Base de dados : MEDLINE
Pesquisa : G04.198.337 [Categoria DeCS]
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[PMID]:27693845
[Au] Autor:Tawara S; Sakai T; Matsuzaki O
[Ad] Endereço:Laboratory for Pharmacology, Pharmaceuticals Research Center, Asahi Kasei Pharma Corporation, Shizuoka, Japan. Electronic address: tawara.sc@om.asahi-kasei.co.jp.
[Ti] Título:Anti-inflammatory and anti-fibrinolytic effects of thrombomodulin alfa through carboxypeptidase B2 in the presence of thrombin.
[So] Source:Thromb Res;147:72-79, 2016 Nov.
[Is] ISSN:1879-2472
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Thrombomodulin (TM) alfa, a recombinant human soluble TM, enhances activation of pro-carboxypeptidase B2 (pro-CPB2) by thrombin. Activated pro-CPB2 (CPB2) exerts anti-inflammatory and anti-fibrinolytic activities. Therefore, TM alfa may also have anti-inflammatory and anti-fibrinolytic effects through CPB2. However, these effects of TM alfa have not been elucidated. In the present study, we investigated the effects of TM alfa on inactivation of complement component C5a as an anti-inflammatory effect and prolongation of clot lysis time as an anti-fibrinolytic effect via CPB2 in vitro. METHODS: CPB2 activity and tissue factor-induced thrombin generation was examined by a chromogenic assay. C5a inactivation was evaluated by C-terminal cleavage of C5a and inhibition of C5a-induced human neutrophil migration. Clot lysis time prolongation was examined by a tissue-type plasminogen activator-induced clot lysis assay. RESULTS: CPB2 activity in human plasma was increased by TM alfa and thrombin in a concentration-dependent manner. TM alfa inhibited tissue factor-induced thrombin generation and enhanced pro-CPB2 activation in human plasma simultaneously. The mass spectrum of C5a treated with TM alfa, thrombin, and pro-CPB2 was decreased at 156m/z, indicating that TM alfa enhanced the processing of C5a to C-terminal-cleaved C5a, an inactive form of C5a. C5a-induced human neutrophil migration was decreased after C5a treatment with TM alfa, thrombin, and pro-CPB2. TM alfa prolonged the clot lysis time in human plasma, and this effect was completely abolished by addition of a CPB2 inhibitor. CONCLUSIONS: TM alfa exerts anti-inflammatory and anti-fibrinolytic effects through CPB2 in the presence of thrombin in vitro.
[Mh] Termos MeSH primário: Anti-Inflamatórios/farmacologia
Carboxipeptidase B2/imunologia
Fibrinolíticos/farmacologia
Trombina/antagonistas & inibidores
[Mh] Termos MeSH secundário: Ensaios de Migração de Leucócitos
Inibição de Migração Celular/efeitos dos fármacos
Complemento C5a/imunologia
Ativação Enzimática/efeitos dos fármacos
Tempo de Lise do Coágulo de Fibrina
Seres Humanos
Neutrófilos/efeitos dos fármacos
Neutrófilos/imunologia
Proteínas Recombinantes/farmacologia
Trombina/imunologia
Trombomodulina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ART123); 0 (Anti-Inflammatory Agents); 0 (Fibrinolytic Agents); 0 (Recombinant Proteins); 0 (Thrombomodulin); 80295-54-1 (Complement C5a); EC 3.4.17.20 (Carboxypeptidase B2); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


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[PMID]:27472894
[Au] Autor:Li M; Su Y; Yu Y; Yu Y; Wang X; Zou Y; Ge J; Chen R
[Ad] Endereço:Department of Cardiovascular Diseases, Key Laboratory of Viral Heart Diseases, Ministry of Public Health, Shanghai Institute of Cardiovascular Diseases, Zhongshan Hospital, Fudan University, Shanghai 200032, China.
[Ti] Título:Dual roles of calpain in facilitating Coxsackievirus B3 replication and prompting inflammation in acute myocarditis.
[So] Source:Int J Cardiol;221:1123-31, 2016 Oct 15.
[Is] ISSN:1874-1754
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Viral myocarditis (VMC) treatment has long been lacking of effective methods. Our former studies indicated roles of calpain in VMC pathogenesis. This study aimed at verifying the potential of calpain in Coxsackievirus B3 (CVB3)-induced myocarditis treatment. METHODS: A transgenic mouse overexpressing the endogenous calpain inhibitor, calpastatin, was introduced in the study. VMC mouse model was established via intraperitoneal injection of CVB3 in transgenic and wild mouse respectively. Myocardial injury was assayed histologically (HE staining and pathology grading) and serologically (myocardial damage markers of CK-MB and cTnI). CVB3 replication was observed in vivo and in vitro via the capsid protein VP1 detection or virus titration. Inflammation/fibrotic factors of MPO, perforin, IFNγ, IL17, Smad3 and MMP2 were evaluated using western blot or immunohistology stain. Role of calpain in regulating fibroblast migration was studied in scratch assays. RESULTS: Calpastatin overexpression ameliorated myocardial injury induced by CVB3 infection significantly in transgenic mouse indicated by reduced peripheral CK-MB and cTnI levels and improved histology injury. Comparing with CVB3-infected wild type mouse, the transgenic mouse heart tissue carried lower virus load. The inflammation factors of MPO, perforin, IFNγ and IL17 were down-regulated accompanied with fibrotic agents of Smad3 and MMP2 inhibition. And calpain participated in the migration of fibroblasts in vitro, which further proves its role in regulating fibrosis. CONCLUSION: Calpain plays dual roles of facilitating CVB3 replication and inflammation promotion. Calpain inhibition in CVB3-induced myocarditis showed significant treatment effect. Calpain might be a novel target for VMC treatment in clinical practices.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cálcio/metabolismo
Calpaína
Inibição de Migração Celular/fisiologia
Infecções por Coxsackievirus
Fibroblastos/fisiologia
Miocardite
[Mh] Termos MeSH secundário: Animais
Calpaína/antagonistas & inibidores
Calpaína/metabolismo
Infecções por Coxsackievirus/metabolismo
Infecções por Coxsackievirus/patologia
Modelos Animais de Doenças
Enterovirus Humano B/fisiologia
Fibrose/metabolismo
Fibrose/patologia
Inflamação/metabolismo
Inflamação/patologia
Camundongos
Miocardite/metabolismo
Miocardite/patologia
Miocardite/virologia
Replicação Viral/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 79079-11-1 (calpastatin); EC 3.4.22.- (Calpain)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160730
[St] Status:MEDLINE


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[PMID]:26969756
[Au] Autor:Schmid M; Gemperle C; Rimann N; Hersberger M
[Ad] Endereço:Division of Clinical Chemistry and Biochemistry, University Children's Hospital Zurich, CH-8032 Zurich, Switzerland; Children's Research Center, University Children's Hospital Zurich, CH-8032 Zurich, Switzerland; and Center for Integrative Human Physiology, University of Zurich, CH-8057 Zurich, Swit
[Ti] Título:Resolvin D1 Polarizes Primary Human Macrophages toward a Proresolution Phenotype through GPR32.
[So] Source:J Immunol;196(8):3429-37, 2016 Apr 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Resolvin D1 (RvD1) was shown to be a potent anti-inflammatory and proresolution lipid mediator in several animal models of inflammation, but its mechanism of action in humans is not clear. We show that the RvD1 receptor GPR32 is present on resting, proinflammatory M(LPS) and alternatively activated primary human M(IL-4) macrophages, whereas TGF-ß and IL-6 reduce its membrane expression. Accordingly, stimulation of resting primary human macrophages with 10 nM RvD1 for 48 h maximally reduced the secretion of the proinflammatory cytokines IL-1ß and IL-8; abolished chemotaxis to several chemoattractants like chemerin, fMLF, and MCP-1; and doubled the phagocytic activity of these macrophages toward microbial particles. In contrast, these functional changes were not accompanied by surface expression of markers specific for alternatively activated M(IL-4) macrophages. Similar proresolution effects of RvD1 were observed when proinflammatory M(LPS) macrophages were treated with RvD1. In addition, we show that these RvD1-mediated effects are GPR32 dependent because reduction of GPR32 expression by small interfering RNA, TGF-ß, and IL-6 treatment ablated these proresolution effects in primary human macrophages. Taken together, our results indicate that in humans RvD1 triggers GPR32 to polarize and repolarize macrophages toward a proresolution phenotype, supporting the role of this mediator in the resolution of inflammation in humans.
[Mh] Termos MeSH primário: Anti-Inflamatórios/farmacologia
Ácidos Docosa-Hexaenoicos/farmacologia
Inflamação/tratamento farmacológico
Macrófagos/imunologia
Receptores Acoplados a Proteínas-G/imunologia
[Mh] Termos MeSH secundário: Inibição de Migração Celular/efeitos dos fármacos
Células Cultivadas
Quimiotaxia/efeitos dos fármacos
Seres Humanos
Inflamação/imunologia
Interleucina-1beta/biossíntese
Interleucina-6/imunologia
Interleucina-8/biossíntese
Fagocitose/efeitos dos fármacos
Fagocitose/imunologia
Fenótipo
Interferência de RNA
RNA Interferente Pequeno/genética
Receptores Acoplados a Proteínas-G/biossíntese
Receptores Acoplados a Proteínas-G/genética
Fator de Crescimento Transformador beta/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (GPR32 protein, human); 0 (IL1B protein, human); 0 (IL8 protein, human); 0 (Interleukin-1beta); 0 (Interleukin-6); 0 (Interleukin-8); 0 (RNA, Small Interfering); 0 (Receptors, G-Protein-Coupled); 0 (Transforming Growth Factor beta); 0 (resolvin D1); 25167-62-8 (Docosahexaenoic Acids)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160405
[Lr] Data última revisão:
160405
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160313
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1501701


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[PMID]:26792186
[Au] Autor:Yang YT; Yang HY; Wang YF; Shen SY; Li MH; Qin JR
[Ad] Endereço:Department of Oral and Maxillofacial Surgery, Peking University Shenzhen Hospital, Shenzhen Guangdong 518036, China.
[Ti] Título:[The influence of urothelial carcinoembryonic antigen 1 on invasion and migration of oral carcinoma cell lines].
[So] Source:Zhonghua Kou Qiang Yi Xue Za Zhi;51(1):36-41, 2016 Jan.
[Is] ISSN:1002-0098
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To investigate the effects of long chain non-coding RNA urothelial carcinoembryonic antigen 1(UCA1) on invasion, migration and proliferation abilities in oral squamous cell carcinoma cell lines SCC15 and CAL27. METHODS: Small interfering RNA of UCA1(UCA1-siRNA) was transfected into SCC15 and CAL27 cell lines by Lipofectamine(TM) 3000 to silence UCA1 , and transfected negtive control si-RNA served as a control. The effect of UCA1-siRNA was detected by quantitative real time-polymerase chain reaction(qRT-PCR) to confirm the successful inhibition of UCA1 by siRNA. The matrix metalloproteinase 9(MMP-9) protein level was detected by Western blotting analysis. The effect of siRNA on cell proliferation and invasion was assessed by transwell migration assay and wound healing assay. Cell counting kit-8(CCK-8) assay was carried out to estimate the proliferation of two cell lines with different expression levels of UCA1. RESULTS: Expressions of UCA1 of SCC15 and CAL27 were successfully suppressed after transfected with siRNA which verified by qRT-PCR, and the efficiency of downregulation of SCC15 and CAL27 was 86.45%(P<0.001)and 78.24%(P<0.001), respectively. The migration, invasion and proliferation of SCC15 and CAL27 cell lines after transfected with siRNA were obviously restrained. The number of migration and invasion of CAL27 cells were 719.20±92.36 versus 208.00±25.58 (P=0.000 7) and 363.40 ± 45.96 versus 164.80 ± 24.68(P= 0.005 2), respectively, the number of migration and invasion of SCC15 cells were 437.20±54.75 vs 145.80±23.31(P=0.001 1) and 249.80±38.41 vs 63.80±11.11 (P=0.001 6), respectively (UCA1-si compare to negtive control), the relative proliferation rates of SCC15 and CAL27 were SCC15: R24 h=0.870, R48 h=0.863, R72 h=0.64, R96 h=0.732; CAL27: R24 h=0.913, R48 h=0.829, R72 h=0.756, R96 h= 0.705(P<0.05), and MMP-9 expression level was decreased by UCA1-siRNA compared with negative control. CONCLUSIONS: UCA1 could enhance the ability of invasion and migration of SCC15 and CAL27 cell lines via regulating MMP-9 protein expression, which suggests that UCA1 might play a pivotal role in oral squamous cell carcinoma invasion and progression.
[Mh] Termos MeSH primário: Antígeno Carcinoembrionário/fisiologia
Carcinoma de Células Escamosas/patologia
Movimento Celular
Proliferação Celular/fisiologia
Metaloproteinase 9 da Matriz/metabolismo
Neoplasias Bucais/patologia
Invasividade Neoplásica
RNA Interferente Pequeno
Transfecção
[Mh] Termos MeSH secundário: Antígeno Carcinoembrionário/genética
Carcinoma de Células Escamosas/enzimologia
Linhagem Celular Tumoral
Inibição de Migração Celular
Regulação para Baixo
Seres Humanos
Metaloproteinase 9 da Matriz/análise
Neoplasias Bucais/enzimologia
RNA Longo não Codificante
Migração Transcelular de Célula
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carcinoembryonic Antigen); 0 (RNA, Long Noncoding); 0 (RNA, Small Interfering); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:160122
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1002-0098.2016.01.009


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[PMID]:26314263
[Au] Autor:Shao J; Stout I; Volger OL; Hendriksen PJ; van Loveren H; Peijnenburg AA
[Ad] Endereço:RIKILT-Institute of Food Safety, Wageningen University and Research Centre, P.O. Box 230, 6700 AE, Wageningen, The Netherlands.
[Ti] Título:Inhibition of CXCL12-mediated chemotaxis of Jurkat cells by direct immunotoxicants.
[So] Source:Arch Toxicol;90(7):1685-94, 2016 Jul.
[Is] ISSN:1432-0738
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Directional migration of cells to specific locations is required in tissue development, wound healing, and immune responses. Immune cell migration plays a crucial role in both innate and adaptive immunity. Chemokines are small pro-inflammatory chemoattractants that control the migration of leukocytes. In addition, they are also involved in other immune processes such as lymphocyte development and immune pathology. In a previous toxicogenomics study using the Jurkat T cell line, we have shown that the model immunotoxicant TBTO inhibited chemotaxis toward the chemokine CXCL12. In the present work, we aimed at assessing a novel approach to detecting chemicals that affect the process of cell migration. For this, we first evaluated the effects of 31 chemicals on mRNA expression of genes that are known to be related to cell migration. With this analysis, seven immunotoxicants were identified as potential chemotaxis modulators, of which five (CoCl2 80 µM, MeHg 1 µM, ochratoxin A 10 µM, S9-treated ochratoxin A 10 µM, and TBTO 100 nM) were confirmed as chemotaxis inhibitor in an in vitro trans-well chemotaxis assay using the chemokine CXCL12. The transcriptome data of the five compounds together with previously obtained protein phosphorylation profiles for two out of five compounds (i.e., ochratoxin A and TBTO) revealed that the mechanisms behind the chemotaxis inhibition are different for these immunotoxicants. Moreover, the mTOR inhibitor rapamycin had no effect on the chemotaxis of Jurkat cells, indicating that the mTOR pathway is not involved in CXCL12-mediated chemotaxis of Jurkat cells, which is opposite to the findings on human primary T cells (Munk et al. in PLoS One 6(9):e24667, 2011). Thus, the results obtained from the chemotaxis assay conducted with Jurkat cells might not fully represent the results obtained with human primary T cells. Despite this difference, the present study indicated that some compounds may exert their immunotoxic effects through inhibition of CXCL12-mediated chemotaxis.
[Mh] Termos MeSH primário: Inibição de Migração Celular/efeitos dos fármacos
Quimiocina CXCL12/farmacologia
Quimiotaxia/efeitos dos fármacos
Imunossupressores/toxicidade
Linfócitos T/efeitos dos fármacos
Compostos de Trialquitina/toxicidade
[Mh] Termos MeSH secundário: Inibição de Migração Celular/genética
Quimiocina CXCL12/imunologia
Quimiotaxia/genética
Seres Humanos
Células Jurkat
RNA Mensageiro/genética
Linfócitos T/imunologia
Transcriptoma/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokine CXCL12); 0 (Immunosuppressive Agents); 0 (RNA, Messenger); 0 (Trialkyltin Compounds); 3353Q84MKM (bis(tri-n-butyltin)oxide)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150829
[St] Status:MEDLINE
[do] DOI:10.1007/s00204-015-1585-7


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[PMID]:26529233
[Au] Autor:Bagheri F; Safarian S; Eslaminejad MB; Sheibani N
[Ad] Endereço:a Department of Cell and Molecular Biology, School of Biology, College of Science, University of Tehran, Tehran, Iran.
[Ti] Título:Sensitization of breast cancer cells to doxorubicin via stable cell line generation and overexpression of DFF40.
[So] Source:Biochem Cell Biol;93(6):604-10, 2015 Dec.
[Is] ISSN:1208-6002
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:There are a number of reports demonstrating a relationship between the alterations in DFF40 expression and development of some cancers. Here, increased DFF40 expression in T-47D cells in the presence of doxorubicin was envisaged for therapeutic usage. The T-47D cells were transfected with an eukaryotic expression vector encoding the DFF40 cDNA. Following incubation with doxorubicin, propidium iodide (PI) staining was used for cell cycle distribution analysis. The rates of apoptosis were determined by annexin V/PI staining. Apoptosis was also evaluated using the DNA laddering analysis. The viability of DFF40-transfected cells incubated with doxorubicin was significantly decreased compared with control cells. However, there were no substantial changes in the cell cycle distribution of pIRES2-DFF40 cells incubated with doxorubicin compared to control cells. The expression of DFF40, without doxorubicin incubation, had also no significant effect on the cell cycle distribution. There was no DNA laddering in cells transfected with the empty pIRES2 vector when incubated with doxorubicin. In contrast, DNA laddering was observed in DFF40 transfected cells in the presence of doxorubicin after 48 h. Also, the expression of DFF40 and DFF45 was increased in DFF40 transfected cells in the presence of doxorubicin enhancing cell death. Collectively our results indicated that co-treatment of DFF40-transfected cells with doxorubicin can enhance the killing of these tumor cells via apoptosis. Thus, modulation of DFF40 level may be a beneficial strategy for treatment of chemo-resistant cancers.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Neoplasias da Mama/tratamento farmacológico
Desoxirribonucleases/metabolismo
Doxorrubicina/farmacologia
Resistência a Medicamentos Antineoplásicos
Proteínas de Neoplasias/metabolismo
Inibidores da Topoisomerase II/farmacologia
[Mh] Termos MeSH secundário: Antibióticos Antineoplásicos/farmacologia
Proteínas Reguladoras de Apoptose/genética
Proteínas Reguladoras de Apoptose/metabolismo
Neoplasias da Mama/metabolismo
Neoplasias da Mama/patologia
Caspase 3/genética
Caspase 3/metabolismo
Ciclo Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Inibição de Migração Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Desoxirribonucleases/genética
Feminino
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Seres Humanos
Proteínas de Neoplasias/genética
Proteínas de Ligação a Poli-ADP-Ribose
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibiotics, Antineoplastic); 0 (Apoptosis Regulatory Proteins); 0 (Neoplasm Proteins); 0 (Poly-ADP-Ribose Binding Proteins); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Topoisomerase II Inhibitors); 0 (caspase-activated DNase inhibitor); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); 80168379AG (Doxorubicin); EC 3.1.- (DFFB protein, human); EC 3.1.- (Deoxyribonucleases); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151104
[St] Status:MEDLINE
[do] DOI:10.1139/bcb-2015-0007


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[PMID]:26473885
[Au] Autor:Mori S; Williams H; Cagle D; Karanovich K; Horgen FD; Smith R; Watanabe CM
[Ad] Endereço:Department of Chemistry, Texas A&M University, College Station, TX 77843, USA. smori@mail.chem.tamu.edu.
[Ti] Título:Macrolactone Nuiapolide, Isolated from a Hawaiian Marine Cyanobacterium, Exhibits Anti-Chemotactic Activity.
[So] Source:Mar Drugs;13(10):6274-90, 2015 10 09.
[Is] ISSN:1660-3397
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:A new bioactive macrolactone, nuiapolide (1) was identified from a marine cyanobacterium collected off the coast of Niihau, near Lehua Rock. The natural product exhibits anti-chemotactic activity at concentrations as low as 1.3 µM against Jurkat cells, cancerous T lymphocytes, and induces a G2/M phase cell cycle shift. Structural characterization of the natural product revealed the compound to be a 40-membered macrolactone with nine hydroxyl functional groups and a rare tert-butyl carbinol residue.
[Mh] Termos MeSH primário: Quimiotaxia/efeitos dos fármacos
Cianobactérias/química
Macrolídeos/farmacologia
[Mh] Termos MeSH secundário: Divisão Celular/efeitos dos fármacos
Inibição de Migração Celular/efeitos dos fármacos
Fase G2/efeitos dos fármacos
Hawaii
Seres Humanos
Células Jurkat
Leucemia de Células T/tratamento farmacológico
Macrolídeos/química
Macrolídeos/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Macrolides); 0 (nuiapolide)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170301
[Lr] Data última revisão:
170301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151017
[St] Status:MEDLINE
[do] DOI:10.3390/md13106274


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Teixeira, Mauro Martins
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[PMID]:26183778
[Au] Autor:Vanheule V; Janssens R; Boff D; Kitic N; Berghmans N; Ronsse I; Kungl AJ; Amaral FA; Teixeira MM; Van Damme J; Proost P; Mortier A
[Ad] Endereço:From the Laboratory of Molecular Immunology, Department of Microbiology and Immunology, Rega Institute, KU Leuven, 3000 Leuven, Belgium.
[Ti] Título:The Positively Charged COOH-terminal Glycosaminoglycan-binding CXCL9(74-103) Peptide Inhibits CXCL8-induced Neutrophil Extravasation and Monosodium Urate Crystal-induced Gout in Mice.
[So] Source:J Biol Chem;290(35):21292-304, 2015 Aug 28.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ELR(-)CXC chemokine CXCL9 is characterized by a long, highly positively charged COOH-terminal region, absent in most other chemokines. Several natural leukocyte- and fibroblast-derived COOH-terminally truncated CXCL9 forms missing up to 30 amino acids were identified. To investigate the role of the COOH-terminal region of CXCL9, several COOH-terminal peptides were chemically synthesized. These peptides display high affinity for glycosaminoglycans (GAGs) and compete with functional intact chemokines for GAG binding, the longest peptide (CXCL9(74-103)) being the most potent. The COOH-terminal peptide CXCL9(74-103) does not signal through or act as an antagonist for CXCR3, the G protein-coupled CXCL9 receptor, and does not influence neutrophil chemotactic activity of CXCL8 in vitro. Based on the GAG binding data, an anti-inflammatory role for CXCL9(74-103) was further evidenced in vivo. Simultaneous intravenous injection of CXCL9(74-103) with CXCL8 injection in the joint diminished CXCL8-induced neutrophil extravasation. Analogously, monosodium urate crystal-induced neutrophil migration to the tibiofemural articulation, a murine model of gout, is highly reduced by intravenous injection of CXCL9(74-103). These data show that chemokine-derived peptides with high affinity for GAGs may be used as anti-inflammatory peptides; by competing with active chemokines for binding and immobilization on GAGs, these peptides may lower chemokine presentation on the endothelium and disrupt the generation of a chemokine gradient, thereby preventing a chemokine from properly performing its chemotactic function. The CXCL9 peptide may serve as a lead molecule for further development of inhibitors of inflammation based on interference with chemokine-GAG interactions.
[Mh] Termos MeSH primário: Anti-Inflamatórios/uso terapêutico
Quimiocina CXCL9/uso terapêutico
Gota/tratamento farmacológico
Interleucina-8/antagonistas & inibidores
Neutrófilos/efeitos dos fármacos
Peptídeos/uso terapêutico
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anti-Inflamatórios/química
Inibição de Migração Celular/efeitos dos fármacos
Quimiocina CXCL9/química
Quimiotaxia de Leucócito/efeitos dos fármacos
Glicosaminoglicanos/imunologia
Gota/induzido quimicamente
Gota/imunologia
Seres Humanos
Interleucina-8/imunologia
Camundongos
Camundongos Endogâmicos C57BL
Dados de Sequência Molecular
Neutrófilos/citologia
Neutrófilos/imunologia
Peptídeos/química
Ácido Úrico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Chemokine CXCL9); 0 (Glycosaminoglycans); 0 (Interleukin-8); 0 (Peptides); 268B43MJ25 (Uric Acid)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:160828
[Lr] Data última revisão:
160828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150718
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.649855


  9 / 5448 MEDLINE  
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[PMID]:25665143
[Au] Autor:Sator P; Richter L; Saxinger W; Vasiljevic M; Stingl G
[Ad] Endereço:Department of Dermatology, Hospital Hietzing with Neurologic Centre Rosenhügel, Vienna, Austria.
[Ti] Título:Adalimumab in the treatment of moderate-to-severe chronic plaque psoriasis in patients switching from other biologics.
[So] Source:J Eur Acad Dermatol Venereol;29(9):1742-9, 2015 Sep.
[Is] ISSN:1468-3083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Ample evidence shows that switching from one biological agent to another may prove effective when response to the first one is inadequate. Nevertheless, there are little data so far showing the efficacy and safety of adalimumab in patients with plaque psoriasis who previously received another biologic agent. OBJECTIVE: We evaluated the 1-year effectiveness, safety and quality-of-life outcomes patients with psoriasis who had switched to adalimumab from other biologic therapies. METHODS: Forty-two patients who participated in this Austrian multicenter study were treated with adalimumab over a 1-year period, after switching from efalizumab, infliximab or etanercept. Effectiveness was assessed using standardized tools for measurement of disease severity [Psoriasis Area and Severity Index (PASI) and Nail Psoriasis Severity Index (NAPSI)] and quality of life [Dermatology Life Quality Index (DLQI)]. The study endpoints were evaluated using the all-treated population. RESULTS: The mean percentage of improvement at the end of the study was 74.3% for PASI, 81.6% for DLQI and 83.6% for NAPSI, demonstrating a considerable benefit of treatment with adalimumab. The safety profile observed was consistent with previous clinical trials for adalimumab, and no new safety signals were observed. CONCLUSION: Adalimumab therapy in patients with plaque psoriasis previously treated with other biologic agents demonstrates effectiveness, safety and improvement in quality of life.
[Mh] Termos MeSH primário: Adalimumab/uso terapêutico
Produtos Biológicos/uso terapêutico
Psoríase/tratamento farmacológico
[Mh] Termos MeSH secundário: Anti-Inflamatórios/uso terapêutico
Anticorpos Monoclonais/uso terapêutico
Inibição de Migração Celular
Fármacos Dermatológicos/uso terapêutico
Etanercepte/uso terapêutico
Seguimentos
Seres Humanos
Imunossupressores/uso terapêutico
Infliximab/uso terapêutico
Estudos Prospectivos
Psoríase/diagnóstico
Qualidade de Vida
Índice de Gravidade de Doença
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY; RANDOMIZED CONTROLLED TRIAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Antibodies, Monoclonal); 0 (Biological Products); 0 (Dermatologic Agents); 0 (Immunosuppressive Agents); B72HH48FLU (Infliximab); FYS6T7F842 (Adalimumab); OP401G7OJC (Etanercept); XX2MN88N5D (efalizumab)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150210
[St] Status:MEDLINE
[do] DOI:10.1111/jdv.12981


  10 / 5448 MEDLINE  
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[PMID]:25660287
[Au] Autor:Li D; Song XY; Yue QX; Cui YJ; Liu M; Feng LX; Wu WY; Jiang BH; Yang M; Qu XB; Liu X; Guo DA
[Ad] Endereço:Changchun University of Chinese Medicine, Changchun 130117, China; Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
[Ti] Título:Proteomic and bioinformatic analyses of possible target-related proteins of gambogic acid in human breast carcinoma MDA-MB-231 cells.
[So] Source:Chin J Nat Med;13(1):41-51, 2015 Jan.
[Is] ISSN:1875-5364
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Gambogic acid (GA) is an anticancer agent in phase ‖b clinical trial in China but its mechanism of action has not been fully clarified. The present study was designed to search the possible target-related proteins of GA in cancer cells using proteomic method and establish possible network using bioinformatic analysis. Cytotoxicity and anti-migration effects of GA in MDA-MB-231 cells were checked using MTT assay, flow cytometry, wound migration assay, and chamber migration assay. Possible target-related proteins of GA at early (3 h) and late stage (24 h) of treatment were searched using a proteomic technology, two-dimensional electrophoresis (2-DE). The possible network of GA was established using bioinformatic analysis. The intracellular expression levels of vimentin, keratin 18, and calumenin were determined using Western blotting. GA inhibited cell proliferation and induced cell cycle arrest at G2/M phase and apoptosis in MDA-MB-231 cells. Additionally, GA exhibited anti-migration effects at non-toxic doses. In 2-DE analysis, totally 23 possible GA targeted proteins were found, including those with functions in cytoskeleton and transport, regulation of redox state, metabolism, ubiquitin-proteasome system, transcription and translation, protein transport and modification, and cytokine. Network analysis of these proteins suggested that cytoskeleton-related proteins might play important roles in the effects of GA. Results of Western blotting confirmed the cleavage of vimentin, increase in keratin 18, and decrease in calumenin levels in GA-treated cells. In summary, GA is a multi-target compound and its anti-cancer effects may be based on several target-related proteins such as cytoskeleton-related proteins.
[Mh] Termos MeSH primário: Antineoplásicos/farmacocinética
Neoplasias da Mama/tratamento farmacológico
Biologia Computacional/métodos
Proteômica/métodos
Xantonas/farmacocinética
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Neoplasias da Mama/metabolismo
Proteínas de Ligação ao Cálcio/genética
Linhagem Celular Tumoral
Ensaios de Migração Celular
Inibição de Migração Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Citoesqueleto/metabolismo
Eletroforese em Gel Bidimensional
Citometria de Fluxo
Expressão Gênica
Seres Humanos
Queratina-18/genética
Oxirredução
Biossíntese de Proteínas/efeitos dos fármacos
Transporte Proteico
Transcrição Genética/efeitos dos fármacos
Proteases Específicas de Ubiquitina/farmacocinética
Vimentina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (CALU protein, human); 0 (Calcium-Binding Proteins); 0 (KRT18 protein, human); 0 (Keratin-18); 0 (Vimentin); 0 (Xanthones); 8N585K83U2 (gambogic acid); EC 3.4.19.12 (Ubiquitin-Specific Proteases)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150210
[St] Status:MEDLINE



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