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[PMID]:27770562
[Au] Autor:Wang C; Tong X; Jiang X; Yang F
[Ad] Endereço:Department of Bioengineering, Stanford University, Stanford, California, 94305.
[Ti] Título:Effect of matrix metalloproteinase-mediated matrix degradation on glioblastoma cell behavior in 3D PEG-based hydrogels.
[So] Source:J Biomed Mater Res A;105(3):770-778, 2017 03.
[Is] ISSN:1552-4965
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glioblastoma (GBM) is the most common and aggressive form of primary brain tumor with median survival of 12 months. To improve clinical outcomes, it is critical to develop in vitro models that support GBM proliferation and invasion for deciphering tumor progression and screening drug candidates. A key hallmark of GBM cells is their extreme invasiveness, a process mediated by matrix metalloproteinase (MMP)-mediated degradation of the extracellular matrix. We recently reported the development of a MMP-degradable, poly(ethylene-glycol)-based hydrogel platform for culturing GBM cells. In the present study, we modulated the percentage of MMP-degradable crosslinks in 3D hydrogels to analyze the effects of MMP-degradability on GBM fates. Using an immortalized GBM cell line (U87) as a model cell type, our results showed that MMP-degradability was not required for supporting GBM proliferation. All hydrogel formulations supported robust GBM proliferation, up to 10 fold after 14 days. However, MMP-degradability was essential for facilitating tumor spreading, and 50% MMP-degradable hydrogels were sufficient to enable both robust tumor cell proliferation and spreading in 3D. The findings of this study highlight the importance of modulating MMP-degradability in engineering 3D in vitro brain cancer models and may be applied for engineering in vitro models for other cancer types. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 105A: 770-778, 2017.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/metabolismo
Matriz Extracelular/química
Glioblastoma/metabolismo
Hidrogéis/química
Polietilenoglicóis/química
[Mh] Termos MeSH secundário: Neoplasias Encefálicas/patologia
Linhagem Celular Tumoral
Gelatinases
Glioblastoma/patologia
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Hydrogels); 30IQX730WE (Polyethylene Glycols); EC 3.4.24.- (Gelatinases); U076Q6Q621 (polyethylene glycol 1000)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1002/jbm.a.35947


  2 / 3176 MEDLINE  
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[PMID]:29304073
[Au] Autor:Saito J; Yokoyama U; Nicho N; Zheng YW; Ichikawa Y; Ito S; Umemura M; Fujita T; Ito S; Taniguchi H; Asou T; Masuda M; Ishikawa Y
[Ad] Endereço:Cardiovascular Research Institute, Yokohama City University, Yokohama, Japan.
[Ti] Título:Tissue-type plasminogen activator contributes to remodeling of the rat ductus arteriosus.
[So] Source:PLoS One;13(1):e0190871, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIMS: The ductus arteriosus (DA) closes after birth to adapt to the robust changes in hemodynamics, which require intimal thickening (IT) to occur. The smooth muscle cells of the DA have been reported to play important roles in IT formation. However, the roles of the endothelial cells (ECs) have not been fully investigated. We herein focused on tissue-type plasminogen activator (t-PA), which is a DA EC dominant gene, and investigated its contribution to IT formation in the DA. METHODS AND RESULTS: ECs from the DA and aorta were isolated from fetal rats using fluorescence-activated cell sorting. RT-PCR showed that the t-PA mRNA expression level was 2.7-fold higher in DA ECs than in aortic ECs from full-term rat fetuses (gestational day 21). A strong immunoreaction for t-PA was detected in pre-term and full-term rat DA ECs. t-PA-mediated plasminogen-plasmin conversion activates gelatinase matrix metalloproteinases (MMPs). Gelatin zymography revealed that plasminogen supplementation significantly promoted activation of the elastolytic enzyme MMP-2 in rat DA ECs. In situ zymography demonstrated that marked gelatinase activity was observed at the site of disruption in the internal elastic laminae (IEL) in full-term rat DA. In a three-dimensional vascular model, EC-mediated plasminogen-plasmin conversion augmented the IEL disruption. In vivo administration of plasminogen to pre-term rat fetuses (gestational day 19), in which IT is poorly formed, promoted IEL disruption accompanied by gelatinase activation and enhanced IT formation in the DA. Additionally, experiments using five human DA tissues demonstrated that the t-PA expression level was 3.7-fold higher in the IT area than in the tunica media. t-PA protein expression and gelatinase activity were also detected in the IT area of the human DAs. CONCLUSION: t-PA expressed in ECs may help to form IT of the DA via activation of MMP-2 and disruption of IEL.
[Mh] Termos MeSH primário: Canal Arterial/patologia
Ativador de Plasminogênio Tecidual/fisiologia
[Mh] Termos MeSH secundário: Animais
Canal Arterial/enzimologia
Células Endoteliais/metabolismo
Feminino
Gelatinases/metabolismo
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Metaloproteinases da Matriz/metabolismo
Plasminogênio/administração & dosagem
Gravidez
Interferência de RNA
Ratos
Ratos Wistar
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Ativador de Plasminogênio Tecidual/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9001-91-6 (Plasminogen); EC 3.4.21.68 (Tissue Plasminogen Activator); EC 3.4.24.- (Gelatinases); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190871


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[PMID]:29025374
[Au] Autor:Park H; Lee Y; Lee H; Kim JW; Hwang JH; Kim J; Yoon YS; Han HS; Kim H
[Ad] Endereço:1 Department of Pathology, Seoul National University Hospital, Seoul National University College of Medicine, Seoul, Korea.
[Ti] Título:The prognostic significance of cancer-associated fibroblasts in pancreatic ductal adenocarcinoma.
[So] Source:Tumour Biol;39(10):1010428317718403, 2017 Oct.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cancer-associated fibroblasts are abundant in the desmoplastic stroma of pancreatic ductal adenocarcinomas and are considered to play important roles in tumor progression. In this study, we investigated the expression status of secreted protein acidic and rich in cysteine, periostin, fibroblast-activated protein, and the newly developed proCOL11A1 antibody in the stroma of surgically resected pancreatic ductal adenocarcinomas and their prognostic implications. Tissue microarrays were constructed from 155 surgically resected pancreatic ductal adenocarcinomas and paired non-neoplastic pancreata and from another independent set of 48 normal/benign pancreata, and immunohistochemical stains were performed for proCOL11A1, fibroblast-activated protein, secreted protein acidic and rich in cysteine, and periostin. The immunohistochemical stain results were correlated with clinicopathological features and survival data. proCOL11A1, fibroblast-activated protein, secreted protein acidic and rich in cysteine, and periostin expression was significantly increased in the intratumoral stroma of pancreatic ductal adenocarcinomas compared to paired non-neoplastic pancreata (proCOL11A1: 145/155 (93.5%) vs 26/154 (16.9%); fibroblast-activated protein: 139/143 (97.2%) vs 82/132 (62.1%); secreted protein acidic and rich in cysteine: 113/150 (75.3%) vs 49/132 (37.1%); periostin: 135/151 (89.4%) vs 45/135 (33.3%); p < 0.001, all). While the four markers were expressed at lower levels in normal/benign pancreata, there were no significant differences in the expression frequencies among normal pancreas, acute pancreatitis, and chronic pancreatitis. Interestingly, on survival analysis, low intratumoral fibroblast-activated protein cancer-associated fibroblast counts (<100/high-power field) were associated with a significantly reduced overall survival compared to those with high fibroblast-activated protein cancer-associated fibroblast counts (p = 0.010; hazard ratio 5.2 (95% confidence interval 1.3-21.3)). Similar patterns were seen for proCOL11A and secreted protein acidic and rich in cysteine and overall and disease-free survival, although not statistically significant. In conclusion, we demonstrate that the presence of cancer-associated fibroblasts in the tumor stroma may not always be associated with a poor prognosis as suggested in many studies; on the contrary, it may even be associated with prolonged survival, supporting the recent experimental findings that tumor stroma may have a protective role rather than enhance aggressive behavior.
[Mh] Termos MeSH primário: Adenocarcinoma/genética
Carcinoma Ductal Pancreático/genética
Moléculas de Adesão Celular/biossíntese
Colágeno Tipo XI/biossíntese
Gelatinases/biossíntese
Proteínas de Membrana/biossíntese
Osteonectina/biossíntese
Serina Endopeptidases/biossíntese
[Mh] Termos MeSH secundário: Adenocarcinoma/patologia
Adenocarcinoma/cirurgia
Adulto
Idoso
Biomarcadores Tumorais/biossíntese
Biomarcadores Tumorais/genética
Fibroblastos Associados a Câncer/metabolismo
Fibroblastos Associados a Câncer/patologia
Carcinoma Ductal Pancreático/patologia
Carcinoma Ductal Pancreático/cirurgia
Moléculas de Adesão Celular/genética
Colágeno Tipo XI/genética
Intervalo Livre de Doença
Feminino
Gelatinases/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Masculino
Proteínas de Membrana/genética
Meia-Idade
Osteonectina/genética
Prognóstico
Serina Endopeptidases/genética
Análise Serial de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (COL11A1 protein, human); 0 (Cell Adhesion Molecules); 0 (Collagen Type XI); 0 (Membrane Proteins); 0 (Osteonectin); 0 (POSTN protein, human); 0 (SPARC protein, human); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (fibroblast activation protein alpha); EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317718403


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[PMID]:28906407
[Au] Autor:Lo Presti R; Hopps E; Caimi G
[Ad] Endereço:aDipartimento di Scienze Psicologiche, Pedagogiche e della Formazione bDipartimento Biomedico di Medicina Interna e Specialistica Università degli Studi di Palermo, Palermo, Italy.
[Ti] Título:Gelatinases and physical exercise: A systematic review of evidence from human studies.
[So] Source:Medicine (Baltimore);96(37):e8072, 2017 Sep.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Matrix metalloproteinases (MMPs), particularly gelatinase A (MMP-2) and gelatinase B (MMP-9), as well as their tissue inhibitors (TIMP-1 and TIMP-2), are involved in the development of skeletal muscle tissue, in the repair process after muscle injury and in the adaptive modifications induced by physical exercise in skeletal muscle. This paper aims at reviewing results from human studies that investigated the role of gelatinases and their inhibitors in skeletal muscle response to acute physical exercise or training. METHODS: Electronic databases PubMed/MEDLINE, Scopus and Web of Science were searched for papers published between January 2000 and February 2017. The papers were eligible when reporting human studies in which MMP-2 and/or MMP-9 and/or the inhibitors TIMP-1/TIMP-2 were evaluated, in blood or muscular tissue, before and after acute physical exercise or before and after a period of structured physical training. We included studies on healthy subjects and patients with chronic metabolic diseases (obesity, diabetes mellitus, metabolic syndrome-MS) or asymptomatic coronary artery disease. We excluded studies on patients with neurological, rheumatologic or neoplastic diseases. RESULTS: Studies conducted on muscle biopsies showed an early stimulation of MMP-9 gene transcription as a result of acute exercise, whereas MMP-2 and TIMP transcription resulted from regular repetition of exercise over time. Studies on serum or plasma level of gelatinases and their inhibitors showed an early release of MMP-9 after acute exercise of sufficient intensity, while data on MMP-2 and TIMP were more contrasting. Most of the studies dealing with the effect of training indicated a trend toward reduction in blood gelatinase levels, once again more clear for MMP-9. This result was related to an anti-inflammatory effect of regular exercise and was more evident when training consisted of aerobic activities. This study has limitations: as the initial selection was done through titles and abstracts, incomplete retrieval cannot be excluded, as well as we cannot exclude bias due to selective reporting within studies. CONCLUSION: A better knowledge of the molecular events activated by different types of acute exercise and regular training could be of great relevance in order to maximize the benefits of physical activity in healthy subjects and patients.
[Mh] Termos MeSH primário: Exercício/fisiologia
Gelatinases/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
Músculo Esquelético/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000008072


  5 / 3176 MEDLINE  
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[PMID]:28846068
[Au] Autor:Chen M; Lei X; Shi C; Huang M; Li X; Wu B; Li Z; Han W; Du B; Hu J; Nie Q; Mai W; Ma N; Xu N; Zhang X; Fan C; Hong A; Xia M; Luo L; Ma A; Li H; Yu Q; Chen H; Zhang D; Ye W
[Ad] Endereço:College of Pharmacy, and.
[Ti] Título:Pericyte-targeting prodrug overcomes tumor resistance to vascular disrupting agents.
[So] Source:J Clin Invest;127(10):3689-3701, 2017 Oct 02.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Blood vessels in the tumor periphery have high pericyte coverage and are resistant to vascular disrupting agents (VDAs). VDA treatment resistance leads to a viable peripheral tumor rim that contributes to treatment failure and disease recurrence. Here, we provide evidence to support a hypothesis that shifting the target of VDAs from tumor vessel endothelial cells to pericytes disrupts tumor peripheral vessels and the viable rim, circumventing VDA treatment resistance. Through chemical engineering, we developed Z-GP-DAVLBH (from the tubulin-binding VDA desacetylvinblastine monohydrazide [DAVLBH]) as a prodrug that can be selectively activated by fibroblast activation protein α (FAPα) in tumor pericytes. Z-GP-DAVLBH selectively destroys the cytoskeleton of FAPα-expressing tumor pericytes, disrupting blood vessels both within the core and around the periphery of tumors. As a result, Z-GP-DAVLBH treatment eradicated the otherwise VDA-resistant tumor rim and led to complete regression of tumors in multiple lines of xenografts without producing the drug-related toxicity that is associated with similar doses of DAVLBH. This study demonstrates that targeting tumor pericytes with an FAPα-activated VDA prodrug represents a potential vascular disruption strategy in overcoming tumor resistance to VDA treatments.
[Mh] Termos MeSH primário: Inibidores da Angiogênese/farmacologia
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Neoplasias/irrigação sanguínea
Neoplasias/tratamento farmacológico
Neovascularização Patológica/tratamento farmacológico
Pró-Fármacos/farmacologia
Vimblastina
[Mh] Termos MeSH secundário: Células A549
Animais
Células 3T3 BALB
Gelatinases/biossíntese
Células HeLa
Células Hep G2
Seres Humanos
Proteínas de Membrana/biossíntese
Camundongos
Neoplasias/metabolismo
Neoplasias/patologia
Neovascularização Patológica/metabolismo
Neovascularização Patológica/patologia
Pericitos
Serina Endopeptidases/biossíntese
Vimblastina/análogos & derivados
Vimblastina/farmacologia
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Angiogenesis Inhibitors); 0 (Membrane Proteins); 0 (Prodrugs); 5V9KLZ54CY (Vinblastine); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (fibroblast activation protein alpha); EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


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[PMID]:28829211
[Au] Autor:Juillerat-Jeanneret L; Tafelmeyer P; Golshayan D
[Ad] Endereço:a Transplantation Center and Transplantation Immunopathology Laboratory, Department of Medicine , Centre Hospitalier Universitaire Vaudois (CHUV) and University of Lausanne (UNIL) , Lausanne , Switzerland.
[Ti] Título:Fibroblast activation protein-α in fibrogenic disorders and cancer: more than a prolyl-specific peptidase?
[So] Source:Expert Opin Ther Targets;21(10):977-991, 2017 Oct.
[Is] ISSN:1744-7631
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Fibroblast activation protein-α (FAP-α) belongs to the family of prolyl-specific serine proteases. FAP-α displays both exopeptidase and endopeptidase/gelatinase/collagenase activities. FAP-α protein and/or activity have been associated with fibrosis, inflammation and cancer, but the protein is undetectable in most normal tissues. FAP-α is selectively expressed at sites of tissue remodeling and repair and enhances tumor progression, suggesting that this protease may be a therapeutic target to treat human disorders associated with fibrotic dysregulation. Areas covered: In this review, we summarize the mechanisms driving tissue fibrosis and describe some of the enzymes involved in fibrosis, concentrating on FAP-α. We describe its enzymatic properties, discuss the tools developed to control its activity and the problem of selectivity toward the other proteases of the family and outline its potential biological substrates. We also consider non-enzymatic functions of this protein and suggest that repression of FAP-α expression may represent therapeutic options. Expert opinion: Questions remain regarding the biological functions of FAP-α, either dependent or independent of its enzyme activity. However, as progress is underway to develop FAP-α-specific inhibitors and therapeutic antibodies, its role in diseases associated with fibrosis is starting to emerge, ultimately leading to novel therapeutic options for inflammatory and oncologic diseases.
[Mh] Termos MeSH primário: Desenho de Drogas
Gelatinases/metabolismo
Proteínas de Membrana/metabolismo
Neoplasias/patologia
Serina Endopeptidases/metabolismo
[Mh] Termos MeSH secundário: Animais
Progressão da Doença
Fibroblastos/metabolismo
Fibrose/tratamento farmacológico
Fibrose/patologia
Gelatinases/antagonistas & inibidores
Gelatinases/genética
Regulação da Expressão Gênica
Seres Humanos
Proteínas de Membrana/antagonistas & inibidores
Proteínas de Membrana/genética
Terapia de Alvo Molecular
Neoplasias/tratamento farmacológico
Serina Endopeptidases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Membrane Proteins); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (fibroblast activation protein alpha); EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1080/14728222.2017.1370455


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[PMID]:28793333
[Au] Autor:Belogortseva N; Krezalek M; Guyton K; Labno C; Poroyko V; Zaborina O; Alverdy JC
[Ad] Endereço:Department of Surgery, University of Chicago, Chicago, Illinois, United States of America.
[Ti] Título:Media from macrophages co-incubated with Enterococcus faecalis induces epithelial cell monolayer reassembly and altered cell morphology.
[So] Source:PLoS One;12(8):e0182825, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Signal exchange between intestinal epithelial cells, microbes and local immune cells is an important mechanism of intestinal homeostasis. Given that intestinal macrophages are in close proximity to both the intestinal epithelium and the microbiota, their pathologic interactions may result in epithelial damage. The present study demonstrates that co-incubation of murine macrophages with E. faecalis strains producing gelatinase (GelE) and serine protease (SprE) leads to resultant condition media (CM) capable of inducing reassembly of primary colonic epithelial cell monolayers. Following the conditioned media (CM) exposure, some epithelial cells are shed whereas adherent cells are observed to undergo dissolution of cell-cell junctions and morphologic transformation with actin cytoskeleton reorganization resulting in flattened and elongated shapes. These cells exhibit marked filamentous filopodia and lamellipodia formation. Cellular reorganization is not observed when epithelial monolayers are exposed to: CM from macrophages co-incubated with E. faecalis GelE/SprE-deficient mutants, CM from macrophages alone, or E. faecalis (GelE/SprE) alone. Flow cytometry analysis reveals increased expression of CD24 and CD44 in cells treated with macrophage/E. faecalis CM. This finding in combination with the appearance colony formation in matrigel demonstrate that the cells treated with macrophage/E. faecalis CM contain a higher proportion progenitor cells compared to untreated control. Taken together, these findings provide evidence for a triangulated molecular dialogue between E. faecalis, macrophages and colonic epithelial cells, which may have important implications for conditions in the gut that involve inflammation, injury or tumorigenesis.
[Mh] Termos MeSH primário: Enterococcus faecalis/metabolismo
Células Epiteliais/citologia
Mucosa Intestinal/citologia
Macrófagos/citologia
[Mh] Termos MeSH secundário: Animais
Antígeno CD24/metabolismo
Linhagem Celular
Forma Celular/fisiologia
Meios de Cultura
Células Epiteliais/metabolismo
Células Epiteliais/microbiologia
Gelatinases/metabolismo
Receptores de Hialuronatos/metabolismo
Mucosa Intestinal/metabolismo
Mucosa Intestinal/microbiologia
Macrófagos/metabolismo
Macrófagos/microbiologia
Camundongos
Serina Endopeptidases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD24 Antigen); 0 (Culture Media); 0 (Hyaluronan Receptors); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182825


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[PMID]:28793332
[Au] Autor:Choi IY; Karpus ON; Turner JD; Hardie D; Marshall JL; de Hair MJH; Maijer KI; Tak PP; Raza K; Hamann J; Buckley CD; Gerlag DM; Filer A
[Ad] Endereço:Division of Clinical Immunology and Rheumatology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
[Ti] Título:Stromal cell markers are differentially expressed in the synovial tissue of patients with early arthritis.
[So] Source:PLoS One;12(8):e0182751, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Previous studies have shown increased expression of stromal markers in synovial tissue (ST) of patients with established rheumatoid arthritis (RA). Here, ST expression of stromal markers in early arthritis in relationship to diagnosis and prognostic outcome was studied. METHODS: ST from 56 patients included in two different early arthritis cohorts and 7 non-inflammatory controls was analysed using immunofluorescence to detect stromal markers CD55, CD248, fibroblast activation protein (FAP) and podoplanin. Diagnostic classification (gout, psoriatic arthritis, unclassified arthritis (UA), parvovirus associated arthritis, reactive arthritis and RA), disease outcome (resolving vs persistent) and clinical variables were determined at baseline and after follow-up, and related to the expression of stromal markers. RESULTS: We observed expression of all stromal markers in ST of early arthritis patients, independent of diagnosis or prognostic outcome. Synovial expression of FAP was significantly higher in patients developing early RA compared to other diagnostic groups and non-inflammatory controls. In RA FAP protein was expressed in both lining and sublining layers. Podoplanin expression was higher in all early inflammatory arthritis patients than controls, but did not differentiate diagnostic outcomes. Stromal marker expression was not associated with prognostic outcomes of disease persistence or resolution. There was no association with clinical or sonographic variables. CONCLUSIONS: Stromal cell markers CD55, CD248, FAP and podoplanin are expressed in ST in the earliest stage of arthritis. Baseline expression of FAP is higher in early synovitis patients who fulfil classification criteria for RA over time. These results suggest that significant fibroblast activation occurs in RA in the early window of disease.
[Mh] Termos MeSH primário: Artrite/metabolismo
Células Estromais/metabolismo
Membrana Sinovial/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Antígenos CD/metabolismo
Antígenos de Neoplasias/metabolismo
Artrite/diagnóstico
Biomarcadores/metabolismo
Antígenos CD55/metabolismo
Progressão da Doença
Feminino
Fibroblastos/metabolismo
Gelatinases/metabolismo
Seres Humanos
Masculino
Glicoproteínas de Membrana/metabolismo
Proteínas de Membrana/metabolismo
Meia-Idade
Prognóstico
Serina Endopeptidases/metabolismo
Sinovite/diagnóstico
Sinovite/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, Neoplasm); 0 (Biomarkers); 0 (CD248 protein, human); 0 (CD55 Antigens); 0 (Membrane Glycoproteins); 0 (Membrane Proteins); 0 (PDPN protein, human); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (fibroblast activation protein alpha); EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182751


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[PMID]:28697174
[Au] Autor:Wäster P; Orfanidis K; Eriksson I; Rosdahl I; Seifert O; Öllinger K
[Ad] Endereço:Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping 58185, Sweden.
[Ti] Título:UV radiation promotes melanoma dissemination mediated by the sequential reaction axis of cathepsins-TGF-ß1-FAP-α.
[So] Source:Br J Cancer;117(4):535-544, 2017 Aug 08.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Ultraviolet radiation (UVR) is the major risk factor for development of malignant melanoma. Fibroblast activation protein (FAP)-α is a serine protease expressed on the surface of activated fibroblasts, promoting tumour invasion through extracellular matrix (ECM) degradation. The signalling mechanism behind the upregulation of FAP-α is not yet completely revealed. METHODS: Expression of FAP-α was analysed after UVR exposure in in vitro co-culture systems, gene expression arrays and artificial skin constructs. Cell migration and invasion was studied in relation to cathepsin activity and secretion of transforming growth factor (TGF)-ß1. RESULTS: Fibroblast activation protein-α expression was induced by UVR in melanocytes of human skin. The FAP-α expression was regulated by UVR-induced release of TGF-ß1 and cathepsin inhibitors prevented such secretion. In melanoma cell culture models and in a xenograft tumour model of zebrafish embryos, FAP-α mediated ECM degradation and facilitated tumour cell dissemination. CONCLUSIONS: Our results provide evidence for a sequential reaction axis from UVR via cathepsins, TGF-ß1 and FAP-α expression, promoting cancer cell dissemination and melanoma metastatic spread.
[Mh] Termos MeSH primário: Catepsinas/metabolismo
Gelatinases/genética
Gelatinases/metabolismo
Melanoma/genética
Melanoma/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Nevo/genética
Serina Endopeptidases/genética
Serina Endopeptidases/metabolismo
Neoplasias Cutâneas/genética
Neoplasias Cutâneas/metabolismo
Fator de Crescimento Transformador beta/secreção
Raios Ultravioleta
[Mh] Termos MeSH secundário: Animais
Catepsinas/genética
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Senescência Celular/genética
Técnicas de Cocultura
Meios de Cultivo Condicionados/farmacologia
Regulação para Baixo
Fibroblastos/efeitos dos fármacos
Gelatinases/efeitos da radiação
Expressão Gênica/efeitos da radiação
Inativação Gênica
Seres Humanos
Queratinócitos
Melanócitos
Proteínas de Membrana/efeitos da radiação
Transplante de Neoplasias
Cultura Primária de Células
Serina Endopeptidases/efeitos da radiação
Transdução de Sinais/efeitos da radiação
Pele/efeitos da radiação
Pele Artificial
Transcriptoma
Fator de Crescimento Transformador beta/antagonistas & inibidores
Fator de Crescimento Transformador beta/genética
Fator de Crescimento Transformador beta/efeitos da radiação
Regulação para Cima
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media, Conditioned); 0 (Membrane Proteins); 0 (Transforming Growth Factor beta); EC 3.4.- (Cathepsins); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (fibroblast activation protein alpha); EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.182


  10 / 3176 MEDLINE  
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[PMID]:28595013
[Au] Autor:Deng LJ; Wang LH; Peng CK; Li YB; Huang MH; Chen MF; Lei XP; Qi M; Cen Y; Ye WC; Zhang DM; Chen WM
[Ad] Endereço:Guangdong Province Key Laboratory of Pharmacodynamic Constituents of TCM and New Drugs Research, College of Pharmacy, Jinan University , Guangzhou 510632, P. R. China.
[Ti] Título:Fibroblast Activation Protein α Activated Tripeptide Bufadienolide Antitumor Prodrug with Reduced Cardiotoxicity.
[So] Source:J Med Chem;60(13):5320-5333, 2017 Jul 13.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bufadienolides are the major pharmacologic constituents of traditional Chinese medicine Chan'su, which is frequently used clinically for cancer treatment in China. Motivated by reducing or avoiding the cardiac toxicity of bufadienolides, we have designed, synthesized, and evaluated the fibroblast activation protein α (FAPα) activated tripeptide arenobufagin prodrugs with the purpose of improving the safety of arenobufagin (a representative bufadienolide). Among these FAPα-activated prodrugs, 3f exhibited the best hydrolytic efficiency by recombinant human FAPα (rhFAPα) and was activated in tumors. The LD of 3f was 6.5-fold higher than that of arenobufagin. We also observed that there are nonapparent changes in echocardiography, pathological section of cardiac muscle, and the lactate dehydrogenase activities (LDH) in 3f-treatment tumor-bearing mice, even when the dose reached 3 times the amount of parent drug arenobufagin that was used. Compound 3f also exhibits significant antitumor activity in vitro and in vivo. The improved safety profile and favorable anticancer properties of 3f warrant further studies of the potential clinical implications. Our study suggests that FAPα prodrug strategy is an effective approach for successful increasing the therapeutic window of bufadienolides.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Bufanolídeos/farmacologia
Cardiotoxicidade/tratamento farmacológico
Gelatinases/metabolismo
Proteínas de Membrana/metabolismo
Oligopeptídeos/farmacologia
Pró-Fármacos/farmacologia
Serina Endopeptidases/metabolismo
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/química
Antineoplásicos/metabolismo
Bufanolídeos/química
Bufanolídeos/metabolismo
Cardiotoxicidade/metabolismo
Cardiotoxicidade/patologia
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Ensaios de Seleção de Medicamentos Antitumorais
Feminino
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Estrutura Molecular
Neoplasias Experimentais/tratamento farmacológico
Neoplasias Experimentais/metabolismo
Neoplasias Experimentais/patologia
Oligopeptídeos/química
Oligopeptídeos/metabolismo
Pró-Fármacos/química
Pró-Fármacos/metabolismo
Proteínas Recombinantes/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Bufanolides); 0 (Membrane Proteins); 0 (Oligopeptides); 0 (Prodrugs); 0 (Recombinant Proteins); 29565-35-3 (bufadienolide); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (fibroblast activation protein alpha); EC 3.4.24.- (Gelatinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.6b01755



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