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[PMID]:28461070
[Au] Autor:Albulescu IC; Kovacikova K; Tas A; Snijder EJ; van Hemert MJ
[Ad] Endereço:Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Leiden, The Netherlands.
[Ti] Título:Suramin inhibits Zika virus replication by interfering with virus attachment and release of infectious particles.
[So] Source:Antiviral Res;143:230-236, 2017 07.
[Is] ISSN:1872-9096
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Zika virus (ZIKV) is a mosquito-borne flavivirus that mostly causes asymptomatic infections or mild disease characterized by low-grade fever, rash, conjunctivitis, and malaise. However, the recent massive ZIKV epidemics in the Americas have also linked ZIKV infection to fetal malformations like microcephaly and Guillain-Barré syndrome in adults, and have uncovered previously unrecognized routes of vertical and sexual transmission. Here we describe inhibition of ZIKV replication by suramin, originally an anti-parasitic drug, which was more recently shown to inhibit multiple viruses. In cell culture-based assays, using reduction of cytopathic effect as read-out, suramin had an EC of ∼40 µM and a selectivity index of 48. In single replication cycle experiments, suramin treatment also caused a strong dose-dependent decrease in intracellular ZIKV RNA levels and a >3-log reduction in infectious progeny titers. Time-of-addition experiments revealed that suramin inhibits a very early step of the replication cycle as well as the release of infectious progeny. Only during the first 2 h of infection suramin treatment strongly reduced the fraction of cells that became infected with ZIKV, suggesting the drug affects virus binding/entry. Binding experiments at 4 °C using S-labeled ZIKV demonstrated that suramin interferes with attachment to host cells. When suramin treatment was initiated post-entry, viral RNA synthesis was unaffected, while both the release of genomes and the infectivity of ZIKV were reduced. This suggests the compound also affects virion biogenesis, possibly by interfering with glycosylation and the maturation of ZIKV during its traffic through the secretory pathway. The inhibitory effect of suramin on ZIKV attachment and virion biogenesis and its broad-spectrum activity warrant further evaluation of this compound as a potential therapeutic.
[Mh] Termos MeSH primário: Suramina/antagonistas & inibidores
Vírion/efeitos dos fármacos
Ligação Viral/efeitos dos fármacos
Liberação de Vírus/efeitos dos fármacos
Replicação Viral/efeitos dos fármacos
Zika virus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Cercopithecus aethiops
Efeito Citopatogênico Viral/efeitos dos fármacos
Replicação do DNA/efeitos dos fármacos
Flavivirus/efeitos dos fármacos
Glicosilação/efeitos dos fármacos
Ácido Micofenólico/administração & dosagem
Ácido Micofenólico/antagonistas & inibidores
RNA Viral/análise
RNA Viral/biossíntese
RNA Viral/efeitos dos fármacos
Suramina/administração & dosagem
Fatores de Tempo
Células Vero
Internalização do Vírus/efeitos dos fármacos
Zika virus/crescimento & desenvolvimento
Zika virus/fisiologia
Infecção pelo Zika virus/tratamento farmacológico
Infecção pelo Zika virus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Viral); 6032D45BEM (Suramin); HU9DX48N0T (Mycophenolic Acid)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  2 / 2647 MEDLINE  
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[PMID]:28457855
[Au] Autor:Tan CW; Sam IC; Chong WL; Lee VS; Chan YF
[Ad] Endereço:Department of Medical Microbiology, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia. Electronic address: tancw86@gmail.com.
[Ti] Título:Polysulfonate suramin inhibits Zika virus infection.
[So] Source:Antiviral Res;143:186-194, 2017 07.
[Is] ISSN:1872-9096
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Zika virus (ZIKV) is an arthropod-borne flavivirus that causes newborn microcephaly and Guillian-Barré syndrome in adults. No therapeutics are available to treat ZIKV infection or other flaviviruses. In this study, we explored the inhibitory effect of glycosaminoglycans and analogues against ZIKV infection. Highly sulfated heparin, dextran sulfate and suramin significantly inhibited ZIKV infection in Vero cells. De-sulfated heparin analogues lose inhibitory effect, implying that sulfonate groups are critical for viral inhibition. Suramin, an FDA-approved anti-parasitic drug, inhibits ZIKV infection with 3-5 log PFU viral reduction with IC value of ∼2.5-5 µg/ml (1.93 µM-3.85 µM). A time-of-drug-addition study revealed that suramin remains potent even when administrated at 1-24 hpi. Suramin inhibits ZIKV infection by preventing viral adsorption, entry and replication. Molecular dynamics simulation revealed stronger interaction of suramin with ZIKV NS3 helicase than with the envelope protein. Suramin warrants further investigation as a potential antiviral candidate for ZIKV infection. Heparan sulfate (HS) is a cellular attachment receptor for multiple flaviviruses. However, no direct ZIKV-heparin interaction was observed in heparin-binding analysis, and downregulate or removal of cellular HS with sodium chlorate or heparinase I/III did not inhibit ZIKV infection. This indicates that cell surface HS is not utilized by ZIKV as an attachment receptor.
[Mh] Termos MeSH primário: Suramina/antagonistas & inibidores
Infecção pelo Zika virus/prevenção & controle
Zika virus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais
Cercopithecus aethiops
Cloratos/farmacologia
DNA Helicases/metabolismo
Sulfato de Dextrana/antagonistas & inibidores
Flavivirus/efeitos dos fármacos
Glicosaminoglicanos/farmacologia
Heparina/análogos & derivados
Heparina/química
Heparina/farmacologia
Heparitina Sulfato/farmacologia
Concentração Inibidora 50
Camundongos
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
RNA Helicases/química
RNA Helicases/efeitos dos fármacos
Serina Endopeptidases/química
Serina Endopeptidases/efeitos dos fármacos
Suramina/administração & dosagem
Células Vero
Proteínas do Envelope Viral/metabolismo
Proteínas não Estruturais Virais/química
Proteínas não Estruturais Virais/efeitos dos fármacos
Internalização do Vírus/efeitos dos fármacos
Replicação Viral/efeitos dos fármacos
Zika virus/fisiologia
Infecção pelo Zika virus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Chlorates); 0 (Glycosaminoglycans); 0 (NS3 protein, flavivirus); 0 (Viral Envelope Proteins); 0 (Viral Nonstructural Proteins); 6032D45BEM (Suramin); 9005-49-6 (Heparin); 9042-14-2 (Dextran Sulfate); 9050-30-0 (Heparitin Sulfate); EC 3.4.21.- (Serine Endopeptidases); EC 3.6.4.- (DNA Helicases); EC 3.6.4.13 (RNA Helicases); T95DR77GMR (sodium chlorate)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  3 / 2647 MEDLINE  
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[PMID]:29183030
[Au] Autor:Wang X; Li L; Guan R; Zhu D; Song N; Shen L
[Ad] Endereço:Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Fudan University, Shanghai, China.
[Ti] Título:Emodin Inhibits ATP-Induced Proliferation and Migration by Suppressing P2Y Receptors in Human Lung Adenocarcinoma Cells.
[So] Source:Cell Physiol Biochem;44(4):1337-1351, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Extracellular ATP performs multiple important functions via activation of P2 receptors on the cell surface. P2Y receptors play critical roles in ATP evoked response in human lung adenocarcinoma cells (A549 cells). Emodin is an anthraquinone derivative originally isolated from Chinese rhubarb, possesses anticancer properties. In this study we examined the inhibiting effects of emodin on proliferation, migration and epithelial-mesenchymal transition (EMT) by suppressing P2Y receptors-dependent Ca2+ increase and nuclear factor-κB (NF-KB) signaling in A549 cells. METHODS: A549 cells were pretreated with emodin before stimulation with ATP for the indicated time. Then, intracellular Ca2+ concentration ([Ca2+]i) was measured by Fluo-8/AM staining. Cell proliferation and cell cycle progression were tested by CCK8 assay and flow cytometry In addition, wound healing and western blot were performed to determine cell migration and related protein levels (Bcl-2, Bax, claudin-1, NF-κB). RESULTS: Emodin blunted ATP/UTP-induced increase of [Ca2+]i and cell proliferation concentration-dependently Meanwhile, it decreased ATP-induced cells accumulation in the S phase. Furthermore, emodin altered protein abundance of Bcl-2, Bax and claudin-1 and attenuated EMT caused by ATP. Such ATP-induced cellular reactions were also inhibited by a nonselective P2Y receptors antagonist, suramin, in a similar way to emodin. Besides, emodin could inhibit activation of NF-κB, thus suppressed ATP-induced proliferation, migration and EMT. CONCLUSION: Our results demonstrated that emodin inhibits ATP-induced proliferation, migration, EMT by suppressing P2Y receptors-mediated [Ca2+]i increase and NF-κB signaling in A549 cells.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/farmacologia
Proliferação Celular/efeitos dos fármacos
Emodina/toxicidade
Receptores Purinérgicos P2Y/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Células A549
Adenocarcinoma
Caderinas/metabolismo
Cálcio/metabolismo
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Claudina-1/metabolismo
Transição Epitelial-Mesenquimal/efeitos dos fármacos
Pontos de Checagem da Fase G1 do Ciclo Celular/efeitos dos fármacos
Seres Humanos
Neoplasias Pulmonares
Microscopia de Fluorescência
NF-kappa B/antagonistas & inibidores
NF-kappa B/metabolismo
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Antagonistas do Receptor Purinérgico P2Y/toxicidade
Receptores Purinérgicos P2Y/química
Receptores Purinérgicos P2Y/genética
Suramina/toxicidade
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (Claudin-1); 0 (NF-kappa B); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (Purinergic P2Y Receptor Antagonists); 0 (Receptors, Purinergic P2Y); 0 (bcl-2-Associated X Protein); 6032D45BEM (Suramin); 8L70Q75FXE (Adenosine Triphosphate); KA46RNI6HN (Emodin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1159/000485495


  4 / 2647 MEDLINE  
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[PMID]:28800362
[Au] Autor:Jiang P; Xing F; Guo B; Yang J; Li Z; Wei W; Hu F; Lee I; Zhang X; Pan L; Xu J
[Ad] Endereço:The Key Laboratory of Weak-Light Nonlinear Photonics, Ministry of Education, TEDA Institute of Applied Physics and School of Physics, Nankai University, Tianjin, China.
[Ti] Título:Nucleotide transmitters ATP and ADP mediate intercellular calcium wave communication via P2Y12/13 receptors among BV-2 microglia.
[So] Source:PLoS One;12(8):e0183114, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nerve injury is accompanied by a liberation of diverse nucleotides, some of which act as 'find/eat-me' signals in mediating neuron-glial interplay. Intercellular Ca2+ wave (ICW) communication is the main approach by which glial cells interact and coordinate with each other to execute immune defense. However, the detailed mechanisms on how these nucleotides participate in ICW communication remain largely unclear. In the present work, we employed a mechanical stimulus to an individual BV-2 microglia to simulate localized injury. Remarkable ICW propagation was observed no matter whether calcium was in the environment or not. Apyrase (ATP/ADP-hydrolyzing enzyme), suramin (broad-spectrum P2 receptor antagonist), 2-APB (IP3 receptor blocker) and thapsigargin (endoplasmic reticulum calcium pump inhibitor) potently inhibited these ICWs, respectively, indicating the dependence of nucleotide signals and P2Y receptors. Then, we detected the involvement of five naturally occurring nucleotides (ATP, ADP, UTP, UDP and UDP-glucose) by desensitizing receptors. Results showed that desensitization with ATP and ADP could block ICW propagation in a dose-dependent manner, whereas other nucleotides had little effect. Meanwhile, the expression of P2Y receptors in BV-2 microglia was identified and their contributions were analyzed, from which we suggested P2Y12/13 receptors activation mostly contributed to ICWs. Besides, we estimated that extracellular ATP and ADP concentration sensed by BV-2 microglia was about 0.3 µM during ICWs by analyzing calcium dynamic characteristics. Taken together, these results demonstrated that the nucleotides ATP and ADP were predominant signal transmitters in mechanical stimulation-induced ICW communication through acting on P2Y12/13 receptors in BV-2 microglia.
[Mh] Termos MeSH primário: Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Cálcio/metabolismo
Microglia/metabolismo
Receptores Purinérgicos P2Y12/metabolismo
Receptores Purinérgicos P2/metabolismo
[Mh] Termos MeSH secundário: Animais
Apirase/farmacologia
Fenômenos Biomecânicos
Compostos de Boro/farmacologia
Sinalização do Cálcio/efeitos dos fármacos
Comunicação Celular/efeitos dos fármacos
Linhagem Celular Transformada
Expressão Gênica
Fosfatos de Inositol/farmacologia
Mecanotransdução Celular/efeitos dos fármacos
Camundongos
Microglia/citologia
Microglia/efeitos dos fármacos
Imagem Molecular
Receptores Purinérgicos P2/genética
Receptores Purinérgicos P2Y12/genética
Suramina/farmacologia
Tapsigargina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-aminoethyl diphenylborinate); 0 (Boron Compounds); 0 (Inositol Phosphates); 0 (P2ry12 protein, mouse); 0 (P2ry13 protein, mouse); 0 (Receptors, Purinergic P2); 0 (Receptors, Purinergic P2Y12); 2831-74-5 (inositol 3-phosphate); 6032D45BEM (Suramin); 61D2G4IYVH (Adenosine Diphosphate); 67526-95-8 (Thapsigargin); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.5 (Apyrase); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183114


  5 / 2647 MEDLINE  
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[PMID]:28798097
[Au] Autor:Chanalaris A; Doherty C; Marsden BD; Bambridge G; Wren SP; Nagase H; Troeberg L
[Ad] Endereço:Arthritis Research UK Centre for Osteoarthritis Pathogenesis, Kennedy Institute of Rheumatology, (A.C., C.D., G.B., H.N., L.T.), Structural Genomics Consortium (B.D.M.), and Alzheimer's Research UK Oxford Drug Discovery Institute (S.P.W.), University of Oxford, Oxford, United Kingdom.
[Ti] Título:Suramin Inhibits Osteoarthritic Cartilage Degradation by Increasing Extracellular Levels of Chondroprotective Tissue Inhibitor of Metalloproteinases 3.
[So] Source:Mol Pharmacol;92(4):459-468, 2017 Oct.
[Is] ISSN:1521-0111
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Osteoarthritis is a common degenerative joint disease for which no disease-modifying drugs are currently available. Attempts to treat the disease with small molecule inhibitors of the metalloproteinases that degrade the cartilage matrix have been hampered by a lack of specificity. We aimed to inhibit cartilage degradation by augmenting levels of the endogenous metalloproteinase inhibitor, tissue inhibitor of metalloproteinases (TIMP)-3, through blocking its interaction with the endocytic scavenger receptor, low-density lipoprotein receptor-related protein 1 (LRP1). We discovered that suramin (C H N O S ) bound to TIMP-3 with a value of 1.9 ± 0.2 nM and inhibited its endocytosis via LRP1, thus increasing extracellular levels of TIMP-3 and inhibiting cartilage degradation by the TIMP-3 target enzyme, adamalysin-like metalloproteinase with thrombospondin motifs 5. NF279 (8,8'-[carbonyl (imino-4,1-phenylenecarbonylimino-4,1-phenylenecarbonylimino)] -1,3,5-naphthalenetrisulfonic acid hexasodium salt), a structural analog of suramin, has an increased affinity for TIMP-3 and increased ability to inhibit TIMP-3 endocytosis and protect cartilage. Suramin is thus a promising scaffold for the development of novel therapeutics to increase TIMP-3 levels and inhibit cartilage degradation in osteoarthritis.
[Mh] Termos MeSH primário: Cartilagem/metabolismo
Condrócitos/metabolismo
Espaço Extracelular/metabolismo
Osteoartrite/metabolismo
Suramina/uso terapêutico
Inibidor Tecidual de Metaloproteinase-3/metabolismo
[Mh] Termos MeSH secundário: Animais
Cartilagem/efeitos dos fármacos
Cartilagem/patologia
Linhagem Celular Tumoral
Condrócitos/efeitos dos fármacos
Condrócitos/patologia
Relação Dose-Resposta a Droga
Espaço Extracelular/efeitos dos fármacos
Células HEK293
Seres Humanos
Técnicas de Cultura de Órgãos
Osteoartrite/tratamento farmacológico
Osteoartrite/patologia
Ligação Proteica/fisiologia
Suramina/farmacologia
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (TIMP3 protein, human); 0 (Tissue Inhibitor of Metalloproteinase-3); 6032D45BEM (Suramin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE
[do] DOI:10.1124/mol.117.109397


  6 / 2647 MEDLINE  
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[PMID]:28760340
[Au] Autor:Lu JW; Hsieh PS; Lin CC; Hu MK; Huang SM; Wang YM; Liang CY; Gong Z; Ho YJ
[Ad] Endereço:Department of Biological Sciences, National University of Singapore, Singapore.
[Ti] Título:Synergistic effects of combination treatment using EGCG and suramin against the chikungunya virus.
[So] Source:Biochem Biophys Res Commun;491(3):595-602, 2017 Sep 23.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chikungunya is a severe disease that results from infection with the chikungunya virus (CHIKV), an arbovirus. Thus, we (1) explored a new approach to combining previously researched drugs that have shown the potential to inhibit CHIKV infection; and (2) demonstrated the antiviral effects of (-)-Epigallocatechin-3-gallate (EGCG) and the underlying mechanisms. Specifically, we used U2OS cells infected with CHIVK to assess the synergistic antiviral activities of EGCG and suramin. EGCG presented the ability to inhibit the viral RNA, progeny yield, and cytopathic effect (CPE) of CHIKV and also demonstrated the ability to protect against virus entry, replication, and release. Moreover, the results confirmed that EGCG and suramin can have synergistic effects against CHIKV strain S27 infection and two other clinical isolates of CHIKV. Our findings suggest that treatment with a combination of EGCG and suramin could provide a basis for the development of novel stretages against CHIKV infection.
[Mh] Termos MeSH primário: Catequina/análogos & derivados
Febre de Chikungunya/tratamento farmacológico
Febre de Chikungunya/virologia
Vírus Chikungunya/efeitos dos fármacos
Vírus Chikungunya/fisiologia
Suramina/administração & dosagem
[Mh] Termos MeSH secundário: Antivirais/administração & dosagem
Catequina/administração & dosagem
Relação Dose-Resposta a Droga
Combinação de Medicamentos
Sinergismo Farmacológico
Seres Humanos
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Drug Combinations); 6032D45BEM (Suramin); 8R1V1STN48 (Catechin); BQM438CTEL (epigallocatechin gallate)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE


  7 / 2647 MEDLINE  
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[PMID]:28624143
[Au] Autor:Berg A; Berg T
[Ad] Endereço:Institute of Organic Chemistry, Leipzig University, Johannisallee 29, 04103 Leipzig, Germany.
[Ti] Título:A small-molecule screen identifies the antitrypanosomal agent suramin and analogues NF023 and NF449 as inhibitors of STAT5a/b.
[So] Source:Bioorg Med Chem Lett;27(15):3349-3352, 2017 08 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The transcription factor STAT5a is a potential target for tumor therapy. We present a fluorescence polarization-based, high-throughput screen of chemical libraries containing natural products and known bioactive molecules, for the identification of small-molecule inhibitors of the STAT5a SH2 domain. This screen identified suramin, a drug used to treat African trypanosomiasis, and its analogues NF023 and NF449 as inhibitors of the SH2 domains of STAT5a/b. Our data extend the known in vitro targets of suramin and analogues to include members of the STAT protein family.
[Mh] Termos MeSH primário: Benzenossulfonatos/farmacologia
Ensaios de Triagem em Larga Escala
Fator de Transcrição STAT5/antagonistas & inibidores
Bibliotecas de Moléculas Pequenas/farmacologia
Suramina/farmacologia
Proteínas Supressoras de Tumor/antagonistas & inibidores
[Mh] Termos MeSH secundário: Benzenossulfonatos/síntese química
Benzenossulfonatos/química
Relação Dose-Resposta a Droga
Seres Humanos
Estrutura Molecular
Bibliotecas de Moléculas Pequenas/síntese química
Bibliotecas de Moléculas Pequenas/química
Relação Estrutura-Atividade
Suramina/análogos & derivados
Suramina/síntese química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (4,4,',4'',4'''-(carbonylbis(imino-5,1,3-benzenetriylbis(carbonylimino)))tetrakis(benzene-1,3-disulfonate)); 0 (Benzenesulfonates); 0 (STAT5 Transcription Factor); 0 (STAT5A protein, human); 0 (STAT5B protein, human); 0 (Small Molecule Libraries); 0 (Tumor Suppressor Proteins); 6032D45BEM (Suramin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170619
[St] Status:MEDLINE


  8 / 2647 MEDLINE  
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[PMID]:28322086
[Au] Autor:Örçen A; Yilmaz V; Giris M; Akcan U; Tüzün E; Erten G
[Ad] Endereço:Department of Neuroscience, Aziz Sancar Institute of Experimental Medicine, Istanbul University , Istanbul , Turkey.
[Ti] Título:Viability of SH-SY5Y cells is associated with purinergic P2 receptor expression alterations.
[So] Source:Acta Biol Hung;68(1):22-34, 2017 Mar.
[Is] ISSN:0236-5383
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:To investigate the role of metabotrophic purinergic P2Y receptors in neuroblastoma cell survival, expression of P2 receptors by normal mouse (C57BL/6) brain and human neuroblastoma SH-SY5Y cells was investigated by Western blot and real time PCR studies. Viability of SH-SY5Y cells treated with purinergic receptor antagonists suramin and pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate (PPADS) was evaluated by MTT assay and flow cytometry. In the brain samples of C57BL/6 mice, expressions of P2Y4 and P2X7 were significantly reduced, whereas that of P2Y1 was significantly elevated in an age-dependent manner. SH-SY5Y cell viability was significantly reduced and necrotic cell rates were mildly increased by 400 µM suramin and 100 µM PPADS treatment. Antagonist treatment downregulated P2Y1, P2Y2 and P2Y4 and upregulated P2Y6, P2Y12 and P2X7 mRNA levels in SH-SY5Y cells on the 24th hour. These alterations were abolished for all P2 receptors except P2Y1 in the 48th hour. P2Y receptors are expressed by both normal mouse brain and human neuroblastoma cells. Purinergic receptor antagonism interferes with neuroblastoma viability through elevation of necrotic cell death and modulation of P2 receptor expression. P2Y receptors might thus be useful targets for future anti-tumor treatment trials.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica/genética
Receptores Purinérgicos P2/genética
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/genética
Citometria de Fluxo
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Immunoblotting
Masculino
Camundongos Endogâmicos C57BL
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Antagonistas do Receptor Purinérgico P2/farmacologia
Fosfato de Piridoxal/análogos & derivados
Fosfato de Piridoxal/farmacologia
Receptores Purinérgicos P2/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Suramina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); 0 (Purinergic P2 Receptor Antagonists); 0 (Receptors, Purinergic P2); 149017-66-3 (pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid); 5V5IOJ8338 (Pyridoxal Phosphate); 6032D45BEM (Suramin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1556/018.68.2017.1.3


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[PMID]:28217922
[Au] Autor:Doleski PH; Adefegha SA; Cabral FL; Leal DB
[Ad] Endereço:Program of Biochemistry and Molecular Biology, Federal University of Santa Maria, Santa Maria, RS, Brazil.
[Ti] Título:Characterization of E-NTPDase (EC 3.6.1.5) activity in hepatic lymphocytes: A different activity profile from peripheral lymphocytes.
[So] Source:Cell Biochem Funct;35(2):105-112, 2017 Mar.
[Is] ISSN:1099-0844
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The activity of ectonucleoside triphosphate diphosphohydrolase (E-NTPDase; EC 3.6.1.5) was characterized in hepatic lymphocytes (HL) of rats. For this purpose, a specific method for the isolation of lymphocytes from hepatic tissue was developed. Subsequently, E-NTPDase activity of rat HL was compared with that of rat peripheral lymphocytes. The HL showed high cell count and viability. Also, the characterization test revealed that the optimal E-NTPDase activities were attained at 37°C and pH 8.0 in the presence of Ca . In addition, in the presence of specific E-NTPDase inhibitors (20mM sodium azide and 0.3mM suramin), there were significant inhibitions in nucleotide hydrolysis. However, there was no significant change in adenosine triphosphate (ATP) or adenosine diphosphate (ADP) hydrolysis in the presence of inhibitors of other E-ATPase (0.1mM Ouabain, 0.5mM orthovanadate, and 1mM, 5mM, and 10mM sodium azide). Furthermore, the kinetic behavior of the enzyme in HL showed apparent Km of 134.90 ± 0.03µM and 214.40 ± 0.06µM as well as Vmax of 345.0 ± 28.32 and 242.0 ± 27.55 Æžmol Pi/min/mg of protein for ATP and ADP, respectively. The Chevillard plot revealed that ATP and ADP were hydrolyzed at the same active site of the enzyme. Our results suggest that the degradation of extracellular nucleotides in HL may have been primarily accomplished by E-NTPDase. The higher E-NTPDase activity observed in HL may be attributed to the important physiological functions of ATP and ADP in HL. SIGNIFICANCE OF THE STUDY: Extracellular purine nucleotides are able to interact with specific receptors and trigger a number of important physiological functions in cells. This interaction is controlled by ectonucleoside triphosphate diphosphohydrolase (E-NTPDase), enzyme that present their catalytic site at the extracellular space and degrades nucleotides. This purinergic signaling has important functions in peripheral lymphocytes and may represent an important new therapeutic target for the treatment of immunological diseases. However, there is dearth of information on the involvement of E-NTPDase in liver lymphocytes. The liver is an important organ, which performs both metabolic and toxicological roles in living organism, and hepatic lymphocytes may play crucial action in the regulation of immune responses in the liver tissue. Furthermore, various chronic diseases such as cirrhosis may be treated with novel pharmacotherapy by targeting the modulation of hepatic lymphocytes. Thus, the significance of this study is to evaluate the activity of E-NTPDase in liver lymphocyte and compare its activity with the peripheral lymphocytes.
[Mh] Termos MeSH primário: Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Antígenos CD/metabolismo
Apirase/metabolismo
Células Sanguíneas/enzimologia
Fígado/enzimologia
Linfócitos/enzimologia
[Mh] Termos MeSH secundário: Animais
Antígenos CD/genética
Apirase/antagonistas & inibidores
Apirase/genética
Células Sanguíneas/citologia
Células Sanguíneas/efeitos dos fármacos
Cálcio/metabolismo
Cátions Bivalentes
Separação Celular/métodos
Ensaios Enzimáticos
Inibidores Enzimáticos/farmacologia
Expressão Gênica
Concentração de Íons de Hidrogênio
Cinética
Fígado/citologia
Fígado/efeitos dos fármacos
Linfócitos/citologia
Linfócitos/efeitos dos fármacos
Masculino
Especificidade de Órgãos
Ouabaína/farmacologia
Ratos
Ratos Wistar
Azida Sódica/farmacologia
Especificidade por Substrato
Suramina/farmacologia
Vanadatos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Cations, Divalent); 0 (Enzyme Inhibitors); 3WHH0066W5 (Vanadates); 5ACL011P69 (Ouabain); 6032D45BEM (Suramin); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); 968JJ8C9DV (Sodium Azide); EC 3.6.1.5 (Apyrase); EC 3.6.1.5 (CD39 antigen); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170317
[Lr] Data última revisão:
170317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE
[do] DOI:10.1002/cbf.3253


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[PMID]:28189815
[Au] Autor:Sahu D; Sharma S; Singla RK; Panda AK
[Ad] Endereço:Product Development Cell, National Institute of Immunology, New Delhi 110067, India. Electronic address: sahudebasis@nii.ac.in.
[Ti] Título:Antioxidant activity and protective effect of suramin against oxidative stress in collagen induced arthritis.
[So] Source:Eur J Pharm Sci;101:125-139, 2017 Apr 01.
[Is] ISSN:1879-0720
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:It is imperative to interrupt the link between arthritis and regulation of oxidative stress with the administration of antioxidants. Suramin is known for its anti-inflammatory, antineoplastic and antiangiogenic activities implying its possible antioxidant property. In this study, the antioxidant activity of suramin in cell free system was found to be higher than l-ascorbic acid (l-AA) with respect to its scavenging effect on nitric oxide (NO), hypochlorous acid and hydrogen peroxide radicals. Besides, suramin was found to be nontoxic to cultured RAW cells even at high concentrations along with marked inhibition of NO production. Suramin was found to curb the inflammation associated with the collagen induced arthritis (CIA) model. Administration of suramin significantly reduced the malondialdehyde and protein carbonyl content in joints, liver, kidney and spleen of rats as studied ex vivo. Furthermore, the increased antioxidant enzymes such as SOD, catalase, GST, GPx and GR activities in the tissues were restored significantly after suramin treatment. In silico experiments using Vlife MDS4.4-GRIP docking method showed strong affinity of suramin towards erythrocyte catalase followed by glutathione peroxidase thus corroborating with the findings of antioxidant enzyme assays. Our studies clearly indicate that suramin has remarkable antioxidant potential and can ameliorate arthritis via modulation of oxidative stress.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Artrite Experimental/induzido quimicamente
Artrite Experimental/tratamento farmacológico
Colágeno/farmacologia
Estresse Oxidativo/efeitos dos fármacos
Substâncias Protetoras/farmacologia
Suramina/farmacologia
[Mh] Termos MeSH secundário: Animais
Artrite Experimental/metabolismo
Ácido Ascórbico/metabolismo
Catalase/metabolismo
Linhagem Celular
Feminino
Glutationa/metabolismo
Glutationa Peroxidase/metabolismo
Glutationa Redutase/metabolismo
Glutationa Transferase/metabolismo
Peróxido de Hidrogênio/metabolismo
Peroxidação de Lipídeos/efeitos dos fármacos
Malondialdeído/metabolismo
Camundongos
Óxido Nítrico/metabolismo
Oxirredução/efeitos dos fármacos
Carbonilação Proteica/efeitos dos fármacos
Ratos
Ratos Wistar
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Protective Agents); 31C4KY9ESH (Nitric Oxide); 4Y8F71G49Q (Malondialdehyde); 6032D45BEM (Suramin); 9007-34-5 (Collagen); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); EC 1.8.1.7 (Glutathione Reductase); EC 2.5.1.18 (Glutathione Transferase); GAN16C9B8O (Glutathione); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170213
[St] Status:MEDLINE



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