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  1 / 3105 MEDLINE  
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[PMID]:29328669
[Au] Autor:Feng Y; Wang S; Wang H; Peng Y; Zheng J
[Ad] Endereço:Wuya College of Innovation, Shenyang Pharmaceutical University , Shenyang, Liaoning 110016, People's Republic of China.
[Ti] Título:Urinary Methyleugenol-deoxyadenosine Adduct as a Potential Biomarker of Methyleugenol Exposure in Rats.
[So] Source:J Agric Food Chem;66(5):1258-1263, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Methyleugenol (ME), a natural ingredient of several herbs and spices used in the human diet, is hepatocarcinogenic in rodents. Following metabolic activation to the reactive carbocation intermediate, ME can bind covalently to DNA, which is directly associated with its carcinogenicity. In this work, a non-invasive approach to determine ME exposure was established by monitoring the urinary N -(methylisoeugenol-3'-yl)-2'-deoxyadenosine (ME-dA) adduct. The developed method entails liquid-liquid extraction enrichment of urinary ME-dA, incorporation of deuterated ME-dA as an internal standard, and analysis by liquid chromatography coupled tandem mass spectrometry. Male rats (10-12 weeks, 180-200 g) were treated (p.o.) with ME, and ME-dA was excreted in urine in a dose- and time-dependent manner. The non-invasive approach enabled us to successfully determine exposure to ME-containing herbs and spices. These results suggest that ME-dA can potentially serve as an effective biomarker of ME exposure in rats. It is expected that the developed approach of detecting urinary ME-dA will facilitate the investigation of ME carcinogenesis.
[Mh] Termos MeSH primário: Biomarcadores/urina
Carcinógenos
Adutos de DNA/urina
Desoxiadenosinas/urina
Eugenol/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Eugenol/análise
Eugenol/toxicidade
Eugenol/urina
Neoplasias Hepáticas/induzido quimicamente
Masculino
Ratos
Ratos Sprague-Dawley
Especificidade da Espécie
Especiarias/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Carcinogens); 0 (DNA Adducts); 0 (Deoxyadenosines); 29T9VA6R7M (methyleugenol); 3T8H1794QW (Eugenol)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05186


  2 / 3105 MEDLINE  
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[PMID]:29045468
[Au] Autor:Hwang IH; Oh SY; Jang HJ; Jo E; Joo JC; Lee KB; Yoo HS; Lee MY; Park SJ; Jang IS
[Ad] Endereço:Department of Physiology, Korea University College of Medicine, Seoul, Republic of Korea.
[Ti] Título:Cordycepin promotes apoptosis in renal carcinoma cells by activating the MKK7-JNK signaling pathway through inhibition of c-FLIPL expression.
[So] Source:PLoS One;12(10):e0186489, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular FLICE inhibitory protein (c-FLIP) is a key anti-apoptotic regulator that associates with the signaling complex downstream of NF-κB, negatively interfering with apoptotic signaling. The role of c-FLIP downregulation by negative regulation of NF-κB signaling during apoptosis is poorly understood. Here, we demonstrate that NF-κB-mediated c-FLIPL negatively regulates the JNK signaling pathway, and that cordycepin treatment of human renal cancer cells leads to apoptosis induction through c-FLIPL inhibition. TNF-α-induced inflammatory microenvironments stimulated NF-κB signaling and the c-FLIP long form (c-FLIPL) in TK-10 cells. Specifically, cordycepin inhibited TNF-α-mediated NF-κB activation, which induced renal cancer cell apoptosis. Cordycepin downregulated GADD45B and c-FLIPL, but upregulated MKK7 and phospho-JNK, by preventing nuclear mobilization of NF-κB. Furthermore, siRNA-mediated knockdown of GADD45B in cordycepin-treated TK-10 cells considerably increased MKK7 compared to cordycepin alone. siRNA-mediated knockdown of c-FLIPL prevented TNF-α-induced JNK inactivation, whereas c-FLIPL overexpression inhibited cordycepin-mediated JNK activation. The JNK inhibitor SP600125 strongly inhibited Bax expression. In nude mice, cordycepin significantly decreased tumor volume. Taken together, the results indicate that cordycepin inhibits TNF-α-mediated NF-κB/GADD45B signaling, which activates the MKK7-JNK signaling pathway through inhibition of c-FLIPL expression, thus inducing TK-10 cell apoptosis.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Proteína Reguladora de Apoptosis Semelhante a CASP8 e FADD/metabolismo
Carcinoma de Células Renais/enzimologia
Carcinoma de Células Renais/patologia
Desoxiadenosinas/farmacologia
MAP Quinase Quinase 7/metabolismo
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Antígenos de Diferenciação/metabolismo
Apoptose/genética
Carcinoma de Células Renais/genética
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Movimento Celular/genética
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/genética
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Células HEK293
Seres Humanos
Inflamação/patologia
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Neoplasias Renais/enzimologia
Neoplasias Renais/genética
Neoplasias Renais/patologia
Sistema de Sinalização das MAP Quinases/genética
Masculino
Camundongos Endogâmicos BALB C
Camundongos Nus
NF-kappa B/metabolismo
Óxido Nítrico/metabolismo
Fosforilação/efeitos dos fármacos
Regiões Promotoras Genéticas/genética
Fator de Necrose Tumoral alfa/farmacologia
Regulação para Cima/efeitos dos fármacos
Regulação para Cima/genética
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Differentiation); 0 (CASP8 and FADD-Like Apoptosis Regulating Protein); 0 (Deoxyadenosines); 0 (GADD45B protein, human); 0 (NF-kappa B); 0 (Tumor Necrosis Factor-alpha); 0 (bcl-2-Associated X Protein); 31C4KY9ESH (Nitric Oxide); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 2.7.12.2 (MAP Kinase Kinase 7); EC 2.7.12.2 (MAP2K7 protein, human); GZ8VF4M2J8 (cordycepin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186489


  3 / 3105 MEDLINE  
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[PMID]:28870956
[Au] Autor:Bi YE; Zhou Y; Wang M; Li L; Lee RJ; Xie J; Teng L
[Ad] Endereço:Jilin University, College of Life Science, P. R. China.
[Ti] Título:Targeted Delivery of Cordycepin to Liver Cancer Cells Using Transferrin-conjugated Liposomes.
[So] Source:Anticancer Res;37(9):5207-5214, 2017 09.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Cordycepin is an endogenous nucleoside with significant anticancer biological activity. The objective of this study was to develop targeted liposomes to improve solubility and biological activity of cordycepin. MATERIALS AND METHODS: We established transferrin-conjugated liposomes to deliver cordycepin to liver cancer cells and evaluated the uptake and effect. RESULTS: The liposomes were loaded with cordycepin. Their average size was 125.3 nm, with drug encapsulation efficiency of 65.3%. The liposomes had good colloidal stability and released cordycepin slowly. Liposomal cordycepin was shown to increase reactive oxygen species production and cause depolarization of the mitochondrial transmembrane in liver cancer cells. Cellular uptake of liposomal cordycepin was enhanced by conjugation to transferrin, that facilitated receptor-mediated endocytosis. CONCLUSION: Transferrin-conjugated liposomes are effective as nanocarriers for cordycepin delivery to liver cancer cells.
[Mh] Termos MeSH primário: Desoxiadenosinas/uso terapêutico
Sistemas de Liberação de Medicamentos
Neoplasias Hepáticas/tratamento farmacológico
Transferrina/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Desoxiadenosinas/farmacologia
Fluorescência
Seres Humanos
Lipossomos
Neoplasias Hepáticas/patologia
Neoplasias Hepáticas/ultraestrutura
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Tamanho da Partícula
Espécies Reativas de Oxigênio/metabolismo
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Liposomes); 0 (Reactive Oxygen Species); 0 (Transferrin); GZ8VF4M2J8 (cordycepin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


  4 / 3105 MEDLINE  
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[PMID]:28862845
[Au] Autor:Xu Y; Wang L; Chen J; Zhao J; Fan S; Dong Y; Ha NC; Quan C
[Ad] Endereço:Department of Bioengineering, College of Life Science, Dalian Minzu University , Dalian 116600, Liaoning, China.
[Ti] Título:Structural and Functional Analyses of Periplasmic 5'-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase from Aeromonas hydrophila.
[So] Source:Biochemistry;56(40):5347-5355, 2017 Oct 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Gram-negative, rod-shaped bacterium Aeromonas hydrophila has two multifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) enzymes, MtaN-1 and MtaN-2, that differ from those in other bacteria. These proteins are essential for several metabolic pathways, including biological methylation, polyamine biosynthesis, methionine recycling, and bacterial quorum sensing. To gain insight into how these two proteins function, we determined four high-resolution crystal structures of MtaN-1 in its apo form and in complex with the substrates S-adenosyl-l-homocysteine, 5'-methylthioadenosine, and 5'-deoxyadenosine. We found that the domain structures were generally similar, although slight differences were evident. The crystal structure demonstrates that AhMtaN-1 has an extension of the binding pocket and revealed that a tryptophan in the active site (Trp199) may play a major role in substrate binding, unlike in other MTAN proteins. Mutation of the Trp199 residue completely abolished the enzyme activity. Trp199 was identified as an active site residue that is essential for catalysis. Furthermore, biochemical characterization of AhMtaN-1 and AhMtaN-2 demonstrated that AhMtaN-1 exhibits inherent trypsin resistance that is higher than that of AhMtaN-2. Additionally, the thermally unfolded AhMtaN-2 protein is capable of refolding into active forms, whereas the thermally unfolded AhMtaN-1 protein does not have this ability. Examining the different biochemical characteristics related to the functional roles of AhMtaN-1 and AhMtaN-2 would be interesting. Indeed, the biochemical characterization of these structural features would provide a structural basis for the design of new antibiotics against A. hydrophila.
[Mh] Termos MeSH primário: Aeromonas hydrophila/citologia
Aeromonas hydrophila/enzimologia
Desoxiadenosinas/metabolismo
N-Glicosil Hidrolases/química
N-Glicosil Hidrolases/metabolismo
Periplasma/enzimologia
Tionucleosídeos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Modelos Moleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Thionucleosides); 634Z2VK3UQ (5'-methylthioadenosine); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.9 (adenosylhomocysteine nucleosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00691


  5 / 3105 MEDLINE  
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[PMID]:28807574
[Au] Autor:Brockway AJ; Volkov OA; Cosner CC; MacMillan KS; Wring SA; Richardson TE; Peel M; Phillips MA; De Brabander JK
[Ad] Endereço:Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9038, USA.
[Ti] Título:Synthesis and evaluation of analogs of 5'-(((Z)-4-amino-2-butenyl)methylamino)-5'-deoxyadenosine (MDL 73811, or AbeAdo) - An inhibitor of S-adenosylmethionine decarboxylase with antitrypanosomal activity.
[So] Source:Bioorg Med Chem;25(20):5433-5440, 2017 Oct 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We describe our efforts to improve the pharmacokinetic properties of a mechanism-based suicide inhibitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (AdoMetDC), essential for the survival of the eukaryotic parasite Trypanosoma brucei responsible for Human African Trypanosomiasis (HAT). The lead compound, 5'-(((Z)-4-amino-2-butenyl)methylamino)-5'-deoxyadenosine (1, also known as MDL 73811, or AbeAdo), has curative efficacy at a low dosage in a hemolymphatic model of HAT but displayed no demonstrable effect in a mouse model of the CNS stage of HAT due to poor blood-brain barrier permeation. Therefore, we prepared and evaluated an extensive set of analogs with modifications in the aminobutenyl side chain, the 5'-amine, the ribose, and the purine fragments. Although we gained valuable structure-activity insights from this comprehensive dataset, we did not gain traction on improving the prospects for CNS penetration while retaining the potent antiparasitic activity and metabolic stability of the lead compound 1.
[Mh] Termos MeSH primário: Adenosilmetionina Descarboxilase/antagonistas & inibidores
Desoxiadenosinas/farmacologia
Inibidores Enzimáticos/farmacologia
Tripanossomicidas/farmacologia
Trypanosoma brucei brucei/efeitos dos fármacos
Tripanossomíase Africana/tratamento farmacológico
[Mh] Termos MeSH secundário: Adenosilmetionina Descarboxilase/metabolismo
Animais
Desoxiadenosinas/síntese química
Desoxiadenosinas/química
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Camundongos
Conformação Molecular
Testes de Sensibilidade Parasitária
Relação Estrutura-Atividade
Tripanossomicidas/síntese química
Tripanossomicidas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Enzyme Inhibitors); 0 (Trypanocidal Agents); 7GI49JB39O (MDL 73811); EC 4.1.1.50 (Adenosylmethionine Decarboxylase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE


  6 / 3105 MEDLINE  
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[PMID]:28752893
[Au] Autor:Honarmand Ebrahimi K; Carr SB; McCullagh J; Wickens J; Rees NH; Cantley J; Armstrong FA
[Ad] Endereço:Department Chemistry, University of Oxford, UK.
[Ti] Título:The radical-SAM enzyme Viperin catalyzes reductive addition of a 5'-deoxyadenosyl radical to UDP-glucose in vitro.
[So] Source:FEBS Lett;591(16):2394-2405, 2017 Aug.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Viperin, a radical-S-adenosylmethionine (SAM) enzyme conserved from fungi to humans, can restrict replication of many viruses. Neither the molecular mechanism underlying the antiviral activity of Viperin, nor its exact physiological function, is understood: most importantly, no radical-SAM activity has been discovered for Viperin. Here, using electron paramagnetic resonance (EPR) spectroscopy, mass spectrometry, and NMR spectroscopy, we show that uridine diphosphate glucose (UDP-glucose) is a substrate of a fungal Viperin (58% pairwise identity with human Viperin at the amino acid level) in vitro. Structural homology modeling and docking experiments reveal a highly conserved binding pocket in which the position of UDP-glucose is consistent with our experimental data regarding catalytic addition of a 5'-deoxyadenosyl radical and a hydrogen atom to UDP-glucose.
[Mh] Termos MeSH primário: Biocatálise
Desoxiadenosinas/metabolismo
Proteínas Fúngicas/metabolismo
S-Adenosilmetionina/metabolismo
Uridina Difosfato Glucose/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência Conservada
Desoxiadenosinas/química
Radicais Livres/química
Radicais Livres/metabolismo
Proteínas Fúngicas/química
Hidrogênio
Simulação de Acoplamento Molecular
Oxirredução
Conformação Proteica
Sordariales/enzimologia
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Free Radicals); 0 (Fungal Proteins); 7LP2MPO46S (S-Adenosylmethionine); 7YNJ3PO35Z (Hydrogen); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170729
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12769


  7 / 3105 MEDLINE  
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[PMID]:28750234
[Au] Autor:Wada T; Sumardika IW; Saito S; Ruma IMW; Kondo E; Shibukawa M; Sakaguchi M
[Ad] Endereço:Chemicals Evaluation and Research Institute, Japan (CERI), CERI Tokyo, Environmental Technology Department, 1600, Shimotakano, Sugito-machi, Kitakatsushika-gun, Saitama 345-0043, Japan; Graduate School of Science and Engineering, Saitama University, 255, Shimo-Okubo, Sakura, Saitama 338-8570, Japan.
[Ti] Título:Identification of a novel component leading to anti-tumor activity besides the major ingredient cordycepin in Cordyceps militaris extract.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1061-1062:209-219, 2017 Sep 01.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In accordance with our previous study that was carried out to identify novel anti-tumor ingredients, chromatographic separation in combination with an anti-tumor activity assay was used for analysis of Cordyceps militaris extract in this study. Various modes of chromatography including reversed-phase, cation-exchange and anion-exchange were used to separate components of Cordyceps militaris, which showed various chemical properties. Anti-tumor activity of each fraction was assessed by a Hoechst staining-based apoptosis assay using malignant melanoma MeWo cells. By these repeated approaches through chromatographic segregation and cell biological assay, we finally succeeded in identifying the target substance from a certain fraction that included neutral hydrophilic components using a pre-column and post-column chlorine adduct ionization LC-APCI-MS method. The target substance was a mono-carbohydrate, xylitol, that induced apoptotic cell death in MeWo cells but not in normal human OUMS-24 fibroblasts. This is the first study showing that Cordyceps militaris extract contains a large amount of xylitol. Thus, our results will contribute greatly to uncovering the mysterious multifunctional herbal drug Cordyceps militaris as an anti-tumor agent.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Apoptose/efeitos dos fármacos
Produtos Biológicos/farmacologia
Cordyceps/química
[Mh] Termos MeSH secundário: Antineoplásicos/química
Produtos Biológicos/química
Linhagem Celular Tumoral
Cromatografia Líquida
Desoxiadenosinas/farmacologia
Seres Humanos
Xilitol/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Biological Products); 0 (Deoxyadenosines); GZ8VF4M2J8 (cordycepin); VCQ006KQ1E (Xylitol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE


  8 / 3105 MEDLINE  
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[PMID]:28737232
[Au] Autor:Stellrecht CM; Chen LS; Ayres ML; Dennison JB; Shentu S; Chen Y; Keating MJ; Wierda WG; Gandhi V
[Ad] Endereço:Department of Experimental Therapeutics, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.
[Ti] Título:Chlorinated adenosine analogue induces AMPK and autophagy in chronic lymphocytic leukaemia cells during therapy.
[So] Source:Br J Haematol;179(2):266-271, 2017 Oct.
[Is] ISSN:1365-2141
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:8-chloro-adenosine (8-Cl-Ado) is currently in phase-I clinical trials for acute myeloid leukaemia and chronic lymphocytic leukaemia (CLL). Previously, we demonstrated that treatment with 8-Cl-Ado leads to diminished ATP levels. We hypothesized that AMP-activated protein kinase (AMPK) signalling would be initiated in these cells, leading to induction of autophagy. AMPK activation and induction of autophagy were demonstrated during preclinical incubations in CLL cells with the analogues. Importantly, we extended similar observations in CLL lymphocytes during an 8-Cl-Ado phase-I trial. In conclusion, 8-Cl-Ado treatment induces autophagy in CLL lymphocytes in vitro as well as in vivo during clinical trial.
[Mh] Termos MeSH primário: Proteínas Quinases Ativadas por AMP/metabolismo
Autofagia/efeitos dos fármacos
Desoxiadenosinas/farmacologia
Leucemia Linfocítica Crônica de Células B
Linfócitos
[Mh] Termos MeSH secundário: Ensaios Clínicos Fase I como Assunto
Indução Enzimática
Feminino
Seres Humanos
Leucemia Linfocítica Crônica de Células B/tratamento farmacológico
Leucemia Linfocítica Crônica de Células B/enzimologia
Leucemia Linfocítica Crônica de Células B/patologia
Linfócitos/enzimologia
Linfócitos/patologia
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (8-chlorodeoxyadenosine); 0 (Deoxyadenosines); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1111/bjh.14859


  9 / 3105 MEDLINE  
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[PMID]:28714368
[Au] Autor:Cao HL; Liu ZJ; Chang Z
[Ad] Endereço:1 Department of Medical Oncology, Shandong Jiaotong Hospital, Jinan, China.
[Ti] Título:Cordycepin induces apoptosis in human bladder cancer cells via activation of A3 adenosine receptors.
[So] Source:Tumour Biol;39(7):1010428317706915, 2017 Jul.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bladder cancer is a neoplasm originated from bladder epithelial cells. The therapy for bladder cancer is so far not satisfactory. In this study, we examined the effects of Cordyceps militaris hot water extracts containing cordycepin on human bladder cells. Cordyceps militaris hot water extracts containing cordycepin was used to treat human T24 bladder carcinoma cells, and we found that Cordyceps militaris hot water extracts containing cordycepin decreased T24 cell survival in a dose-dependent manner, which was seemingly mediated by activation of A3 adenosine receptor and the subsequent inactivation of Akt pathways, resulting in increases in cleaved Caspase-3 and apoptosis. Overexpression of A3 adenosine receptor in T24 cells mimicked the effects of Cordyceps militaris hot water extracts, while A3 adenosine receptor depletion abolished the effects of Cordyceps militaris hot water extracts containing cordycepin. Together, these data suggest that Cordyceps militaris hot water extracts containing cordycepin may be a promising treatment for bladder cancer via A3 adenosine receptor activation.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Desoxiadenosinas/administração & dosagem
Receptor A3 de Adenosina/genética
Neoplasias da Bexiga Urinária/tratamento farmacológico
[Mh] Termos MeSH secundário: Caspase 3/genética
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Cordyceps/química
Desoxiadenosinas/química
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Proteína Oncogênica v-akt/genética
Extratos Vegetais/administração & dosagem
Extratos Vegetais/química
Transdução de Sinais/efeitos dos fármacos
Neoplasias da Bexiga Urinária/genética
Neoplasias da Bexiga Urinária/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Plant Extracts); 0 (Receptor, Adenosine A3); EC 2.7.11.1 (Oncogene Protein v-akt); EC 3.4.22.- (Caspase 3); GZ8VF4M2J8 (cordycepin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317706915


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[PMID]:28692281
[Au] Autor:Buchko GW; Echols N; Flynn EM; Ng HL; Stephenson S; Kim HB; Myler PJ; Terwilliger TC; Alber T; Kim CY
[Ad] Endereço:Seattle Structural Genomics Center for Infectious Diseases.
[Ti] Título:Structural and Biophysical Characterization of the Mycobacterium tuberculosis Protein Rv0577, a Protein Associated with Neutral Red Staining of Virulent Tuberculosis Strains and Homologue of the Streptomyces coelicolor Protein KbpA.
[So] Source:Biochemistry;56(30):4015-4027, 2017 Aug 01.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycobacterium tuberculosis protein Rv0577 is a prominent antigen in tuberculosis patients, the component responsible for neutral red staining of virulent strains of M. tuberculosis, a putative component in a methylglyoxal detoxification pathway, and an agonist of toll-like receptor 2. It also has an amino acid sequence that is 36% identical to that of Streptomyces coelicolor AfsK-binding protein A (KbpA), a component in the complex secondary metabolite pathways in the Streptomyces genus. To gain insight into the biological function of Rv0577 and the family of KpbA kinase regulators, the crystal structure for Rv0577 was determined to a resolution of 1.75 Å, binding properties with neutral red and deoxyadenosine were surveyed, backbone dynamics were measured, and thermal stability was assayed by circular dichroism spectroscopy. The protein is composed of four approximate repeats with a ßαßßß topology arranged radially in consecutive pairs to form two continuous eight-strand ß-sheets capped on both ends with an α-helix. The two ß-sheets intersect in the center at roughly a right angle and form two asymmetric deep "saddles" that may serve to bind ligands. Nuclear magnetic resonance chemical shift perturbation experiments show that neutral red and deoxyadenosine bind to Rv0577. Binding to deoxyadenosine is weaker with an estimated dissociation constants of 4.1 ± 0.3 mM for saddle 1. Heteronuclear steady-state { H}- N nuclear Overhauser effect, T , and T values were generally uniform throughout the sequence with only a few modest pockets of differences. Circular dichroism spectroscopy characterization of the thermal stability of Rv0577 indicated irreversible unfolding upon heating with an estimated melting temperature of 56 °C.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Desoxiadenosinas/metabolismo
Modelos Moleculares
Mycobacterium tuberculosis/metabolismo
Vermelho Neutro/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação
Proteínas de Transporte/química
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Dicroísmo Circular
Cristalografia por Raios X
Desoxiadenosinas/química
Temperatura Alta/efeitos adversos
Cinética
Ligantes
Conformação Molecular
Vermelho Neutro/química
Isótopos de Nitrogênio
Ressonância Magnética Nuclear Biomolecular
Conformação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Estabilidade Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Streptomyces coelicolor/metabolismo
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (Cfp32 protein, Mycobacterium tuberculosis); 0 (Deoxyadenosines); 0 (KbpA protein, Steptomyces coelicolor); 0 (Ligands); 0 (Nitrogen Isotopes); 0 (Recombinant Fusion Proteins); 261QK3SSBH (Neutral Red); P582C98ULC (2'-deoxyadenosine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00511



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