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Pesquisa : D08.811.277.656.300.480.525.700 [Categoria DeCS]
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[PMID]:29300772
[Au] Autor:Yang F; Yu N; Wang H; Zhang C; Zhang Z; Li Y; Li D; Yan L; Liu H; Xu Z
[Ad] Endereço:Department of Urology, Qilu Hospital of Shandong University, Jinan, P.R. China.
[Ti] Título:Downregulated expression of hepatoma-derived growth factor inhibits migration and invasion of prostate cancer cells by suppressing epithelial-mesenchymal transition and MMP2, MMP9.
[So] Source:PLoS One;13(1):e0190725, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatoma-derived growth factor (HDGF) is commonly over-expressed and plays critical roles in the development and progression in a variety of cancers. It has previously been shown that HDGF is overregulated in prostate cancer cells compared to normal prostate cells, which is correlated with cellular migration and invasion of prostate cancer. Here, the molecular mechanisms of HDGF in prostate cancer is investigated. It is shown that HDGF knockdown reduces prostate cancer cellular migration and invasion in both androgen-sensitive LNCaP cells and androgen-insensitive DU145 and PC3 cells. Furthermore, Western blot analysis reveals that HDGF knockdown inhibits epithelial-mesenchymal transition (EMT) of prostate cancer cells by upregulation of protein E-cadherin and downregulation of proteins N-cadherin, Vimentin, Snail and Slug. In addition, mechanistic studies reveal that proteins MMP2 and MMP9 are down-regulated. In conclusion, our data suggested that HDGF knockdown inhibits cellular migration and invasion in vitro of prostate cancer via modulating epithelial-mesenchymal transition (EMT) signaling pathway, as well as MMP2 and MMP9 signaling pathway. These results supported that HDGF is a relevant protein in the progression of prostate cancer and may serve as a potentially therapeutic target for prostate cancer as well as its downstream targets.
[Mh] Termos MeSH primário: Movimento Celular/fisiologia
Transição Epitelial-Mesenquimal/fisiologia
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Metaloproteinases da Matriz Secretadas/metabolismo
Invasividade Neoplásica/fisiopatologia
Neoplasias da Próstata/metabolismo
[Mh] Termos MeSH secundário: Antígenos CD/metabolismo
Western Blotting
Caderinas/metabolismo
Linhagem Celular Tumoral
Regulação para Baixo
Técnicas de Silenciamento de Genes
Vetores Genéticos
Seres Humanos
Peptídeos e Proteínas de Sinalização Intercelular/genética
Lentivirus/genética
Masculino
RNA Mensageiro/metabolismo
RNA Interferente Pequeno
Reação em Cadeia da Polimerase em Tempo Real
Vimentina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (CDH1 protein, human); 0 (CDH2 protein, human); 0 (Cadherins); 0 (Intercellular Signaling Peptides and Proteins); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (Vimentin); 0 (hepatoma-derived growth factor); EC 3.4.24.- (Matrix Metalloproteinases, Secreted)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190725


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[PMID]:28295306
[Au] Autor:Arosarena OA; Barr EW; Thorpe R; Yankey H; Tarr JT; Safadi FF
[Ad] Endereço:Department of Otolaryngology-Head and Neck Surgery, Lewis Katz School of Medicine, Temple University, Philadelphia, Pennsylvania.
[Ti] Título:Osteoactivin regulates head and neck squamous cell carcinoma invasion by modulating matrix metalloproteases.
[So] Source:J Cell Physiol;233(1):409-421, 2018 Jan.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nearly 60% of patients with head and neck squamous cell carcinoma (HNSCC) die of metastases or locoregional recurrence. Metastasis is mediated by cancer cell migration and invasion, which are in part dependent on extracellular matrix degradation by matrix metalloproteinases. Osteoactivin (OA) overexpression plays a role in metastases in several malignancies, and has been shown to upregulate matrix metalloproteinase (MMP) expression and activity. To determine how OA modulates MMP expression and activity in HNSCC, and to investigate OA effects on cell invasion, we assessed effects of OA treatment on MMP mRNA and protein expression, as well as gelatinase and caseinolytic activity in HNSCC cell lines. We assessed the effects of OA gene silencing on MMP expression, gelatinase and caseinolytic activity, and cell invasion. OA treatment had differential effects on MMP mRNA expression. OA treatment upregulated MMP-10 expression in UMSCC14a (p = 0.0431) and SCC15 (p < 0.0001) cells, but decreased MMP-9 expression in UMSCC14a cells (p = 0.0002). OA gene silencing decreased MMP-10 expression in UMSCC12 cells (p = 0.0001), and MMP-3 (p = 0.0005) and -9 (p = 0.0036) expression in SCC25 cells. In SCC15 and SCC25 cells, OA treatment increased MMP-2 (p = 0.0408) and MMP-9 gelatinase activity (p < 0.0001), respectively. OA depletion decreased MMP-2 (p = 0.0023) and -9 (p < 0.0001) activity in SCC25 cells. OA treatment increased 70 kDa caseinolytic activity in UMSCC12 cells consistent with tissue type plasminogen activator (p = 0.0078). OA depletion decreased invasive capacity of UMSCC12 cells (p < 0.0001). OA's effects on MMP expression in HNSCC are variable, and may promote cancer cell invasion.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/enzimologia
Movimento Celular
Neoplasias de Cabeça e Pescoço/enzimologia
Metaloproteinases da Matriz Secretadas/metabolismo
Glicoproteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Carcinoma de Células Escamosas/genética
Carcinoma de Células Escamosas/patologia
Linhagem Celular Tumoral
Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Neoplasias de Cabeça e Pescoço/genética
Neoplasias de Cabeça e Pescoço/patologia
Seres Humanos
Metaloproteinases da Matriz Secretadas/genética
Glicoproteínas de Membrana/genética
Invasividade Neoplásica
Interferência de RNA
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Transdução de Sinais
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GPNMB protein, human); 0 (Membrane Glycoproteins); 0 (RNA, Messenger); EC 3.4.24.- (Matrix Metalloproteinases, Secreted)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25900


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[PMID]:28572156
[Au] Autor:Steury MD; Lucas PC; McCabe LR; Parameswaran N
[Ad] Endereço:Department of Physiology, Michigan State University, East Lansing, MI 48824, U.S.A.
[Ti] Título:G-protein-coupled receptor kinase-2 is a critical regulator of TNFα signaling in colon epithelial cells.
[So] Source:Biochem J;474(14):2301-2313, 2017 Jun 27.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:G-protein-coupled receptor kinase-2 (GRK2) belongs to the GRK family of serine/threonine protein kinases critical in the regulation of G-protein-coupled receptors. Apart from this canonical role, GRK2 is also involved in several signaling pathways via distinct intracellular interactomes. In the present study, we examined the role of GRK2 in TNFα signaling in colon epithelial cell-biological processes including wound healing, proliferation, apoptosis, and gene expression. Knockdown of GRK2 in the SW480 human colonic cells significantly enhanced TNFα-induced epithelial cell wound healing without any effect on apoptosis/proliferation. Consistent with wound-healing effects, GRK2 knockdown augmented TNFα-induced matrix metalloproteinases (MMPs) 7 and 9, as well as urokinase plasminogen activator (uPA; factors involved in cell migration and wound healing). To assess the mechanism by which GRK2 affects these physiological processes, we examined the role of GRK2 in TNFα-induced MAPK and NF-κB pathways. Our results demonstrate that while GRK2 knockdown inhibited TNFα-induced IκBα phosphorylation, activation of ERK was significantly enhanced in GRK2 knockdown cells. Our results further demonstrate that GRK2 inhibits TNFα-induced ERK activation by inhibiting generation of reactive oxygen species (ROS). Together, these data suggest that GRK2 plays a critical role in TNFα-induced wound healing by modulating MMP7 and 9 and uPA levels via the ROS-ERK pathway. Consistent with findings, GRK2 heterozygous mice exhibited enhanced intestinal wound healing. Together, our results identify a novel role for GRK2 in TNFα signaling in intestinal epithelial cells.
[Mh] Termos MeSH primário: Colo/metabolismo
Quinase 2 de Receptor Acoplado a Proteína G/metabolismo
Mucosa Intestinal/metabolismo
Sistema de Sinalização das MAP Quinases
Fator de Necrose Tumoral alfa/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Colo/citologia
Colo/imunologia
Quinase 2 de Receptor Acoplado a Proteína G/antagonistas & inibidores
Quinase 2 de Receptor Acoplado a Proteína G/genética
Regulação Enzimológica da Expressão Gênica
Heterozigoto
Seres Humanos
Mucosa Intestinal/citologia
Mucosa Intestinal/imunologia
Metaloproteinases da Matriz Secretadas/genética
Metaloproteinases da Matriz Secretadas/metabolismo
Camundongos
Camundongos Knockout
Espécies Reativas de Oxigênio/metabolismo
Proteínas Recombinantes/metabolismo
Organismos Livres de Patógenos Específicos
Fator de Necrose Tumoral alfa/genética
Cicatrização
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 0 (Recombinant Proteins); 0 (TNF protein, human); 0 (Tumor Necrosis Factor-alpha); EC 2.7.11.15 (ADRBK1 protein, human); EC 2.7.11.15 (Adrbk1 protein, mouse); EC 2.7.11.16 (G-Protein-Coupled Receptor Kinase 2); EC 3.4.24.- (Matrix Metalloproteinases, Secreted)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170093


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[PMID]:28399390
[Au] Autor:Manicone AM; Gharib SA; Gong KQ; Eddy WE; Long ME; Frevert CW; Altemeier WA; Parks WC; Houghton AM
[Ad] Endereço:Department of Medicine, Center for Lung Biology, University of Washington, Seattle, Washington. Electronic address: manicone@uw.edu.
[Ti] Título:Matrix Metalloproteinase-28 Is a Key Contributor to Emphysema Pathogenesis.
[So] Source:Am J Pathol;187(6):1288-1300, 2017 Jun.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chronic obstructive pulmonary disease (COPD) comprises chronic bronchitis and emphysema, and is a leading cause of morbidity and mortality. Because tissue destruction is the prominent characteristic of emphysema, extracellular proteinases, particularly those with elastolytic ability, are often considered to be key drivers in this disease. Several human and mouse studies have implicated roles for matrix metalloproteinases (MMPs), particularly macrophage-derived proteinases, in COPD pathogenesis. MMP-28 is expressed by the pulmonary epithelium and macrophage, and we have found that it regulates macrophage recruitment and polarization. We hypothesized that MMP-28 has contributory roles in emphysema via alteration of macrophage numbers and activation. Because of the established association of emphysema pathogenesis to macrophage influx, we evaluated the inflammatory changes and lung histology of Mmp28 mice exposed to 3 and 6 months of cigarette smoke. At earlier time points, we found altered macrophage polarization in the smoke-exposed Mmp28 lung consistent with other published findings that MMP-28 regulates macrophage activation. At both 3 and 6 months, Mmp28 mice had blunted inflammatory responses more closely resembling nonsmoked mice, with a reduction in neutrophil recruitment and CXCL1 chemokine expression. By 6 months, Mmp28 mice were protected from emphysema. These results highlight a previously unrecognized role for MMP-28 in promoting chronic lung inflammation and tissue remodeling induced by cigarette smoke and highlight another potential target to modulate COPD.
[Mh] Termos MeSH primário: Metaloproteinases da Matriz Secretadas/fisiologia
Enfisema Pulmonar/enzimologia
[Mh] Termos MeSH secundário: Animais
Líquido da Lavagem Broncoalveolar/citologia
Quimiocinas/metabolismo
Modelos Animais de Doenças
Feminino
Perfilação da Expressão Gênica/métodos
Regulação Enzimológica da Expressão Gênica/fisiologia
Pulmão/enzimologia
Macrófagos Alveolares/enzimologia
Masculino
Metaloproteinases da Matriz Secretadas/deficiência
Metaloproteinases da Matriz Secretadas/genética
Camundongos Endogâmicos C57BL
Camundongos Knockout
Infiltração de Neutrófilos/fisiologia
Pneumonia/enzimologia
Pneumonia/etiologia
Pneumonia/genética
Pneumonia/patologia
Doença Pulmonar Obstrutiva Crônica/enzimologia
Enfisema Pulmonar/etiologia
Enfisema Pulmonar/genética
Enfisema Pulmonar/patologia
Poluição por Fumaça de Tabaco/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokines); 0 (Tobacco Smoke Pollution); EC 3.4.24.- (Matrix Metalloproteinases, Secreted); EC 3.4.24.- (Mmp28 protein, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE


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[PMID]:28293015
[Au] Autor:Lorenc Z; Waniczek D; Lorenc-Podgórska K; Krawczyk W; Domagala M; Majewski M; Mazurek U
[Ad] Endereço:Chair and Clinical Department of General, Colorectal and Trauma Surgery, Medical University of Silesia, Sosnowiec, Poland.
[Ti] Título:Profile of Expression of Genes Encoding Matrix Metallopeptidase 9 (MMP9), Matrix Metallopeptidase 28 (MMP28) and TIMP Metallopeptidase Inhibitor 1 (TIMP1) in Colorectal Cancer: Assessment of the Role in Diagnosis and Prognostication.
[So] Source:Med Sci Monit;23:1305-1311, 2017 Mar 15.
[Is] ISSN:1643-3750
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND Studies on the pathomechanism of colorectal cancer (CRC) expansion indicate a significant role of metalloproteinases and their inhibitors in the extracellular matrix. The results of the analysis of a profile of transcriptional activity of genes encoding metalloproteinases were the basis of the hypothesis indicating changes in the expression of genes encoding MMP9, MMP28, and TIMP1 as an additional diagnostic and prognostic marker of CRC. MATERIAL AND METHODS The material consisted of samples obtained from resected tumors and healthy tissue samples from 15 CRC patients (aged 46-72 years) at clinical stages (CSs) I and II-IV. Gene expression analysis was done using microarrays. Microarray data analysis was done using the GeneSpring 11.5 platform. The results were validated using the qRT-PCR technique. RESULTS We found high levels of expression of MMP9 at each CS, as well as in the tissues at the early stage of CRC. Additionally, we observed high levels of expression of TIMP1 and low levels of MMP28 genes in CS II-IV. No statistically significant differences based on the stage of CRC were observed. CONCLUSIONS MMP9 gene profile may be a complementary diagnostic marker in CRC. The results suggest a crucial role of MMP9 at the early stage of carcinogenesis in the large intestine. The increase in MMP9 and TIMP1 mRNA concentration and the decrease in MMP28 in the large intestinal tissue may be a confirmation of cancer, but it may not indicate the advance of CRC.
[Mh] Termos MeSH primário: Neoplasias Colorretais/genética
Metaloproteinase 9 da Matriz/genética
Metaloproteinases da Matriz Secretadas/genética
Inibidor Tecidual de Metaloproteinase-1/genética
[Mh] Termos MeSH secundário: Idoso
Biomarcadores Tumorais/biossíntese
Biomarcadores Tumorais/genética
Estudos de Casos e Controles
Neoplasias Colorretais/diagnóstico
Neoplasias Colorretais/enzimologia
Neoplasias Colorretais/metabolismo
Feminino
Seres Humanos
Masculino
Metaloproteinase 9 da Matriz/biossíntese
Metaloproteinases da Matriz Secretadas/biossíntese
Metaloproteinases da Matriz Secretadas/metabolismo
Meia-Idade
Prognóstico
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Inibidor Tecidual de Metaloproteinase-1/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (RNA, Messenger); 0 (TIMP1 protein, human); 0 (Tissue Inhibitor of Metalloproteinase-1); EC 3.4.24.- (MMP28 protein, human); EC 3.4.24.- (Matrix Metalloproteinases, Secreted); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[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:170316
[St] Status:MEDLINE


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[PMID]:28098862
[Au] Autor:Zhou G; Peng F; Zhong Y; Chen Y; Tang M; Li D
[Ad] Endereço:Affiliated Tumor Hospital of Guangxi Medical University, Nanning, Guangxi Zhuang Autonomous Region 530021, P.R. China.
[Ti] Título:Rhein suppresses matrix metalloproteinase production by regulating the Rac1/ROS/MAPK/AP-1 pathway in human ovarian carcinoma cells.
[So] Source:Int J Oncol;50(3):933-941, 2017 Mar.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Matrix metalloproteinases (MMPs) are a family of calcium-dependent zinc-containing endopeptidases, which play an integral role in migration and invasion of ovarian cancer. Rac1 proteins might mostly influence cell migration and invasion by generating endogenous reactive oxygen species. Therefore, inhibiting MMPs and regulating the Rac1/ROS/MAPK/AP-1 pathway may be a new therapeutic strategy for ovarian cancer. In this study, we found that rhein could suppress the invasion and migration of SKOV3-PM4 cells with characteristics of directional highly lymphatic metastasis. Phorbol 12-myristate 13-acetate (PMA), which is a Rac1 activator, significantly enhanced the expression levels of MMP-2, -3, -9 and -19 proteins, whereas the results of rhein and Rac1 inhibitor NSC23766 were just the opposite. The inhibitory effects of rhein were associated with the upregulation of tissue inhibitors of metalloproteinase (TIMP)-1, TIMP-2 and NM23-H1. Subsequent mechanism studies revealed that rhein reduce the production of reactive oxygen species (ROS) and lower NADPH oxidase activity. Furthermore, rhein significantly inhibited JNK, AP-1 phosphorylation in the cells treated with PMA. The results obtained from the cells treated with NSC23766 alone or NSC23766 combined with rhein, were consistent with rhein treatment alone. Taken together, these results indicate that rhein may be a potential inhibitor of Rac1 and can inhibit the migration and invasion of SKOV3-PM4 cells through modulating matrix metalloproteinases and RAC1/ROS/MAPK/AP-1 signaling pathway-associated proteins.
[Mh] Termos MeSH primário: Antraquinonas/farmacologia
Inibidores de Metaloproteinases de Matriz/farmacologia
Metaloproteinases da Matriz/metabolismo
Neoplasias Ovarianas/patologia
Espécies Reativas de Oxigênio/metabolismo
Fator de Transcrição AP-1/metabolismo
Proteínas rac1 de Ligação ao GTP/antagonistas & inibidores
[Mh] Termos MeSH secundário: Aminoquinolinas/farmacologia
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Feminino
Seres Humanos
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 3 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/metabolismo
Metaloproteinases da Matriz Secretadas/metabolismo
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Invasividade Neoplásica/patologia
Neoplasias Ovarianas/genética
Fosforilação/efeitos dos fármacos
Pirimidinas/farmacologia
Acetato de Tetradecanoilforbol/farmacologia
Inibidor Tecidual de Metaloproteinase-1/metabolismo
Inibidor Tecidual de Metaloproteinase-2/metabolismo
Proteínas rac1 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoquinolines); 0 (Anthraquinones); 0 (Matrix Metalloproteinase Inhibitors); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (NSC 23766); 0 (Pyrimidines); 0 (RAC1 protein, human); 0 (Reactive Oxygen Species); 0 (TIMP1 protein, human); 0 (TIMP2 protein, human); 0 (Tissue Inhibitor of Metalloproteinase-1); 0 (Transcription Factor AP-1); 127497-59-0 (Tissue Inhibitor of Metalloproteinase-2); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 2.7.4.6 (NME1 protein, human); EC 3.4.24.- (Matrix Metalloproteinases); EC 3.4.24.- (Matrix Metalloproteinases, Secreted); EC 3.4.24.- (matrix metalloproteinase 19); EC 3.4.24.17 (MMP3 protein, human); EC 3.4.24.17 (Matrix Metalloproteinase 3); EC 3.4.24.24 (MMP2 protein, human); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 3.6.5.2 (rac1 GTP-Binding Protein); NI40JAQ945 (Tetradecanoylphorbol Acetate); YM64C2P6UX (rhein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2017.3853


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[PMID]:27959447
[Au] Autor:Chen T; Gong W; Tian H; Wang H; Chu S; Ma J; Yang H; Cheng J; Liu M; Li X; Jiang C
[Ad] Endereço:School of Pharmaceutical Science, Wenzhou Medical University, Wenzhou, Zhejiang 325035, P.R. China.
[Ti] Título:Fibroblast growth factor 18 promotes proliferation and migration of H460 cells via the ERK and p38 signaling pathways.
[So] Source:Oncol Rep;37(2):1235-1242, 2017 Feb.
[Is] ISSN:1791-2431
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Recently, fibroblast growth factor 18 (FGF18) expression was reported to be upregulated in colon cancer and ovarian cancer, and increased expression of FGF18 mRNA and protein is associated with tumor progression and poor overall survival in patients; however, its role in lung cancer remains to be explored. In the present study, the effect and underlying molecular mechanisms of FGF18 on H460 cells were investigated. Cell proliferation and cell cycle alterations were detected using a 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide assay and flow cytometry. A wound healing assay was conducted to detect cell migration. Reverse transcription-quantitative polymerase chain reaction and western blotting were performed to measure extracellular signal-regulated kinase (ERK), p38 and matrix metalloproteinase 26 (MMP26) expression. Knockdown of FGF18 using short interfering RNA (siRNA-FGF18) suppressed H460 cell proliferation, inhibited cell migration via the downregulation of MMP26 levels, with siRNA-FGF18 additionally inhibiting the ERK and p38 signaling pathway. The present study indicates that FGF18 serves an essential role in the growth and migration of non-small cell lung cancer (NSCLC) cells by regulating the ERK, p38 signaling pathways and MMP26 protein levels, suggesting that FGF18 may be a potential molecular drug target for the treatment NSCLC.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/patologia
Fatores de Crescimento de Fibroblastos/metabolismo
Neoplasias Pulmonares/patologia
Sistema de Sinalização das MAP Quinases
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Mh] Termos MeSH secundário: Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Ciclo Celular
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Fatores de Crescimento de Fibroblastos/genética
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/metabolismo
Metaloproteinases da Matriz Secretadas/metabolismo
RNA Interferente Pequeno
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Interfering); 0 (fibroblast growth factor 18); 62031-54-3 (Fibroblast Growth Factors); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.4.24.- (MMP26 protein, human); EC 3.4.24.- (Matrix Metalloproteinases, Secreted)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170323
[Lr] Data última revisão:
170323
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161214
[St] Status:MEDLINE
[do] DOI:10.3892/or.2016.5301


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[PMID]:27511626
[Au] Autor:Tanaka T; Imamura T; Yoneda M; Irie A; Ogi H; Nagata M; Yoshida R; Fukuma D; Kawahara K; Shinohara M; Nakayama H
[Ad] Endereço:Department of Oral and Maxillofacial Surgery, Faculty of Life Sciences, Kumamoto University, Kumamoto 860-8556, Japan.
[Ti] Título:Enhancement of active MMP release and invasive activity of lymph node metastatic tongue cancer cells by elevated signaling via the TNF-α-TNFR1-NF-κB pathway and a possible involvement of angiopoietin-like 4 in lung metastasis.
[So] Source:Int J Oncol;49(4):1377-84, 2016 Oct.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:To study the role of TNF-α in tongue cancer metastasis, we made highly metastatic cells from a human oral squamous cell carcinoma cell line (SAS) by repeating the passage in which the cells were injected into a nude mouse tongue and harvested from metastasized cervical lymph nodes. Cancer cells after 5 passages (GSAS/N5) increased invasive activity 7-fold in a TNF-α receptor 1 (TNFR1)-dependent manner and enhanced mRNA expression of TNF-α and TNFR1. In the highly metastatic cells, NF-κB activation was upregulated via elevated phosphorylation of Akt and Ikkα/ß in the signaling pathway and secretion of TNF-α, active MMP-2 and MMP-9 increased. Suppression of increase of TNF-α mRNA expression and MMP secretion by NF-κB inhibitor NBD peptide suggested a positive feedback loop in GSAS/N5 cells; TNF-α activates NF-κB and activated NF-κB induces further TNF-α secretion, leading to increase of active MMP release and promotion of invasion and metastasis of the cells. GSAS/N5 cells that had been injected into the nude mouse tongue and harvested from metastasized lungs multiplied angiopoietin-like 4 (angptl4) expression with enhanced migration activity, which indicated a possible involvement of angptl4 in lung metastasis of the cells. These results suggest that TNF-α and angptl4 promote metastasis of the oral cancer cells, thus, these molecules may be therapeutic targets for patients with tongue cancer.
[Mh] Termos MeSH primário: Angiopoietinas/metabolismo
Carcinoma de Células Escamosas/metabolismo
Neoplasias Pulmonares/metabolismo
Metaloproteinases da Matriz Secretadas/secreção
Receptores Tipo I de Fatores de Necrose Tumoral/genética
Neoplasias da Língua/metabolismo
Fator de Necrose Tumoral alfa/genética
[Mh] Termos MeSH secundário: Proteínas Semelhantes a Angiopoietina
Animais
Carcinoma de Células Escamosas/genética
Carcinoma de Células Escamosas/patologia
Linhagem Celular Tumoral
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Metástase Linfática
Metaloproteinase 2 da Matriz/secreção
Metaloproteinase 9 da Matriz/secreção
Camundongos
Camundongos Nus
NF-kappa B/metabolismo
Invasividade Neoplásica
Transplante de Neoplasias
Transdução de Sinais
Neoplasias da Língua/genética
Neoplasias da Língua/patologia
Fator de Necrose Tumoral alfa/secreção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ANGPTL1 protein, human); 0 (Angiopoietin-like Proteins); 0 (Angiopoietins); 0 (NF-kappa B); 0 (Receptors, Tumor Necrosis Factor, Type I); 0 (TNF protein, human); 0 (TNFRSF1A protein, human); 0 (Tumor Necrosis Factor-alpha); EC 3.4.24.- (Matrix Metalloproteinases, Secreted); EC 3.4.24.24 (MMP2 protein, human); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160812
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2016.3653


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[PMID]:27471391
[Au] Autor:Jaoude J; Koh Y
[Ad] Endereço:Department of Biology.
[Ti] Título:Matrix metalloproteinases in exercise and obesity.
[So] Source:Vasc Health Risk Manag;12:287-95, 2016.
[Is] ISSN:1178-2048
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:Matrix metalloproteinases (MMPs) are zinc- and calcium-dependent endoproteinases that have the ability to break down extracellular matrix. The large range of MMPs' functions widens their spectrum of potential role as activators or inhibitors in tissue remodeling, cardiovascular diseases, and obesity. In particular, MMP-1, -2, and -9 may be associated with exercise and obesity. Thus, the current study reviewed the effects of different types of exercise (resistance and aerobic) on MMP-1, -2, and -9. Previous studies report that the response of MMP-2 and -9 to resistance exercise is dependent upon the length of exercise training, since long-term resistance exercise training increased both MMP-2 and -9, whereas acute bout of resistance exercise decreased these MMPs. Aerobic exercise produces an inconsistent result on MMPs, although some studies showed a decrease in MMP-1. Obesity is related to a relatively lower level of MMP-9, indicating that an exercise-induced increase in MMP-9 may positively influence obesity. A comprehensive understanding of the relationship between exercise, obesity, and MMPs does not exist yet. Future studies examining the acute and chronic responses of these MMPs using different subject models may provide a better understanding of the molecular mechanisms that are associated with exercise, obesity, and cardiovascular disease.
[Mh] Termos MeSH primário: Colagenases/metabolismo
Exercício/fisiologia
Metaloproteinases da Matriz Secretadas/metabolismo
Obesidade/enzimologia
[Mh] Termos MeSH secundário: Animais
Ativação Enzimática
Seres Humanos
Metaloproteinase 1 da Matriz/metabolismo
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/metabolismo
Obesidade/fisiopatologia
Inibidores Teciduais de Metaloproteinases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Tissue Inhibitor of Metalloproteinases); EC 3.4.24.- (Collagenases); EC 3.4.24.- (Matrix Metalloproteinases, Secreted); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 3.4.24.7 (Matrix Metalloproteinase 1)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170227
[Lr] Data última revisão:
170227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160730
[St] Status:MEDLINE
[do] DOI:10.2147/VHRM.S103877


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[PMID]:27406754
[Au] Autor:Bouvagnet P; Guimier A; Amiel J; Gordon CT
[Ad] Endereço:Inserm U1217, CNRS 5310, Université Lyon 1, 8, avenue Rockefeller, 69008 Lyon, France.
[Ti] Título:[A gene coding for a metalloprotease for the first time implied in heterotaxy].
[Ti] Título:Un gène codant une métalloprotéase impliqué dans l'hétérotaxie..
[So] Source:Med Sci (Paris);32(6-7):551-3, 2016 Jun-Jul.
[Is] ISSN:1958-5381
[Cp] País de publicação:France
[La] Idioma:fre
[Mh] Termos MeSH primário: Padronização Corporal/genética
Síndrome de Heterotaxia/genética
Metaloproteinases da Matriz Secretadas/genética
[Mh] Termos MeSH secundário: Animais
Embrião de Mamíferos
Embrião não Mamífero
Predisposição Genética para Doença
Seres Humanos
Metaloproteinases da Matriz Secretadas/fisiologia
Metaloproteases/genética
[Pt] Tipo de publicação:NEWS
[Nm] Nome de substância:
EC 3.4.- (Metalloproteases); EC 3.4.24.- (MMP21 protein, human); EC 3.4.24.- (Matrix Metalloproteinases, Secreted)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160714
[St] Status:MEDLINE
[do] DOI:10.1051/medsci/20163206007



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