). Serum 2HG levels ≥170 ng/mL could predict the presence of an IDH1/2 mutation with a sensitivity of 83% and a specificity of 90%. No differences were noted between the allelic variants IDH1 or IDH2 in regard to the levels of circulating 2HG. CONCLUSIONS: This study indicates that circulating 2HG may be a surrogate biomarker of IDH1 or IDH2 mutation status in intrahepatic cholangiocarcinoma and that circulating 2HG levels may correlate directly with tumor burden. Clin Cancer Res; 20(7); 1884-90. ©2014 AACR.
[Mh] MeSH terms primary: Bile Duct Neoplasms/genetics
Cholangiocarcinoma/genetics
Glutarates/blood
Isocitrate Dehydrogenase/genetics
Tumor Markers, Biological/blood
[Mh] MeSH terms secundary: Adult
Aged
Bile Duct Neoplasms/blood
Bile Duct Neoplasms/pathology
Bile Ducts, Intrahepatic/pathology
Cholangiocarcinoma/blood
Cholangiocarcinoma/pathology
Female
Humans
Isocitrate Dehydrogenase/blood
Male
Middle Aged
Mutation
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Name of substance:0 (Glutarates); 0 (Tumor Markers, Biological); 2889-31-8 (alpha-hydroxyglutarate); EC 1.1.1.41 (Isocitrate Dehydrogenase); EC 1.1.1.41 (isocitrate dehydrogenase 2, human); EC 1.1.1.42. (IDH1 protein, human)
[Em] Entry month:1411
[Cu] Class update date: 150117
[Lr] Last revision date:150117
[Js] Journal subset:IM
[Da] Date of entry for processing:140402
[St] Status:MEDLINE
[do] DOI:10.1158/1078-0432.CCR-13-2649


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