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Pesquisa : D08.811.277.656.300.480.664 [Categoria DeCS]
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[PMID]:29364909
[Au] Autor:de Bruyn JR; Becker MA; Steenkamer J; Wildenberg ME; Meijer SL; Buskens CJ; Bemelman WA; Löwenberg M; Ponsioen CY; van den Brink GR; D'Haens GR
[Ad] Endereço:Department of Gastroenterology and Hepatology, Academic Medical Center, Amsterdam, The Netherlands.
[Ti] Título:Intestinal fibrosis is associated with lack of response to Infliximab therapy in Crohn's disease.
[So] Source:PLoS One;13(1):e0190999, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Overt fibrostenotic disease is a relative contraindication for anti-TNF therapy in Crohn's disease. We hypothesized that subclinical fibrosis may also contribute to an incomplete response to anti-TNF therapy before the onset of symptomatic stenosis. METHODS: In a previous trial, patients with ileocecal Crohn's disease were randomized to either immediate ileocecal resection or medical treatment with Infliximab. In case of insufficient response to Infliximab, the latter underwent secondary ileocecal resection. We compared specimens from those patients undergoing immediate resection (Infliximab naïve, n = 20) to those who failed Infliximab therapy (n = 20). RESULTS: Infliximab naïve and Infliximab failure patients had similar severity of inflammation when assessed by CRP levels (median 14 vs 9 mg/L) and histology (Geboes-D'Haens-score, median 10 vs 11 points). On immunohistochemistry, collagen-III and fibronectin depositions were increased in patients previously exposed to Infliximab compared to patients naïve to Infliximab. On mRNA level, procollagen peptidase showed significantly more mucosal mRNA expression in Crohn's disease patients who failed Infliximab. Infliximab responders showed no increase of this marker after 4 weeks of successful Infliximab treatment. DISCUSSION: Failure to Infliximab therapy is associated with subclinical fibrosis in Crohn's disease.
[Mh] Termos MeSH primário: Doença de Crohn/tratamento farmacológico
Fármacos Gastrointestinais/uso terapêutico
Infliximab/uso terapêutico
Enteropatias/complicações
[Mh] Termos MeSH secundário: Adulto
Doença de Crohn/complicações
Doença de Crohn/metabolismo
Proteínas da Matriz Extracelular/metabolismo
Feminino
Fibrose
Seres Humanos
Enteropatias/metabolismo
Enteropatias/patologia
Mucosa Intestinal/enzimologia
Masculino
Meia-Idade
Pró-Colágeno N-Endopeptidase/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Extracellular Matrix Proteins); 0 (Gastrointestinal Agents); B72HH48FLU (Infliximab); EC 3.4.24.14 (Procollagen N-Endopeptidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190999


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[PMID]:28213441
[Au] Autor:Ogino H; Hisanaga A; Kohno T; Kondo Y; Okumura K; Kamei T; Sato T; Asahara H; Tsuiji H; Fukata M; Hattori M
[Ad] Endereço:Department of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi 467-8603, Japan.
[Ti] Título:Secreted Metalloproteinase ADAMTS-3 Inactivates Reelin.
[So] Source:J Neurosci;37(12):3181-3191, 2017 Mar 22.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The secreted glycoprotein Reelin regulates embryonic brain development and adult brain functions. It has been suggested that reduced Reelin activity contributes to the pathogenesis of several neuropsychiatric and neurodegenerative disorders, such as schizophrenia and Alzheimer's disease; however, noninvasive methods that can upregulate Reelin activity have yet to be developed. We previously found that the proteolytic cleavage of Reelin within Reelin repeat 3 (N-t site) abolishes Reelin activity , but it remains controversial as to whether this effect occurs Here we partially purified the enzyme that mediates the N-t cleavage of Reelin from the culture supernatant of cerebral cortical neurons. This enzyme was identified as a disintegrin and metalloproteinase with thrombospondin motifs-3 (ADAMTS-3). Recombinant ADAMTS-3 cleaved Reelin at the N-t site. ADAMTS-3 was expressed in excitatory neurons in the cerebral cortex and hippocampus. N-t cleavage of Reelin was markedly decreased in the embryonic cerebral cortex of ADAMTS-3 knock-out (KO) mice. Importantly, the amount of Dab1 and the phosphorylation level of Tau, which inversely correlate with Reelin activity, were significantly decreased in the cerebral cortex of ADAMTS-3 KO mice. Conditional KO mice, in which ADAMTS-3 was deficient only in the excitatory neurons of the forebrain, showed increased dendritic branching and elongation in the postnatal cerebral cortex. Our study shows that ADAMTS-3 is the major enzyme that cleaves and inactivates Reelin in the cerebral cortex and hippocampus. Therefore, inhibition of ADAMTS-3 may be an effective treatment for neuropsychiatric and neurodegenerative disorders. ADAMTS-3 was identified as the protease that cleaves and inactivates Reelin in the cerebral cortex and hippocampus. ADAMTS-3 was expressed in the excitatory neurons of the embryonic and postnatal cerebral cortex and hippocampus. Cleavage by ADAMTS-3 is the major contributor of Reelin inactivation Tau phosphorylation was decreased and dendritic branching and elongation was increased in ADAMTS-3-deficient mice. Therefore, inhibition of ADAMTS-3 upregulates Reelin activity and may be a potential therapeutic strategy for the prevention or treatment of neuropsychiatric and neurodegenerative disorders, such as schizophrenia and Alzheimer's disease.
[Mh] Termos MeSH primário: Proteínas ADAMTS/secreção
Moléculas de Adesão Celular Neuronais/metabolismo
Córtex Cerebral/metabolismo
Proteínas da Matriz Extracelular/metabolismo
Hipocampo/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Neurônios/metabolismo
Pró-Colágeno N-Endopeptidase/secreção
Serina Endopeptidases/metabolismo
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Ativação Enzimática
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos ICR
Camundongos Knockout
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (Extracellular Matrix Proteins); 0 (Nerve Tissue Proteins); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (reelin protein); EC 3.4.24.- (ADAMTS Proteins); EC 3.4.24.- (ADAMTS3 protein, human); EC 3.4.24.14 (Procollagen N-Endopeptidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.3632-16.2017


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[PMID]:28146470
[Au] Autor:Marouli E; Graff M; Medina-Gomez C; Lo KS; Wood AR; Kjaer TR; Fine RS; Lu Y; Schurmann C; Highland HM; Rüeger S; Thorleifsson G; Justice AE; Lamparter D; Stirrups KE; Turcot V; Young KL; Winkler TW; Esko T; Karaderi T; Locke AE; Masca NG; Ng MC; Mudgal P; Rivas MA; Vedantam S; Mahajan A; Guo X; Abecasis G; Aben KK; Adair LS; Alam DS; Albrecht E; Allin KH; Allison M; Amouyel P; Appel EV; Arveiler D; Asselbergs FW; Auer PL; Balkau B; Banas B; Bang LE; Benn M; Bergmann S; Bielak LF; Blüher M; Boeing H; Boerwinkle E; Böger CA; EPIC-InterAct Consortium; CHD Exome; Consortium; ExomeBP Consortium; T2D-Genes Consortium; GoT2D Genes Consortium; Global Lipids Genetics Consortium; ReproGen Consortium; MAGIC Investigators
[Ad] Endereço:William Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, London EC1M 6BQ, UK.
[Ti] Título:Rare and low-frequency coding variants alter human adult height.
[So] Source:Nature;542(7640):186-190, 2017 02 09.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Height is a highly heritable, classic polygenic trait with approximately 700 common associated variants identified through genome-wide association studies so far. Here, we report 83 height-associated coding variants with lower minor-allele frequencies (in the range of 0.1-4.8%) and effects of up to 2 centimetres per allele (such as those in IHH, STC2, AR and CRISPLD2), greater than ten times the average effect of common variants. In functional follow-up studies, rare height-increasing alleles of STC2 (giving an increase of 1-2 centimetres per allele) compromised proteolytic inhibition of PAPP-A and increased cleavage of IGFBP-4 in vitro, resulting in higher bioavailability of insulin-like growth factors. These 83 height-associated variants overlap genes that are mutated in monogenic growth disorders and highlight new biological candidates (such as ADAMTS3, IL11RA and NOX4) and pathways (such as proteoglycan and glycosaminoglycan synthesis) involved in growth. Our results demonstrate that sufficiently large sample sizes can uncover rare and low-frequency variants of moderate-to-large effect associated with polygenic human phenotypes, and that these variants implicate relevant genes and pathways.
[Mh] Termos MeSH primário: Estatura/genética
Frequência do Gene/genética
Variação Genética/genética
[Mh] Termos MeSH secundário: Proteínas ADAMTS/genética
Adulto
Alelos
Moléculas de Adesão Celular/genética
Feminino
Genoma Humano/genética
Glicoproteínas/genética
Glicoproteínas/metabolismo
Glicosaminoglicanos/biossíntese
Proteínas Hedgehog/genética
Seres Humanos
Peptídeos e Proteínas de Sinalização Intercelular/genética
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Fatores Reguladores de Interferon/genética
Subunidade alfa de Receptor de Interleucina-11/genética
Masculino
Herança Multifatorial/genética
NADPH Oxidase 4
NADPH Oxidases/genética
Fenótipo
Proteína Plasmática A Associada à Gravidez/metabolismo
Pró-Colágeno N-Endopeptidase/genética
Proteoglicanas/biossíntese
Proteólise
Receptores Androgênicos/genética
Somatomedinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AR protein, human); 0 (CRISPLD2 protein, human); 0 (Cell Adhesion Molecules); 0 (Glycoproteins); 0 (Glycosaminoglycans); 0 (Hedgehog Proteins); 0 (IHH protein, human); 0 (IL11RA protein, human); 0 (Intercellular Signaling Peptides and Proteins); 0 (Interferon Regulatory Factors); 0 (Interleukin-11 Receptor alpha Subunit); 0 (Proteoglycans); 0 (Receptors, Androgen); 0 (STC2 protein, human); 0 (Somatomedins); EC 1.6.3.- (NADPH Oxidase 4); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX4 protein, human); EC 3.4.24.- (ADAMTS Proteins); EC 3.4.24.- (ADAMTS3 protein, human); EC 3.4.24.- (Pregnancy-Associated Plasma Protein-A); EC 3.4.24.14 (Procollagen N-Endopeptidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170202
[St] Status:MEDLINE
[do] DOI:10.1038/nature21039


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[PMID]:28088271
[Au] Autor:Pekcan MK; Sarikaya E; Tokmak A; Alisik M; Alkan A; Özaksit G; Erel Ö
[Ad] Endereço:Department of Obstetrics and Gynecology, Zekai Tahir Burak Women's Health Education and Research Hospital, Ankara, Turkey.
[Ti] Título:ADAMTS-3, -13, -16, and -19 levels in patients with habitual abortion.
[So] Source:Kaohsiung J Med Sci;33(1):30-35, 2017 Jan.
[Is] ISSN:1607-551X
[Cp] País de publicação:China (Republic : 1949- )
[La] Idioma:eng
[Ab] Resumo:A disintegrin-like and metalloproteinase domain with thrombospondin-type 1 motifs (ADAMTS) protein superfamily includes 19 secreted metalloproteases. Proteolytic substrates of ADAMTS enzymes have been linked to reproductive function. The aim of this study was to investigate serum ADAMTS-3, -13, -16, and -19 levels in women with habitual abortions compared with those in healthy controls. A total of 86 women were enrolled in this prospective case-control study. ADAMTS-3, -13, -16, and -19 values were recorded and analyzed in association with demographic and clinical parameters. There were no statistically significant differences between the two groups in terms of demographics. No statistically significant differences were observed between the groups with regard to ADAMTS-13 and -19 levels (p>0.05). However, ADAMTS-3 and -16 were significantly higher in the study group than in the control group (p=0.004 and p=0.005, respectively). To estimate habitual abortions using an area under receiver operating characteristic curve analysis, the cutoff values for ADAMTS-3 and -16 were found to be 87.28 ng/mL (sensitivity, 64.44%; specificity 68.29%) and 15.75 ng/mL (sensitivity, 66.67%; specificity 68.29%), respectively. In conclusion, the pregnancy-loss rate seems to be affected by both ADAMTS-3 and -16.
[Mh] Termos MeSH primário: Proteínas ADAMTS/genética
Proteína ADAMTS13/genética
Aborto Habitual/genética
Pró-Colágeno N-Endopeptidase/genética
[Mh] Termos MeSH secundário: Proteínas ADAMTS/sangue
Proteína ADAMTS13/sangue
Aborto Habitual/sangue
Aborto Habitual/diagnóstico
Aborto Habitual/patologia
Adulto
Área Sob a Curva
Biomarcadores/sangue
Estudos de Casos e Controles
Feminino
Expressão Gênica
Seres Humanos
Gravidez
Pró-Colágeno N-Endopeptidase/sangue
Estudos Prospectivos
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); EC 3.4.24.- (ADAMTS Proteins); EC 3.4.24.- (ADAMTS16 protein, human); EC 3.4.24.- (ADAMTS19 protein, human); EC 3.4.24.- (ADAMTS3 protein, human); EC 3.4.24.14 (Procollagen N-Endopeptidase); EC 3.4.24.87 (ADAMTS13 Protein); EC 3.4.24.87 (ADAMTS13 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170116
[St] Status:MEDLINE


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[PMID]:27159393
[Au] Autor:Bui HM; Enis D; Robciuc MR; Nurmi HJ; Cohen J; Chen M; Yang Y; Dhillon V; Johnson K; Zhang H; Kirkpatrick R; Traxler E; Anisimov A; Alitalo K; Kahn ML
[Ti] Título:Proteolytic activation defines distinct lymphangiogenic mechanisms for VEGFC and VEGFD.
[So] Source:J Clin Invest;126(6):2167-80, 2016 Jun 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lymphangiogenesis is supported by 2 homologous VEGFR3 ligands, VEGFC and VEGFD. VEGFC is required for lymphatic development, while VEGFD is not. VEGFC and VEGFD are proteolytically cleaved after cell secretion in vitro, and recent studies have implicated the protease a disintegrin and metalloproteinase with thrombospondin motifs 3 (ADAMTS3) and the secreted factor collagen and calcium binding EGF domains 1 (CCBE1) in this process. It is not well understood how ligand proteolysis is controlled at the molecular level or how this process regulates lymphangiogenesis, because these complex molecular interactions have been difficult to follow ex vivo and test in vivo. Here, we have developed and used biochemical and cellular tools to demonstrate that an ADAMTS3-CCBE1 complex can form independently of VEGFR3 and is required to convert VEGFC, but not VEGFD, into an active ligand. Consistent with these ex vivo findings, mouse genetic studies revealed that ADAMTS3 is required for lymphatic development in a manner that is identical to the requirement of VEGFC and CCBE1 for lymphatic development. Moreover, CCBE1 was required for in vivo lymphangiogenesis stimulated by VEGFC but not VEGFD. Together, these studies reveal that lymphangiogenesis is regulated by two distinct proteolytic mechanisms of ligand activation: one in which VEGFC activation by ADAMTS3 and CCBE1 spatially and temporally patterns developing lymphatics, and one in which VEGFD activation by a distinct proteolytic mechanism may be stimulated during inflammatory lymphatic growth.
[Mh] Termos MeSH primário: Linfangiogênese/fisiologia
Fator C de Crescimento do Endotélio Vascular/metabolismo
Fator D de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Proteínas ADAMTS/deficiência
Proteínas ADAMTS/genética
Proteínas ADAMTS/metabolismo
Animais
Proteínas de Ligação ao Cálcio/deficiência
Proteínas de Ligação ao Cálcio/genética
Proteínas de Ligação ao Cálcio/metabolismo
Proliferação Celular
Células Endoteliais/citologia
Células Endoteliais/metabolismo
Células HEK293
Seres Humanos
Ligantes
Linfangiogênese/genética
Vasos Linfáticos/metabolismo
Camundongos
Camundongos Knockout
Modelos Biológicos
Peptídeo Hidrolases/metabolismo
Pró-Colágeno N-Endopeptidase/genética
Pró-Colágeno N-Endopeptidase/metabolismo
Transdução de Sinais
Proteínas Supressoras de Tumor/deficiência
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
Fator C de Crescimento do Endotélio Vascular/deficiência
Fator C de Crescimento do Endotélio Vascular/genética
Fator D de Crescimento do Endotélio Vascular/deficiência
Fator D de Crescimento do Endotélio Vascular/genética
Receptor 3 de Fatores de Crescimento do Endotélio Vascular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (Ccbe1 protein, mouse); 0 (Ligands); 0 (Tumor Suppressor Proteins); 0 (VEGFC protein, human); 0 (VEGFD protein, human); 0 (Vascular Endothelial Growth Factor C); 0 (Vascular Endothelial Growth Factor D); 0 (vascular endothelial growth factor C, mouse); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-3); EC 3.4.- (Peptide Hydrolases); EC 3.4.24.- (ADAMTS Proteins); EC 3.4.24.- (ADAMTS3 protein, human); EC 3.4.24.14 (Procollagen N-Endopeptidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160510
[St] Status:MEDLINE


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[PMID]:26927563
[Au] Autor:Fu J; Miao S; Wang L
[Ad] Endereço:State Key Laboratory of Medical Molecular Biology, Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, Peking Union Medical College, Beijing 100005, China.
[Ti] Título:[Preparation of rabbit polyclonal antibody against mouse ADAMTS2].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;32(3):393-6, 2016 Mar.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To obtain recombinant mouse collagenase ADAMTS2 (ADAM metallopeptidase with thrombospondin type 1 motif, 2) C terminal (1109-1213), and prepare the corresponding rabbit anti-ADAMTS2 polyclonal antibodies. METHODS: The recombinant expression plasmid pGEX-6p-1-ADAMTS2 (1109-1213) was transformed into E.coli. The target protein was induced by IPTG and identified by mass spectrometry following affinity purification. The expressed and purified ADAMTS2 (1109-1213) protein was used to immunize New Zealand rabbits to prepare anti-ADAMTS2 polyclonal antibodies. The antibody titers were detected by ELISA and the antibody specificity by Western blotting. RESULTS: The protein ADAMTS2 (1109-1213) was expressed in E.coli after IPTG induction, and with the purified protein, we prepared antiserum in the immunized rabbits. The titer of the antiserum reached over 1:160 000. The antiserum showed a good specificity. CONCLUSION: The high titer and specific rabbit anti-ADAMTS2 antibody has been prepared successfully.
[Mh] Termos MeSH primário: Proteínas ADAM/imunologia
Anticorpos Monoclonais/imunologia
Soros Imunes/imunologia
Pró-Colágeno N-Endopeptidase/imunologia
Proteínas Recombinantes/imunologia
[Mh] Termos MeSH secundário: Proteínas ADAM/genética
Proteínas ADAM/metabolismo
Proteínas ADAMTS
Proteína ADAMTS4
Animais
Especificidade de Anticorpos/imunologia
Western Blotting
Ensaio de Imunoadsorção Enzimática
Feminino
Masculino
Camundongos Endogâmicos C57BL
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/imunologia
Fragmentos de Peptídeos/metabolismo
Pró-Colágeno N-Endopeptidase/genética
Pró-Colágeno N-Endopeptidase/metabolismo
Coelhos
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Immune Sera); 0 (Peptide Fragments); 0 (Recombinant Proteins); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (ADAMTS Proteins); EC 3.4.24.14 (Adamts2 protein, mouse); EC 3.4.24.14 (Procollagen N-Endopeptidase); EC 3.4.24.82 (ADAMTS4 Protein)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160302
[St] Status:MEDLINE


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[PMID]:26921206
[Au] Autor:Chou PH; Wang ST; Yen MH; Liu CL; Chang MC; Lee OK
[Ad] Endereço:School of Medicine, National Yang-Ming University, Taipei, Taiwan.
[Ti] Título:Fluid-induced, shear stress-regulated extracellular matrix and matrix metalloproteinase genes expression on human annulus fibrosus cells.
[So] Source:Stem Cell Res Ther;7:34, 2016 Feb 27.
[Is] ISSN:1757-6512
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mechanical loading plays an important role in the regulation of extracellular matrix (ECM) homeostasis as well as pathogenesis of intervertebral disc (IVD) degeneration. The human annulus fibrosus (hAF) in the IVD is subjected to contact shear stress during body motion. However, the effects of shear stress on hAF cells remain unclear. This aim of the study was to investigate the expression of the ECM (COLI, COLIII and aggrecan) and matrix metalloproteinase (MMP-1, MMP-3 and ADAMTS-4) genes in hAF cells following fluid-induced shear stress in a custom-fabricated bio-microfluidic device. METHODS: hAF cells were harvested from degenerated disc tissues in routine spine surgery, staged by magnetic resonance imaging, expanded in monolayers and then seeded onto the bio-microfluidic device. The experimental groups were subjected to 1 and 10 dyne/cm(2) shear stress for 4 h, and no shear stress was applied to the control group. We used real time polymerase chain reaction for gene expression. RESULTS: Shear stress of 1 dyne/cm(2) exerted an anabolic effect on COLI and COLIII genes and catabolic effects on the aggrecan gene, while 10 dyne/cm(2) had an anabolic effect on the COLI gene and a catabolic effect on COLIII and aggrecan genes. The COLI gene was upregulated in a stress-dependent manner. Expression of MMP-1 was significantly higher in the 10 dyne/cm(2) group compared to the control group (P < 0.05), but was similar in the control and 1 dyne/cm(2) groups. Expression of MMP-3 and ADAMTS-4 were similar in all three groups. CONCLUSION: Taken together, hAF cells responded to shear stress. The findings help us understand and clarify the effects of shear stress on IVD degeneration as well as the development of a new therapeutic strategy for IVD degeneration.
[Mh] Termos MeSH primário: Matriz Extracelular/enzimologia
[Mh] Termos MeSH secundário: Proteínas ADAM/genética
Proteínas ADAM/metabolismo
Proteína ADAMTS4
Fenômenos Biomecânicos
Células Cultivadas
Indução Enzimática
Matriz Extracelular/genética
Feminino
Expressão Gênica
Seres Humanos
Disco Intervertebral/enzimologia
Disco Intervertebral/patologia
Degeneração do Disco Intervertebral/enzimologia
Degeneração do Disco Intervertebral/patologia
Masculino
Metaloproteinase 1 da Matriz/genética
Metaloproteinase 1 da Matriz/metabolismo
Metaloproteinase 3 da Matriz/genética
Metaloproteinase 3 da Matriz/metabolismo
Meia-Idade
Pró-Colágeno N-Endopeptidase/genética
Pró-Colágeno N-Endopeptidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.24.- (ADAM Proteins); EC 3.4.24.14 (Procollagen N-Endopeptidase); EC 3.4.24.17 (MMP3 protein, human); EC 3.4.24.17 (Matrix Metalloproteinase 3); EC 3.4.24.7 (MMP1 protein, human); EC 3.4.24.7 (Matrix Metalloproteinase 1); EC 3.4.24.82 (ADAMTS4 Protein); EC 3.4.24.82 (ADAMTS4 protein, human)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170103
[Lr] Data última revisão:
170103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160228
[St] Status:MEDLINE
[do] DOI:10.1186/s13287-016-0292-5


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[PMID]:26916548
[Au] Autor:Lima MA; da Silva SV; Freitas VM
[Ad] Endereço:Cell and Developmental Biology Department, Biomedical Sciences Institute (ICB), University of Sao Paulo, Avenida Professor Lineu Prestes, 1524, Biomédicas 1, room 428, São Paulo, SP, 05508-000, Brazil. maira.alima@hotmail.com.
[Ti] Título:Progesterone acts via the progesterone receptor to induce adamts proteases in ovarian cancer cells.
[So] Source:J Ovarian Res;9:9, 2016 Feb 25.
[Is] ISSN:1757-2215
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Ovarian carcinomas, usually associated with sex hormones dysregulation, are the leading cause of gynecological neoplastic death. In normal ovaries, hormones play a central role in regulating cell proliferation, differentiation, and apoptosis. On the other hand, hormonal alterations also play a variety of roles in cancer. Stimulation by sex hormones potentially affects gene expression, invasiveness, cell growth and angiogenesis. Proteases of the "a disintegrin and metalloproteinase with thrombospondin motifs" (ADAMTS) family are secreted by different cell types and become involved in collagen processing, cleavage of the proteoglycan matrix, and angiogenesis. We evaluated whether sex hormones affect ADAMTS 1 and 4 expression in ovarian cancer cells. METHODS: We analysed mRNA and protein levels in human ovarian tumor cells with different degrees of malignancy, NIH-OVCAR-3 and ES-2, that were treated or not with estrogen, testosterone and progesterone. RESULTS: Our results suggest that progesterone increases ADAMTS protein and mRNA levels in the lysates from ES-2 cells, and it increases ADAMTS protein in the lysates and conditioned media from NIH-OVCAR-3. Progesterone effects were reversed by RU486 treatment. CONCLUSION: We conclude that progesterone acts via the progesterone receptor to modulate ADAMTS 1 and 4 levels in ovarian cancer cell lines.
[Mh] Termos MeSH primário: Proteínas ADAM/metabolismo
Pró-Colágeno N-Endopeptidase/metabolismo
Progesterona/fisiologia
Receptores de Progesterona/metabolismo
[Mh] Termos MeSH secundário: Proteínas ADAM/genética
Proteína ADAMTS1
Proteína ADAMTS4
Linhagem Celular Tumoral
Indução Enzimática
Feminino
Expressão Gênica
Seres Humanos
Mifepristona/farmacologia
Neoplasias Ovarianas
Pró-Colágeno N-Endopeptidase/genética
Receptores Androgênicos/metabolismo
Receptores Estrogênicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Receptors, Androgen); 0 (Receptors, Estrogen); 0 (Receptors, Progesterone); 320T6RNW1F (Mifepristone); 4G7DS2Q64Y (Progesterone); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (ADAMTS1 Protein); EC 3.4.24.- (ADAMTS1 protein, human); EC 3.4.24.14 (Procollagen N-Endopeptidase); EC 3.4.24.82 (ADAMTS4 Protein)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170103
[Lr] Data última revisão:
170103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160227
[St] Status:MEDLINE
[do] DOI:10.1186/s13048-016-0219-x


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[PMID]:26809777
[Au] Autor:Lemarchant S; Pomeshchik Y; Kidin I; Kärkkäinen V; Valonen P; Lehtonen S; Goldsteins G; Malm T; Kanninen K; Koistinaho J
[Ad] Endereço:Department of Neurobiology, A. I. Virtanen Institute for Molecular Sciences, Biocenter Kuopio, University of Eastern Finland, P.O. Box 1627, 70211, Kuopio, Finland. sighild.lemarchant@uef.fi.
[Ti] Título:ADAMTS-4 promotes neurodegeneration in a mouse model of amyotrophic lateral sclerosis.
[So] Source:Mol Neurodegener;11:10, 2016 Jan 25.
[Is] ISSN:1750-1326
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) proteoglycanases are specialized in the degradation of chondroitin sulfate proteoglycans and participate in mechanisms mediating neuroplasticity. Despite the beneficial effect of ADAMTS-4 on neurorepair after spinal cord injury, the functions of ADAMTS proteoglycanases in other CNS disease states have not been studied. Therefore, we investigated the expression, effects and associated mechanisms of ADAMTS-4 during amyotrophic lateral sclerosis (ALS) in the SOD1(G93A) mouse model. RESULTS: ADAMTS-4 expression and activity were reduced in the spinal cord of SOD1(G93A) mice at disease end-stage when compared to WT littermates. To counteract the loss of ADAMTS-4, SOD1(G93A) and WT mice were treated with saline or a recombinant ADAMTS-4 before symptom onset. Administration of ADAMTS-4 worsened the prognosis of SOD1(G93A) mice by accelerating clinical signs of neuromuscular dysfunctions. The worsened prognosis of ADAMTS-4-treated SOD1(G93A) mice was accompanied by increased degradation of perineuronal nets enwrapping motoneurons and increased motoneuron degeneration in the lumbar spinal cord. Motoneurons of ADAMTS-4-treated SOD1(G93A) mice were more vulnerable to degeneration most likely due to the loss of their extracellular matrix envelopes. The decrease of neurotrophic factor production induced by ADAMTS-4 in vitro and in vivo may also contribute to a hostile environment for motoneuron especially when devoid of a net. CONCLUSIONS: This study suggests that the reduction of ADAMTS-4 activity during the progression of ALS pathology may be an adaptive change to mitigate its neurodegenerative impact in CNS tissues. Therapies compensating the compromized ADAMTS-4 activity are likely not promising approaches for treating ALS.
[Mh] Termos MeSH primário: Proteínas ADAM/metabolismo
Esclerose Amiotrófica Lateral/metabolismo
Neurônios Motores/metabolismo
Neurônios Motores/patologia
Pró-Colágeno N-Endopeptidase/metabolismo
Medula Espinal/metabolismo
[Mh] Termos MeSH secundário: Proteína ADAMTS4
Esclerose Amiotrófica Lateral/patologia
Animais
Encéfalo/metabolismo
Modelos Animais de Doenças
Progressão da Doença
Feminino
Masculino
Camundongos Transgênicos
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.15.1.1 (Superoxide Dismutase); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.14 (Procollagen N-Endopeptidase); EC 3.4.24.82 (ADAMTS4 Protein)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160127
[St] Status:MEDLINE
[do] DOI:10.1186/s13024-016-0078-3


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[PMID]:26755702
[Au] Autor:Tonna S; Poulton IJ; Taykar F; Ho PW; Tonkin B; Crimeen-Irwin B; Tatarczuch L; McGregor NE; Mackie EJ; Martin TJ; Sims NA
[Ad] Endereço:St Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia The University of Melbourne, Department of Medicine at St Vincent's Hospital, Fitzroy, Victoria 3065, Australia.
[Ti] Título:Chondrocytic ephrin B2 promotes cartilage destruction by osteoclasts in endochondral ossification.
[So] Source:Development;143(4):648-57, 2016 Feb 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The majority of the skeleton arises by endochondral ossification, whereby cartilaginous templates expand and are resorbed by osteoclasts then replaced by osteoblastic bone formation. Ephrin B2 is a receptor tyrosine kinase expressed by osteoblasts and growth plate chondrocytes that promotes osteoblast differentiation and inhibits osteoclast formation. We investigated the role of ephrin B2 in endochondral ossification using Osx1Cre-targeted gene deletion. Neonatal Osx1Cre.Efnb2(Δ/Δ) mice exhibited a transient osteopetrosis demonstrated by increased trabecular bone volume with a high content of growth plate cartilage remnants and increased cortical thickness, but normal osteoclast numbers within the primary spongiosa. Osteoclasts at the growth plate had an abnormal morphology and expressed low levels of tartrate-resistant acid phosphatase; this was not observed in more mature bone. Electron microscopy revealed a lack of sealing zones and poor attachment of Osx1Cre.Efnb2(Δ/Δ) osteoclasts to growth plate cartilage. Osteoblasts at the growth plate were also poorly attached and impaired in their ability to deposit osteoid. By 6 months of age, trabecular bone mass, osteoclast morphology and osteoid deposition by Osx1Cre.Efnb2(Δ/Δ) osteoblasts were normal. Cultured chondrocytes from Osx1Cre.Efnb2(Δ/Δ) neonates showed impaired support of osteoclastogenesis but no significant change in Rankl (Tnfsf11) levels, whereas Adamts4 levels were significantly reduced. A population of ADAMTS4(+) early hypertrophic chondrocytes seen in controls was absent from Osx1Cre.Efnb2(Δ/Δ) neonates. This suggests that Osx1Cre-expressing cells, including hypertrophic chondrocytes, are dependent on ephrin B2 for their production of cartilage-degrading enzymes, including ADAMTS4, and this might be required for attachment of osteoclasts and osteoblasts to the cartilage surface during endochondral ossification.
[Mh] Termos MeSH primário: Cartilagem/patologia
Condrócitos/metabolismo
Efrina-B2/metabolismo
Osteoclastos/patologia
Osteogênese
[Mh] Termos MeSH secundário: Proteínas ADAM/metabolismo
Proteína ADAMTS4
Animais
Animais Recém-Nascidos
Cartilagem/metabolismo
Adesão Celular
Diferenciação Celular
Condrócitos/patologia
Feminino
Regulação da Expressão Gênica
Imuno-Histoquímica
Integrases/metabolismo
Camundongos Endogâmicos C57BL
Modelos Biológicos
Tamanho do Órgão
Osteoblastos/patologia
Osteoclastos/metabolismo
Osteoclastos/ultraestrutura
Osteogênese/genética
Osteopetrose/genética
Osteopetrose/patologia
Fenótipo
Pró-Colágeno N-Endopeptidase/metabolismo
Tíbia/metabolismo
Tíbia/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ephrin-B2); EC 2.7.7.- (Cre recombinase); EC 2.7.7.- (Integrases); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.14 (Procollagen N-Endopeptidase); EC 3.4.24.82 (ADAMTS4 Protein); EC 3.4.24.82 (Adamts4 protein, mouse)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160113
[St] Status:MEDLINE
[do] DOI:10.1242/dev.125625



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