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Pesquisa : D08.811.277.656.300.480.525.700.450 [Categoria DeCS]
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  1 / 273 MEDLINE  
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[PMID]:29374701
[Au] Autor:Greco M; Arcidiacono B; Chiefari E; Vitagliano T; Ciriaco AG; Brunetti FS; Cuda G; Brunetti A
[Ad] Endereço:Department of Clinical and Experimental Medicine, University "Magna Græcia" of Catanzaro, Catanzaro, Italy.
[Ti] Título:HMGA1 and MMP-11 Are Overexpressed in Human Non-melanoma Skin Cancer.
[So] Source:Anticancer Res;38(2):771-778, 2018 02.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: The High-Mobility Group A1 (HMGA1) protein has been implicated in human malignancies, playing an important role in cancer proliferation, angiogenesis and metastasis. Increased HMGA1 expression has been found in skin mouse tumors, whereas Hmga1-null mice were protected against skin carcinogenesis. Here, we examined the expression of HMGA1 in human skin tumors, squamous cell carcinoma and basal cell carcinoma. MATERIALS AND METHODS: Tumor and normal skin tissues from 15 affected patients were surgically excised, and mRNA and protein extraction was performed. mRNA and protein content for both HMGA1 and MMP-11, a proteinase enzyme that plays a role in tumor development and progression, was measured by real-time PCR and western blotting, respectively. Data were analyzed by the SPSS software. RESULTS: HMGA1 mRNA and protein expression patterns were higher in neoplastic skin lesions, compared to normal skin (p<0.001). Similar results were observed for MMP-11. CONCLUSION: Our data confirm previous observations in mice studies, and suggest that HMGA1 and MMP-11 may play a key role in the proliferation and progression of skin tumors in humans.
[Mh] Termos MeSH primário: Proteína HMGA1a/biossíntese
Metaloproteinase 11 da Matriz/biossíntese
Neoplasias Cutâneas/metabolismo
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Feminino
Proteína HMGA1a/genética
Seres Humanos
Masculino
Metaloproteinase 11 da Matriz/genética
Meia-Idade
RNA Mensageiro/biossíntese
RNA Mensageiro/genética
Neoplasias Cutâneas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 124544-67-8 (HMGA1a Protein); EC 3.4.24.- (MMP11 protein, human); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180129
[St] Status:MEDLINE


  2 / 273 MEDLINE  
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[PMID]:27787597
[Au] Autor:Eiro N; Fernandez-Gomez J; Sacristán R; Fernandez-Garcia B; Lobo B; Gonzalez-Suarez J; Quintas A; Escaf S; Vizoso FJ
[Ad] Endereço:Unidad de Investigación, Fundación Hospital de Jove, Avda. Eduardo Castro, 161, 33920, Gijón, Asturias, Spain.
[Ti] Título:Stromal factors involved in human prostate cancer development, progression and castration resistance.
[So] Source:J Cancer Res Clin Oncol;143(2):351-359, 2017 Feb.
[Is] ISSN:1432-1335
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To detect new predictive markers from the prostate cancer tissue, to study the expression by cultured cancer-associated fibroblasts (CAFs) of stromal factors implicated in prostate carcinogenesis, and to compare their expressions in localized, metastatic, castration-sensitive (CSCP), castration-resistant prostate tumors (CRCP) as well as in fibroblasts from benign prostatic hyperplasia (BPH). MATERIALS AND METHODS: The genomic expression of 20 stroma-derived factors, including the androgen receptor (AR), growth factors (FGF2, FGF7, FGF10, HGF, TGFß, PDGFB), protein implicated in invasion (MMP-2, MMP-9 and MMP-11), inflammation (IL-6, IL-17, STAT-3 and NFκB), stroma/epithelium interaction (CDH11, FAP, CXCL12 and CXCL14) and chaperones (HPA1A and HSF1), was evaluated in cultured fibroblasts both from BHP and prostate carcinomas (PCa). After isolation and culture of fibroblasts by biopsy specimens, RNA was isolated and genomic studies performed. RESULTS: Finally, 5 BPH and 37 PCa specimens were selected: clinically localized (19), metastatic (5), CSCP (7) and CRPC (6). Interleukin-17 receptor (IL-17RB) was highly expressed in CAFs compared with fibroblasts from BPH. However, metalloproteinase-2 and chemokine ligand 14 (CXCL14) were expressed at higher levels by fibroblasts from BPH. The fibroblastic growth factor-7 was highly expressed by CAFs from localized tumors, but metalloproteinase-11 in metastatic tumors. MMP-11, androgen receptor (AR) and heat-shock-70kda-protein-1A (HSPA1A) expressions were significantly higher in CAFs from CRPC. CONCLUSIONS: These results demonstrate a CAFs heterogeneity among prostate carcinomas with regard to some molecular profile expressions that may be relevant in tumor development (IL-17RB), progression (MMP-11) and castration resistance (AR, MMP-11 and HSPA1A).
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Neoplasias de Próstata Resistentes à Castração/metabolismo
[Mh] Termos MeSH secundário: Idoso
Biomarcadores Tumorais/genética
Fibroblastos Associados a Câncer/metabolismo
Carcinogênese/metabolismo
Progressão da Doença
Expressão Gênica
Proteínas de Choque Térmico HSP70/metabolismo
Seres Humanos
Masculino
Metaloproteinase 11 da Matriz/metabolismo
Neoplasias de Próstata Resistentes à Castração/patologia
Receptores Androgênicos/metabolismo
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (HSP70 Heat-Shock Proteins); 0 (HSPA1A protein, human); 0 (Receptors, Androgen); EC 3.4.24.- (MMP11 protein, human); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE
[do] DOI:10.1007/s00432-016-2284-3


  3 / 273 MEDLINE  
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[PMID]:27302099
[Au] Autor:Paul RK; Kumar M; Kataria M
[Ad] Endereço:Division of Animal Biochemistry, ICAR-Indian Veterinary Research Institute, Bareilly, Uttar Pradesh, India.
[Ti] Título:Production of a bioactive recombinant chicken matrix metalloproteinase-11 peptide in Escherichia coli.
[So] Source:Biotechnol Appl Biochem;64(4):555-563, 2017 Jul.
[Is] ISSN:1470-8744
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Matrix metalloproteinase-11 (MMP-11) is known to be highly expressed in metastatic and most invasive forms of tumors. Being selectively expressed in tumor tissues, MMP-11 is a promising target for immunotherapy against tumors. Here, we report the production of a thioredoxin-tagged bioactive recombinant chicken MMP-11 (cMMP-11) peptide excluding the secretory signal and propeptide in Escherichia coli T7 Express lysY using pET32b(+) vector. High-level expression and purification of the bioactive peptide were achieved by induction with 1.0 mM isopropyl-ß-d-thiogalactopyranoside for 4 H at 37 °C followed by affinity chromatography under denaturing condition and slow dialysis. The recombinant peptide exhibited both caseinolytic and gelatinase activities without requiring activation by 4-aminophenylmercuric acetate. The antisera raised against the peptide in rabbits showed a strong reaction with the whole recombinant peptide as well as 37 kDa cMMP-11 mature peptide and cross-reactivity with a 43 kDa protein in murine breast tumor of 4T1 origin in Western blot analysis. The 43 kDa protein in the tumor homogenate showed immunoreactivity with a monoclonal antibody against human MMP-11, suggesting it to be murine MMP-11 having cross-reactivity with the antisera raised against cMMP-11 peptide. Altogether, the study characterized the production of a bioactive and immunogenic recombinant cMMP-11 peptide in E. coli.
[Mh] Termos MeSH primário: Escherichia coli/genética
Metaloproteinase 11 da Matriz/biossíntese
Metaloproteinase 11 da Matriz/genética
[Mh] Termos MeSH secundário: Animais
Galinhas
Clonagem Molecular
Escherichia coli/metabolismo
Metaloproteinase 11 da Matriz/isolamento & purificação
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160616
[St] Status:MEDLINE
[do] DOI:10.1002/bab.1521


  4 / 273 MEDLINE  
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[PMID]:27355528
[Au] Autor:Yonemori M; Seki N; Yoshino H; Matsushita R; Miyamoto K; Nakagawa M; Enokida H
[Ad] Endereço:Department of Urology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima, Japan.
[Ti] Título:Dual tumor-suppressors miR-139-5p and miR-139-3p targeting matrix metalloprotease 11 in bladder cancer.
[So] Source:Cancer Sci;107(9):1233-42, 2016 Sep.
[Is] ISSN:1349-7006
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Our recent study of the microRNA (miRNA) expression signature of bladder cancer (BC) by deep-sequencing revealed that two miRNA, microRNA-139-5p/microRNA-139-3p were significantly downregulated in BC tissues. The aim of this study was to investigate the functional roles of these miRNA and their modulation of cancer networks in BC cells. Functional assays of BC cells were performed using transfection of mature miRNA or small interfering RNA (siRNA). Genome-wide gene expression analysis, in silico analysis and dual-luciferase reporter assays were applied to identify miRNA targets. The associations between the expression of miRNA and its targets and overall survival were estimated by the Kaplan-Meier method. Gain-of-function studies showed that miR-139-5p and miR-139-3p significantly inhibited cell migration and invasion by BC cells. The matrix metalloprotease 11 gene (MMP11) was identified as a direct target of miR-139-5p and miR-139-3p. Kaplan-Meier survival curves showed that higher expression of MMP11 predicted shorter survival of BC patients (P = 0.029). Downregulated miR-139-5p or miR-139-3p enhanced BC cell migration and invasion in BC cells. MMP11 was directly regulated by these miRNA and might be a good prognostic marker for survival of BC patients.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Metaloproteinase 11 da Matriz/genética
MicroRNAs/genética
Interferência de RNA
Neoplasias da Bexiga Urinária/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular
Feminino
Expressão Gênica
Perfilação da Expressão Gênica
Técnicas de Silenciamento de Genes
Genes Reporter
Seres Humanos
Imuno-Histoquímica
Masculino
Prognóstico
RNA Mensageiro/genética
Transfecção
Neoplasias da Bexiga Urinária/mortalidade
Neoplasias da Bexiga Urinária/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN139 microRNA, human); 0 (MicroRNAs); 0 (RNA, Messenger); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160630
[St] Status:MEDLINE
[do] DOI:10.1111/cas.13002


  5 / 273 MEDLINE  
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[PMID]:27141287
[Au] Autor:Jenkins MH; Alrowaished SS; Goody MF; Crawford BD; Henry CA
[Ad] Endereço:School of Biology and Ecology, University of Maine, 217 Hitchner Hall, Orono, ME 04469 USA.
[Ti] Título:Laminin and Matrix metalloproteinase 11 regulate Fibronectin levels in the zebrafish myotendinous junction.
[So] Source:Skelet Muscle;6:18, 2016.
[Is] ISSN:2044-5040
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Remodeling of the extracellular matrix (ECM) regulates cell adhesion as well as signaling between cells and their microenvironment. Despite the importance of tightly regulated ECM remodeling for normal muscle development and function, mechanisms underlying ECM remodeling in vivo remain elusive. One excellent paradigm in which to study ECM remodeling in vivo is morphogenesis of the myotendinous junction (MTJ) during zebrafish skeletal muscle development. During MTJ development, there are dramatic shifts in the primary components comprising the MTJ matrix. One such shift involves the replacement of Fibronectin (Fn)-rich matrix, which is essential for both somite and early muscle development, with laminin-rich matrix essential for normal function of the myotome. Here, we investigate the mechanism underlying this transition. RESULTS: We show that laminin polymerization indirectly promotes Fn downregulation at the MTJ, via a matrix metalloproteinase 11 (Mmp11)-dependent mechanism. Laminin deposition and organization is required for localization of Mmp11 to the MTJ, where Mmp11 is both necessary and sufficient for Fn downregulation in vivo. Furthermore, reduction of residual Mmp11 in laminin mutants promotes a Fn-rich MTJ that partially rescues skeletal muscle architecture. CONCLUSIONS: These results identify a mechanism for Fn downregulation at the MTJ, highlight crosstalk between laminin and Fn, and identify a new in vivo function for Mmp11. Taken together, our data demonstrate a novel signaling pathway mediating Fn downregulation. Our data revealing new regulatory mechanisms that guide ECM remodeling during morphogenesis in vivo may inform pathological conditions in which Fn is dysregulated.
[Mh] Termos MeSH primário: Fibronectinas/metabolismo
Laminina/metabolismo
Metaloproteinase 11 da Matriz/metabolismo
Desenvolvimento Muscular
Músculo Esquelético/enzimologia
Tendões/enzimologia
Proteínas de Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Regulação para Baixo
Regulação da Expressão Gênica no Desenvolvimento
Genótipo
Laminina/genética
Metaloproteinase 11 da Matriz/genética
Músculo Esquelético/embriologia
Mutação
Fenótipo
Transdução de Sinais
Tendões/embriologia
Fatores de Tempo
Técnicas de Cultura de Tecidos
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fibronectins); 0 (Laminin); 0 (Zebrafish Proteins); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160504
[St] Status:MEDLINE
[do] DOI:10.1186/s13395-016-0089-3


  6 / 273 MEDLINE  
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[PMID]:27081863
[Au] Autor:Waresijiang N; Sun J; Abuduaini R; Jiang T; Zhou W; Yuan H
[Ad] Endereço:Department of Orthopaedics, People's Hospital of Xinjiang Uygur Autonomous Region, Urumqi, Xinjiang 830001, P.R. China.
[Ti] Título:The downregulation of miR­125a­5p functions as a tumor suppressor by directly targeting MMP­11 in osteosarcoma.
[So] Source:Mol Med Rep;13(6):4859-64, 2016 Jun.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Osteosarcoma is one of the most common primary malignant bone cancers in juveniles and adults. Increasingly, reports indicate that microRNAs (miRNAs) may provide novel therapeutic targets for cancer treatment. The aim of the present study was to investigate the expression of miR­125a­5p and to identify its functional significance in osteosarcoma. This indicated that miR­125a­5p was downregulated in osteosarcoma tissue and cell lines using reverse transcription­quantitative polymerase chain reaction. Following transfection with miR­125a­5p mimics or the negative control, cell migration, invasion and epithelial­mesenchymal transition (EMT) assays were conducted in osteosarcoma cells. These results indicated that the overexpression of miR­125a­5p resulted in inhibited osteosarcoma cell migration, invasion and EMT in vitro. Furthermore, mechanistic studies showed that matrix metallopeptidase­11 (MMP­11), was a direct target of miR­125a­5p in osteosarcoma. Taken together, the data demonstrate that miR­125a­5p functions as a tumor suppressor gene and serves an important role in inhibiting osteosarcoma cell migration, invasion and EMT by targeting MMP­11.
[Mh] Termos MeSH primário: Neoplasias Ósseas/genética
Regulação Neoplásica da Expressão Gênica
Genes Supressores de Tumor
Metaloproteinase 11 da Matriz/genética
MicroRNAs/genética
Osteossarcoma/genética
Interferência de RNA
[Mh] Termos MeSH secundário: Neoplasias Ósseas/patologia
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular
Transição Epitelial-Mesenquimal/genética
Seres Humanos
Osteossarcoma/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN125 microRNA, human); 0 (MicroRNAs); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170406
[Lr] Data última revisão:
170406
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160416
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2016.5141


  7 / 273 MEDLINE  
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[PMID]:27002762
[Au] Autor:Pang L; Wang DW; Zhang N; Xu DH; Meng XW
[Ad] Endereço:Department of Emergency, The First Hospital of Jilin University, Changchun, Jilin, China.
[Ti] Título:Elevated serum levels of MMP-11 correlate with poor prognosis in colon cancer patients.
[So] Source:Cancer Biomark;16(4):599-607, 2016 Mar 11.
[Is] ISSN:1875-8592
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Matrix metalloproteinase 11 (MMP11) has been shown to play a key role in human tumor progression and indicates poor clinical outcome in cancer patients. OBJECTIVE: The current study aimed to evaluate the relationship between serum levels of MMP-11 and prognosis in colon cancer patients. METHODS: Serum levels of MMP-11 were determined in 92 colon cancer patients and 92 healthy individuals using an enzyme-linked immunosorbent assay (ELISA). Associations between serum MMP-11 levels and clinicopathological characteristics of the patients and their outcomes were investigated. Survival analyses were performed to measure the 5-year overall survival (OS) and disease-free survival (DFS). RESULTS: Serum MMP-11 levels were substantially higher in colon cancer patients than in healthy controls. Moreover, serum MMP-11 levels were significantly higher in patients with advanced T status, lymph node metastasis, distant metastasis, and a higher TNM stage. Elevated serum levels of MMP-11 were identified as an independent prognostic factor for 5-year mortality and adverse events associated with colon cancer. Multivariate Cox regression analysis identified the serum MMP-11 level as an independent predictor of OS and DFS. CONCLUSION: Our study established that high serum levels of MMP-11 are associated with poor clinical outcome and may serve as a prognostic biomarker in colon cancer patients.
[Mh] Termos MeSH primário: Biomarcadores Tumorais
Neoplasias do Colo/sangue
Neoplasias do Colo/mortalidade
Metaloproteinase 11 da Matriz/sangue
[Mh] Termos MeSH secundário: Adulto
Idoso
Estudos de Casos e Controles
Neoplasias do Colo/diagnóstico
Neoplasias do Colo/tratamento farmacológico
Ensaio de Imunoadsorção Enzimática
Feminino
Seres Humanos
Masculino
Meia-Idade
Gradação de Tumores
Metástase Neoplásica
Estadiamento de Neoplasias
Prognóstico
Curva ROC
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 3.4.24.- (MMP11 protein, human); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170118
[Lr] Data última revisão:
170118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160323
[St] Status:MEDLINE
[do] DOI:10.3233/CBM-160601


  8 / 273 MEDLINE  
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[PMID]:26956825
[Au] Autor:Aras AB; Guven M; Balak N; Ayan E; Uyar SB; Elmaci I
[Ad] Endereço:Canakkale Onsekiz Mart University, School of Medicine, Department of Neurosurgery, Canakkale, Turkey.
[Ti] Título:Evaluation of the Association Between Matrix Metalloproteinase 11 and Intervertebral Disc Disease.
[So] Source:Turk Neurosurg;26(2):274-9, 2016.
[Is] ISSN:1019-5149
[Cp] País de publicação:Turkey
[La] Idioma:eng
[Ab] Resumo:AIM: The intervertebral disc starts to degenerate when a human being begins to stand and learn to walk. It is known that many extrinsic, intrinsic and genetic factors play a role in disc degeneration. In this study, we examined whether the matrix metalloproteinase 11 might be associated with intervertebral disc degeneration. MATERIAL AND METHODS: Fifty-six patients with lumbar disc herniations who were operated at Göztepe Education and Research Hospital, Neurosurgery Clinic between September 2008 and December 2009 were prospectively reviewed. History and complaints were obtained from the case reports. Neuroradiological evaluation was performed with magnetic resonance imaging. Surgical findings of cases were reported in the operation notes. Microscopic posterior hemipartial laminectomy and discectomy were performed in all cases. Degenerated herniated disc material of all cases extracted during surgery was evaluated with immunohistochemical staining in Marmara University, Institute of Neurological Sciences, Pathology Laboratory. RESULTS: Comparing the immunohistochemical staining of cases who were 50 years or younger and cases who were over 50 years old, statistical significance was determined. CONCLUSION: Matrix metalloproteinase 11 has a role in degenerating intervertebral disc disease, but it is not the only factor. Matrix metalloproteinase 11 might be a genetic factor in young-middle aged patients.
[Mh] Termos MeSH primário: Deslocamento do Disco Intervertebral/enzimologia
Metaloproteinase 11 da Matriz/biossíntese
[Mh] Termos MeSH secundário: Adolescente
Adulto
Discotomia/métodos
Feminino
Seres Humanos
Imuno-Histoquímica
Disco Intervertebral/cirurgia
Deslocamento do Disco Intervertebral/cirurgia
Laminectomia
Vértebras Lombares/cirurgia
Imagem por Ressonância Magnética
Masculino
Metaloproteinase 11 da Matriz/análise
Meia-Idade
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.24.- (MMP11 protein, human); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160310
[St] Status:MEDLINE
[do] DOI:10.5137/1019-5149.JTN.12762-14.0


  9 / 273 MEDLINE  
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[PMID]:26892540
[Au] Autor:Zhang X; Huang S; Guo J; Zhou L; You L; Zhang T; Zhao Y
[Ad] Endereço:Department of General Surgery, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences/Peking Union Medical College, Beijing 100730, P.R. China.
[Ti] Título:Insights into the distinct roles of MMP-11 in tumor biology and future therapeutics (Review).
[So] Source:Int J Oncol;48(5):1783-93, 2016 May.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:The biological processes of cancer cells such as tumorigenesis, proliferation, angiogenesis, apoptosis and invasion are greatly influenced by the surrounding microenvironment. The ability of solid malignant tumors to alter the microenvironment represents an important characteristic through which tumor cells are able to acquire specific functions necessary for their malignant biological behaviors. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases with the capacity of remodeling extracellular matrix (ECM) by degrading almost all ECM proteins, which plays essential roles during the invasion and metastasis process of solid malignant tumors, including allowing tumor cells to modify the ECM components and release cytokines, ultimately facilitating protease-dependent tumor progression. MMP-11, also named stromelysin-3, is a member of the stromelysin subgroup belonging to MMPs superfamily, which has been detected in cancer cells, stromal cells and adjacent microenvironment. Differently, MMP-11 exerts a dual effect on tumors. On the one hand MMP-11 promotes cancer development by inhibiting apoptosis as well as enhancing migration and invasion of cancer cells, on the other hand MMP-11 plays a negative role against cancer development via suppressing metastasis in animal models. Overexpression of MMP-11 was discovered in sera of cancer patients compared with normal control group as well as in multiple tumor tissue specimens, such as gastric cancer, breast cancer, and pancreatic cancer. At present, some evidence supports that MMP-11 may work as a significant tumor biomarker for early detection of cancer, tumor staging, prognostic analysis, monitoring recurrence during follow-up and also a potential target for immunotherapy against cancer. In view of the importance of MMP-11 in modifying tumor microenvironment and potent antitumoral effects on solid tumors, there is an urgent need for a deeper understanding of how MMP-11 modulates tumor progression, and exploring its potential clinical application.
[Mh] Termos MeSH primário: Metaloproteinase 11 da Matriz/metabolismo
Neoplasias/patologia
Regulação para Cima
[Mh] Termos MeSH secundário: Animais
Biomarcadores Tumorais/sangue
Proliferação Celular
Progressão da Doença
Detecção Precoce de Câncer
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Metaloproteinase 11 da Matriz/sangue
Neoplasias/metabolismo
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 3.4.24.- (MMP11 protein, human); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160220
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2016.3400


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[PMID]:26861489
[Au] Autor:Li WM; Wei YC; Huang CN; Ke HL; Li CC; Yeh HC; Chang LL; Huang CH; Li CF; Wu WJ
[Ad] Endereço:Graduate Institute of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
[Ti] Título:Matrix metalloproteinase-11 as a marker of metastasis and predictor of poor survival in urothelial carcinomas.
[So] Source:J Surg Oncol;113(6):700-7, 2016 May.
[Is] ISSN:1096-9098
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND OBJECTIVES: Urothelial carcinomas (UC) of urinary bladder (UB) and upper urinary tract (UT) are heterogeneous diseases with high morbidity and mortality. We looked for genes with metalloendopeptidase activity in a published UBUC transcriptomic database (GSE31684):MMP-11 was the most significant, showing stepwise up-regulation. We analyzed MMP-11 expression and association with clinicopathologic factors and survival in our well-characterized cohort of UCs. METHODS: We determined MMP-11 expression in 295 UBUCs and 340 UTUCs with immunohistochemistry, evaluated by H-score. In a retrospective study, MMP-11 expression was correlated with clinicopathologic features and with disease-specific survival (DSS) and metastasis-free survival (MeFS). The statistical significance was evaluated with univariate and multivariate analyses. RESULTS: High MMP-11 expression was significantly associated with advanced pT status, nodal metastasis, high histological grade, vascular and perineural invasion, and frequent mitoses. In multivariate Cox regression analyses, which adjusted for standard clinicopathologic characteristics, MMP-11 expression was independently associated with cancer-specific mortality (hazard ratio [HR] in UTUC:3.027, P = 0.005; in UBUC: 2.631, P = 0.010) and with metastasis development (HR in UTUC:2.261, P = 0.018; in UBUC:1.801, P = 0.026). CONCLUSIONS: MMP-11 overexpression is associated with aggressive tumor phenotype and unfavorable clinical outcome in UTUC and UBUC, suggesting it may serve as a novel prognostic and therapeutic target. J. Surg. Oncol. 2016;113:700-707. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Carcinoma de Células de Transição/diagnóstico
Metaloproteinase 11 da Matriz/metabolismo
Neoplasias da Bexiga Urinária/diagnóstico
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Carcinoma de Células de Transição/metabolismo
Carcinoma de Células de Transição/mortalidade
Carcinoma de Células de Transição/patologia
Feminino
Seguimentos
Seres Humanos
Imuno-Histoquímica
Masculino
Meia-Idade
Metástase Neoplásica
Prognóstico
Estudos Retrospectivos
Análise de Sobrevida
Regulação para Cima
Neoplasias da Bexiga Urinária/metabolismo
Neoplasias da Bexiga Urinária/mortalidade
Neoplasias da Bexiga Urinária/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 3.4.24.- (MMP11 protein, human); EC 3.4.24.- (Matrix Metalloproteinase 11)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170203
[Lr] Data última revisão:
170203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE
[do] DOI:10.1002/jso.24195



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