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[PMID]:28453768
[Au] Autor:Lamb CA; Mansfield JC; Tew GW; Gibbons D; Long AK; Irving P; Diehl L; Eastham-Anderson J; Price MB; O'Boyle G; Jones DEJ; O'Byrne S; Hayday A; Keir ME; Egen JG; Kirby JA
[Ad] Endereço:Institute of Cellular Medicine, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
[Ti] Título:αEß7 Integrin Identifies Subsets of Pro-Inflammatory Colonic CD4+ T Lymphocytes in Ulcerative Colitis.
[So] Source:J Crohns Colitis;11(5):610-620, 2017 May 01.
[Is] ISSN:1876-4479
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Background and Aims: The αEß7 integrin is crucial for retention of T lymphocytes at mucosal surfaces through its interaction with E-cadherin. Pathogenic or protective functions of these cells during human intestinal inflammation, such as ulcerative colitis [UC], have not previously been defined, with understanding largely derived from animal model data. Defining this phenotype in human samples is important for understanding UC pathogenesis and is of translational importance for therapeutic targeting of αEß7-E-cadherin interactions. Methods: αEß7+ and αEß7- colonic T cell localization, inflammatory cytokine production and expression of regulatory T cell-associated markers were evaluated in cohorts of control subjects and patients with active UC by immunohistochemistry, flow cytometry and real-time PCR of FACS-purified cell populations. Results: CD4+αEß7+ T lymphocytes from both healthy controls and UC patients had lower expression of regulatory T cell-associated genes, including FOXP3, IL-10, CTLA-4 and ICOS in comparison with CD4+αEß7- T lymphocytes. In UC, CD4+αEß7+ lymphocytes expressed higher levels of IFNγ and TNFα in comparison with CD4+αEß7- lymphocytes. Additionally the CD4+αEß7+ subset was enriched for Th17 cells and the recently described Th17/Th1 subset co-expressing both IL-17A and IFNγ, both of which were found at higher frequencies in UC compared to control. Conclusion: αEß7 integrin expression on human colonic CD4+ T cells was associated with increased production of pro-inflammatory Th1, Th17 and Th17/Th1 cytokines, with reduced expression of regulatory T cell-associated markers. These data suggest colonic CD4+αEß7+ T cells are pro-inflammatory and may play a role in UC pathobiology.
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos/imunologia
Colite Ulcerativa/imunologia
Colo/citologia
Integrinas/imunologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Estudos de Casos e Controles
Colite Ulcerativa/metabolismo
Colo/imunologia
Citocinas/metabolismo
Feminino
Citometria de Fluxo
Seres Humanos
Masculino
Meia-Idade
Reação em Cadeia da Polimerase em Tempo Real
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Integrins); 0 (integrin alphaEbeta7)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1093/ecco-jcc/jjw189


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[PMID]:28450296
[Au] Autor:Tian H; Ketova T; Hardy D; Xu X; Gao X; Zijlstra A; Blobe GC
[Ad] Endereço:From the Division of Medical Oncology, Department of Medicine (H.T., D.H., G.C.B.) and Department of Pharmacology and Cancer Biology (G.C.B.), Duke University Medical Center, Durham, NC; Department of Pathology, Microbiology, and Immunology (T.K., A.Z.) and Department of Cancer Biology (A.Z.), Vande
[Ti] Título:Endoglin Mediates Vascular Maturation by Promoting Vascular Smooth Muscle Cell Migration and Spreading.
[So] Source:Arterioscler Thromb Vasc Biol;37(6):1115-1126, 2017 Jun.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Endoglin, a transforming growth factor-ß superfamily coreceptor, is predominantly expressed in endothelial cells and has essential roles in vascular development. However, whether endoglin is also expressed in vascular smooth muscle cells (VSMCs), especially in vivo, remains controversial. Furthermore, the roles of endoglin in VSMC biology remain largely unknown. Our objective was to examine the expression and determine the function of endoglin in VSMCs during angiogenesis. APPROACH AND RESULTS: Here, we determine that endoglin is robustly expressed in VSMCs. Using CRISPR/CAS9 knockout and short hairpin RNA knockdown in the VSMC/endothelial coculture model system, we determine that endoglin in VSMCs, but not in endothelial cells, promotes VSMCs recruitment by the endothelial cells both in vitro and in vivo. Using an unbiased bioinformatics analysis of RNA sequencing data and further study, we determine that, mechanistically, endoglin mediates VSMC recruitment by promoting VSMC migration and spreading on endothelial cells via increasing integrin/FAK pathway signaling, whereas endoglin has minimal effects on VSMC adhesion to endothelial cells. In addition, we further determine that loss of endoglin in VSMCs inhibits VSMC recruitment in vivo. CONCLUSIONS: These studies demonstrate that endoglin has an important role in VSMC recruitment and blood vessel maturation during angiogenesis and also provide novel insights into how discordant endoglin function in endothelial and VSMCs may regulate vascular maturation and angiogenesis.
[Mh] Termos MeSH primário: Movimento Celular
Forma Celular
Endoglina/metabolismo
Músculo Liso Vascular/metabolismo
Miócitos de Músculo Liso/metabolismo
[Mh] Termos MeSH secundário: Animais
Sistemas CRISPR-Cas
Células Cultivadas
Técnicas de Cocultura
Endoglina/genética
Células Endoteliais/metabolismo
Quinase 1 de Adesão Focal/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Integrinas/metabolismo
Camundongos Endogâmicos C57BL
Fenótipo
Interferência de RNA
Transdução de Sinais
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ENG protein, human); 0 (Endoglin); 0 (Eng protein, mouse); 0 (Integrins); EC 2.7.10.2 (Focal Adhesion Kinase 1); EC 2.7.10.2 (PTK2 protein, human); EC 2.7.10.2 (Ptk2 protein, mouse)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.116.308859


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[PMID]:28459388
[Au] Autor:Gomez JC; Doerschuk CM
[Ad] Endereço:1 Marsico Lung Institute, Division of Pulmonary Diseases and Critical Care Medicine University of North Carolina Chapel Hill, North Carolina.
[Ti] Título:Activating Integrins Isn't Always "Beta" for Neutrophil Migration!
[So] Source:Am J Respir Cell Mol Biol;56(5):561-562, 2017 05.
[Is] ISSN:1535-4989
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Integrinas/imunologia
Pulmão/imunologia
Macrófagos Alveolares/imunologia
Infiltração de Neutrófilos/imunologia
Pneumonia Bacteriana/imunologia
Infecções por Pseudomonas/imunologia
Pseudomonas aeruginosa/imunologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Pulmão/patologia
Macrófagos Alveolares/patologia
Pneumonia Bacteriana/patologia
Infecções por Pseudomonas/patologia
[Pt] Tipo de publicação:EDITORIAL; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Integrins)
[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:170502
[St] Status:MEDLINE
[do] DOI:10.1165/rcmb.2017-0066ED


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[PMID]:27777142
[Au] Autor:Fløisand Y; Lundin KEA; Lazarevic V; Kristiansen JD; Osnes LTN; Tjønnfjord GE; Reims HM; Gedde-Dahl T
[Ad] Endereço:Department of Hematology, Oslo University Hospital, Rikshospitalet, Oslo, Norway. Electronic address: yfl70@me.com.
[Ti] Título:Targeting Integrin α4ß7 in Steroid-Refractory Intestinal Graft-versus-Host Disease.
[So] Source:Biol Blood Marrow Transplant;23(1):172-175, 2017 Jan.
[Is] ISSN:1523-6536
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Steroid refractory acute graft-versus-host-disease of the gut is a serious complication associated with high mortality after allogeneic stem cell transplantation. Treatment options are limited and not predictably effective. We describe the treatment of steroid-refractory acute graft-versus-host-disease with vedolizumab, an antibody directed against integrin α4ß7, in 6 patients. All patients responded, and 4 of 6 patients are alive with a median follow-up of 10 months.
[Mh] Termos MeSH primário: Anticorpos Monoclonais Humanizados/uso terapêutico
Doença Enxerto-Hospedeiro/tratamento farmacológico
Integrinas/efeitos dos fármacos
Enteropatias/tratamento farmacológico
[Mh] Termos MeSH secundário: Adulto
Feminino
Fármacos Gastrointestinais/uso terapêutico
Doença Enxerto-Hospedeiro/patologia
Transplante de Células-Tronco Hematopoéticas/efeitos adversos
Seres Humanos
Masculino
Meia-Idade
Terapia de Salvação/métodos
Esteroides/uso terapêutico
Transplante Homólogo
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Humanized); 0 (Gastrointestinal Agents); 0 (Integrins); 0 (Steroids); 0 (integrin alpha4beta7); 9RV78Q2002 (vedolizumab)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  5 / 14188 MEDLINE  
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[PMID]:29284478
[Au] Autor:Petpiroon N; Sritularak B; Chanvorachote P
[Ad] Endereço:Cell-Based Drug and Health Product Development Research Unit, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.
[Ti] Título:Phoyunnanin E inhibits migration of non-small cell lung cancer cells via suppression of epithelial-to-mesenchymal transition and integrin αv and integrin ß3.
[So] Source:BMC Complement Altern Med;17(1):553, 2017 Dec 29.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The conversion of the epithelial phenotype of cancer cells into cells with a mesenchymal phenotype-so-called epithelial-mesenchymal transition (EMT)-has been shown to enhance the capacity of the cells to disseminate throughout the body. EMT is therefore becoming a potential target for anti-cancer drug discovery. Here, we showed that phoyunnanin E, a compound isolated from Dendrobium venustum, possesses anti-migration activity and addressed its mechanism of action. METHODS: The cytotoxic and proliferative effects of phoyunnanin E on human non-small cell lung cancer-derived H460, H292, and A549 cells and human keratinocyte HaCaT cells were investigated by MTT assay. The effect of phoyunnanin E on EMT was evaluated by determining the colony formation and EMT markers. The migration and invasion of H460, H292, A549 and HaCaT cells was evaluated by wound healing assay and transwell invasion assay, respectively. EMT markers, integrins and migration-associated proteins were examined by western blot analysis. RESULTS: Phoyunnanin E at the concentrations of 5 and 10 µM, which are non-toxic to H460, H292, A549 and HaCaT cells showed good potential to inhibit the migratory activity of three types of human lung cancer cells. The anti-migration effect of phoyunnanin E was shown to relate to the suppressed EMT phenotypes, including growth in anchorage-independent condition, cell motility, and EMT-specific protein markers (N-cadherin, vimentin, slug, and snail). In addition to EMT suppression, we found that phoyunnanin E treatment with 5 and 10 µM could decrease the cellular level of integrin αv and integrin ß3, these integrins are frequently up-regulated in highly metastatic tumor cells. We further characterized the regulatory proteins in cell migration and found that the cells treated with phoyunnanin E exhibited a significantly lower level of phosphorylated focal adhesion kinase (p-FAK) and phosphorylated ATP-dependent tyrosine kinase (p-AKT), and their downstream effectors (including Ras-related C3 botulinum (Rac-GTP); Cell division cycle 42 (Cdc42); and Ras homolog gene family, member A (Rho-GTP)) in comparison to those of the non-treated control. CONCLUSIONS: We have determined for the first time that phoyunnanin E could inhibit the motility of lung cancer cells via the suppression of EMT and metastasis-related integrins. This new information could support further development of this compound for anti-metastasis approaches.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/tratamento farmacológico
Movimento Celular/efeitos dos fármacos
Transição Epitelial-Mesenquimal/efeitos dos fármacos
Integrinas/metabolismo
Neoplasias Pulmonares/tratamento farmacológico
Fenantrenos/farmacologia
Extratos Vegetais/farmacologia
[Mh] Termos MeSH secundário: Células A549
Carcinoma Pulmonar de Células não Pequenas/patologia
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Dendrobium/química
Seres Humanos
Neoplasias Pulmonares/patologia
Fenantrenos/química
Extratos Vegetais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrins); 0 (Phenanthrenes); 0 (Plant Extracts); 0 (phoyunnanin E)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-2059-7


  6 / 14188 MEDLINE  
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[PMID]:28743718
[Au] Autor:Stritt S; Beck S; Becker IC; Vögtle T; Hakala M; Heinze KG; Du X; Bender M; Braun A; Lappalainen P; Nieswandt B
[Ad] Endereço:Institute of Experimental Biomedicine I, University Hospital and.
[Ti] Título:Twinfilin 2a regulates platelet reactivity and turnover in mice.
[So] Source:Blood;130(15):1746-1756, 2017 10 12.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulated reorganization of the actin cytoskeleton is a prerequisite for proper platelet production and function. Consequently, defects in proteins controlling actin dynamics have been associated with platelet disorders in humans and mice. Twinfilin 2a (Twf2a) is a small actin-binding protein that inhibits actin filament assembly by sequestering actin monomers and capping filament barbed ends. Moreover, Twf2a binds heterodimeric capping proteins, but the role of this interaction in cytoskeletal dynamics has remained elusive. Even though Twf2a has pronounced effects on actin dynamics in vitro, only little is known about its function in vivo. Here, we report that constitutive Twf2a-deficient mice ( ) display mild macrothrombocytopenia due to a markedly accelerated platelet clearance in the spleen. platelets showed enhanced integrin activation and α-granule release in response to stimulation of (hem) immunoreceptor tyrosine-based activation motif (ITAM) and G-protein-coupled receptors, increased adhesion and aggregate formation on collagen I under flow, and accelerated clot retraction and spreading on fibrinogen. In vivo, Twf2a deficiency resulted in shortened tail bleeding times and faster occlusive arterial thrombus formation. The hyperreactivity of platelets was attributed to enhanced actin dynamics, characterized by an increased activity of n-cofilin and profilin 1, leading to a thickened cortical cytoskeleton and hence sustained integrin activation by limiting calpain-mediated integrin inactivation. In summary, our results reveal the first in vivo functions of mammalian Twf2a and demonstrate that Twf2a-controlled actin rearrangements dampen platelet activation responses in a n-cofilin- and profilin 1-dependent manner, thereby indirectly regulating platelet reactivity and half-life in mice.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Proteínas dos Microfilamentos/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Animais
Apoptose
Artérias/patologia
Integrinas/metabolismo
Camundongos
Trombocitopenia/metabolismo
Trombocitopenia/patologia
Trombose/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Integrins); 0 (Microfilament Proteins); 0 (TWF2 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-02-770768


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[PMID]:29261670
[Au] Autor:Jeffery HC; McDowell P; Lutz P; Wawman RE; Roberts S; Bagnall C; Birtwistle J; Adams DH; Oo YH
[Ad] Endereço:Centre for Liver Research and National Institute for Health Research Birmingham Biomedical Research Centre, Institute of Immunology and Immunotherapy, University of Birmingham, Birmingham, United Kingdom.
[Ti] Título:Human intrahepatic ILC2 are IL-13positive amphiregulinpositive and their frequency correlates with model of end stage liver disease score.
[So] Source:PLoS One;12(12):e0188649, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Innate lymphoid cells (ILC) have been implicated in the initiation of inflammation and fibrosis in mice. However, ILC have not been characterized in inflamed human liver tissue. METHODS: Human intrahepatic lymphocytes were isolated by mechanical digestion and phenotyped by flow cytometry. Conditioned medium from cultures of primary human biliary epithelial cells, stellate cells, fibroblasts and inflamed human liver tissue was used to model the effects of the inflammatory liver environment of ILC phenotype and function. RESULTS: All three ILC subsets were present in the human liver, with the ILC1 (CRTH2negCD117neg) subset constituting around 70% of intrahepatic ILCs. Both NCRpos (NKp44+) and NCRneg ILC3 (CRTH2negCD117pos) subsets were also detected. ILC2 (CRTH2pos) frequency correlated with disease severity measured by model of end stage liver disease (MELD) scoring leading us to study this subset in more detail. ILC2 displayed a tissue resident CD69+ CD161++ phenotype and expressed chemokine receptor CCR6 allowing them to respond to CCL20 secreted by cholangiocytes and stellate cells. ILC2 expressed integrins VLA-5 and VLA-6 and the IL-2 and IL-7 cytokine receptors CD25 and CD127 although IL-2 and IL-7 were barely detectable in inflamed liver tissue. Although biliary epithelial cells secrete IL-33, intrahepatic ILC2 had low expression of the ST2 receptor. Intrahepatic ILC2 secreted the immunoregulatory and repair cytokines IL-13 and amphiregulin. CONCLUSIONS: Intrahepatic ILC2 express receptors allowing them to be recruited to bile ducts in inflamed portal tracts. Their frequencies increased with worsening liver function. Their secretion of IL-13 and amphiregulin suggests they may be recruited to promote resolution and repair and thereby they may contribute to ongoing fibrogenesis in liver disease.
[Mh] Termos MeSH primário: Anfirregulina/metabolismo
Doença Hepática Terminal/imunologia
Imunidade Inata
Interleucina-13/metabolismo
Fígado/metabolismo
Linfócitos/metabolismo
Modelos Biológicos
[Mh] Termos MeSH secundário: Células Epiteliais/metabolismo
Seres Humanos
Inflamação/patologia
Integrinas/genética
Integrinas/metabolismo
Interleucina-2/metabolismo
Subunidade alfa de Receptor de Interleucina-2/metabolismo
Interleucina-7/metabolismo
Fígado/patologia
Contagem de Linfócitos
Subfamília B de Receptores Semelhantes a Lectina de Células NK/metabolismo
Fenótipo
Receptores de Quimiocinas/genética
Receptores de Quimiocinas/metabolismo
Receptores Imunológicos/metabolismo
Receptores de Prostaglandina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphiregulin); 0 (Integrins); 0 (Interleukin-13); 0 (Interleukin-2); 0 (Interleukin-2 Receptor alpha Subunit); 0 (Interleukin-7); 0 (NK Cell Lectin-Like Receptor Subfamily B); 0 (Receptors, Chemokine); 0 (Receptors, Immunologic); 0 (Receptors, Prostaglandin); 0 (prostaglandin D2 receptor)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188649


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[PMID]:29190039
[Au] Autor:Uotila L; Savinko T; Guenther C; Fagerholm S
[Ti] Título:Blood cell integrins and diseases.
[So] Source:Duodecim;132(20):1865-73, 2016.
[Is] ISSN:0012-7183
[Cp] País de publicação:Finland
[La] Idioma:eng
[Ab] Resumo:Integrins are adhesion molecules on the surface of cells. In blood cells they are responsible for rapid changes during adhesion of the cell to the endothelium. Deficiency or defective function of integrins will result in severe illnesses. Surprisingly, certain variants of integrins are associated with an increased risk of developing SLE. In autoimmune diseases and as a result of organ transplantations integrins participate in reactions in which leukocytes attack the body's own tissues. This has resulted in the development of drugs in antibody form for inhibition of the action of integrins. These drugs may, however, exhibit severe adverse effects.
[Mh] Termos MeSH primário: Doenças Autoimunes/sangue
Moléculas de Adesão Celular/sangue
Integrinas/sangue
[Mh] Termos MeSH secundário: Adesão Celular
Endotélio Vascular
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Integrins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE


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[PMID]:29277769
[Au] Autor:Lee C; Ramos DM
[Ad] Endereço:Department of Orofacial Sciences, University of California at San Francisco, San Francisco, CA, U.S.A.
[Ti] Título:αvß6-Fyn Kinase Promotes Epithelial Phenotype in SYF Cells.
[So] Source:Anticancer Res;38(1):165-168, 2018 01.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:The 5-year survival rate for patients with oral cancer remains at 50%, in large part due the high rate of post-treatment recurrence. In this study, we transfected epithelial-specific integrin αvß6 and Fyn-kinase, a member of the Src-family kinases, into embryonic murine fibroblasts. In oral cancer, expression of αvß6 is neo-expressed. Using a variety of in vitro assays, including cell migration and multicellular spheroid formation, we determined that these embryonic fibroblasts expressing αvß6 and Fyn-kinase were able to acquire an epithelial phenotype. This is in direct contrast to human oral SCC, where expression of αvß6 with Fyn-kinase promotes epithelial to mesenchymal transition. This demonstrates that signaling pathways can be species-specific.
[Mh] Termos MeSH primário: Antígenos de Neoplasias/genética
Células Epiteliais/citologia
Transição Epitelial-Mesenquimal
Fibroblastos/citologia
Integrinas/genética
Proteínas Proto-Oncogênicas c-fyn/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Movimento Celular
Células Epiteliais/metabolismo
Fibroblastos/metabolismo
Camundongos
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Neoplasm); 0 (Integrins); 0 (integrin alphavbeta6); EC 2.7.10.2 (Fyn protein, mouse); EC 2.7.10.2 (Proto-Oncogene Proteins c-fyn); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


  10 / 14188 MEDLINE  
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[PMID]:28448919
[Au] Autor:Yu J; Huang J; Jansen JA; Xiong C; Walboomers XF
[Ad] Endereço:Center for BioMed-X Research, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, PR China; Department of Biomaterials, Radboud University Medical Center, Nijmegen, The Netherlands.
[Ti] Título:Mechanochemical mechanism of integrin clustering modulated by nanoscale ligand spacing and rigidity of extracellular substrates.
[So] Source:J Mech Behav Biomed Mater;72:29-37, 2017 Aug.
[Is] ISSN:1878-0180
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Experimental findings indicate that cell function and behavior such as cell growth, division, migration and differentiation, are subtly regulated via integrin-dependent cell adhesion. Cell adhesion is influenced by nanoscale ligand spacing and rigidity of extracellular substrates, as cell adhesion drops greatly when the ligand spacing is larger than ~60nm, and cell adhesion is stronger on stiff than soft substrates. However, how nanoscale ligand spacing and substrate stiffness jointly affect integrin clustering and hence nascent cell adhesion remains to be elucidated. To quantitatively investigate the phenomena and the underlying mechanochemical mechanism of integrin clustering modulated by ligand spacing and substrate stiffness, we introduced Monte Carlo simulations varying the values of ligand spacing and substrate stiffness. Moreover, the effects of integrin number, integrin binding free energy, integrin association free energy, and local ligand spacing were investigated. The simulation results showed that integrin clustering decreased sharply, when ligand spacing was relatively large such as d >60nm in the current simulations, regardless of substrate rigidities, though with close spacing, the clustering increased with the substrate stiffness. The investigation contributes to the goals of understanding and predicting experimental phenomena, directing and optimizing biomaterial design, and manipulating integrin-dependent cell-substrate adhesion in tissue engineering.
[Mh] Termos MeSH primário: Adesão Celular
Integrinas/química
[Mh] Termos MeSH secundário: Ligantes
Fenômenos Mecânicos
Modelos Biológicos
Método de Monte Carlo
Ligação Proteica
Engenharia Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrins); 0 (Ligands)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE



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