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Pesquisa : D12.776.543.750.705.408.530 [Categoria DeCS]
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[PMID]:28297759
[Au] Autor:Yu X; Zhang QQ; Wang B; Sun L
[Ad] Endereço:Department of Pathology, Dalian Medical University, Dalian 116044, China.
[Ti] Título:[Expression and significance of integrin α5ß1 and fibronectin in atherosclerotic plaques from autopsy specimens].
[So] Source:Zhonghua Bing Li Xue Za Zhi;46(3):182-186, 2017 Mar 08.
[Is] ISSN:0529-5807
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To investigate the expression of integrin α5ß1 and fibronectin in the human aorta and coronary artery, and their effects in the development of atherosclerosis. One hundred and twenty autopsy aorta and coronary artery specimens were collected, and the expression of CD68, actin, integrin α5ß1 and fibronectin was detected by immunohistochemical staining. Atherosclerotic plaques were located by CD68 and actin staining, and the degree of coronary artery stenosis was determined by elastic fiber staining and NIH Scion Image(60.1) software. The coronary artery tissues were divided into groups A (0-25%); B (26%-50%); C (51%-75%) and D (76%-100%) according to the degree of stenosis. Integrin α5ß1 showed cytoplasmic expression in endothelium, foam cells, monocytes, smooth muscle cells and adjacent tissue around calcification. In both the aorta and coronary artery, integrin α5ß1 expression was stronger in the smooth muscle cells in the internal elastic lamina than in the tunica. The expression intensity in coronary artery smooth muscle decreased with increasing degree of coronary artery stenosis. Fibronectin showed cytoplasmic expression in foam cells, monocytes, smooth muscle cells of the internal elastic lamina and adjacent tissue around calcification. There was positive correlation of fibronectin and integrin α5ß1 expression in smooth muscle cells and adjacent tissue around calcification. In the development of atherosclerosis, integrin α5ß1 and fibronectin may participate in the regulating the migration of smooth muscle cells to the intima, and promote the formation of local calcification of atherosclerotic plaques. But integrin α5ß1 is not involved in the late stage of atherosclerosis with increasing coronary artery stenosis.
[Mh] Termos MeSH primário: Aorta/patologia
Vasos Coronários/patologia
Fibronectinas/metabolismo
Integrina alfa5beta1/metabolismo
Músculo Liso Vascular/metabolismo
Placa Aterosclerótica/patologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Aorta/metabolismo
Autopsia
Constrição Patológica
Vasos Coronários/metabolismo
Endotélio Vascular
Seres Humanos
Imuno-Histoquímica
Músculo Liso Vascular/patologia
Receptores de Fibronectina/metabolismo
Túnica Íntima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (FN1 protein, human); 0 (Fibronectins); 0 (Integrin alpha5beta1); 0 (Receptors, Fibronectin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.0529-5807.2017.03.008


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[PMID]:25081983
[Au] Autor:Hemmati M; Seghatoleslam A; Rasti M; Ebadat S; Naghibalhossaini F; Mostafavi-Pour Z
[Ad] Endereço:Recombinant Protein Laboratory, School of Advanced Medical Sciences and Technologies, Department of Biochemistry, Shiraz University of Medical Sciences, Shiraz, Islamic Republic of Iran; Department of Biochemistry, School of Medicine, Birjand University of Medical Sciences, Birjand, Islamic Republic
[Ti] Título:Additive effect of recombinant Mycobacterium tuberculosis ESAT-6 protein and ESAT-6/CFP-10 fusion protein in adhesion of macrophages through fibronectin receptors.
[So] Source:J Microbiol Immunol Infect;49(2):249-56, 2016 Apr.
[Is] ISSN:1995-9133
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/PURPOSE: Tuberculous granulomas are the sites of interaction between the T cells, macrophages, and extracellular matrix (ECM) to control the infection caused by Mycobacterium tuberculosis (M. tuberculosis). A predominant role of RD-1-encoded secretory proteins, early secreted antigenic target-6 (ESAT-6), and culture filtrate protein-10 (CFP-10) in the formation of granulomas has recently been emphasized. However, the precise molecular events that induce the formation of these granulomatous structures are yet to be elucidated. Macrophages use integrins to adhere to fibronectin (FN) as a major component of the ECM. The major goal of this study was to investigate whether recombinant M. tuberculosis antigens can modulate integrin-mediated macrophage adhesion. METHODS: Differentiated THP-1 cell line was stimulated with recombinant ESAT-6, CFP-10, and ESAT-6/CFP-10 proteins and evaluated for alterations in the expression levels of α5ß1 and α4ß1 by semiquantitative real-time polymerase chain reaction. The role of these recombinant antigens in the cytoskeleton rearrangement was determined by adhesion assay and immunofluorescent microscopy. RESULTS: Our data showed that ESAT-6 and ESAT-6/CFP-10 fusion proteins could induce adhesion of macrophages to FN through α4ß1 integrin. An increased expression level of α4ß1 integrin in comparison with α5ß1 integrin in differentiated THP-1 cells was also observed. Results of immunofluorescence studies showed that recombinant proteins-treated THP-1 cells form well-organized stress fibers and focal contacts containing vinculin compared with untreated THP-1 cells. CONCLUSION: Increased expression level of α4ß1 in differentiated THP-1 cells could suggest the important role of α4ß1 integrin in adhesion and focal contact formation of macrophages exposed to M. tuberculosis antigens.
[Mh] Termos MeSH primário: Antígenos de Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Fibronectinas/metabolismo
Interações Hospedeiro-Patógeno
Macrófagos/metabolismo
Mycobacterium tuberculosis/fisiologia
Receptores de Fibronectina/análise
[Mh] Termos MeSH secundário: Antígenos de Bactérias/genética
Proteínas de Bactérias/genética
Linhagem Celular
Perfilação da Expressão Gênica
Seres Humanos
Integrina alfa4beta1/análise
Integrina alfa4beta1/genética
Integrina alfa5beta1/análise
Integrina alfa5beta1/genética
Mycobacterium tuberculosis/genética
Ligação Proteica
Receptores de Fibronectina/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (CFP-10 protein, Mycobacterium tuberculosis); 0 (ESAT-6 protein, Mycobacterium tuberculosis); 0 (Fibronectins); 0 (Integrin alpha4beta1); 0 (Integrin alpha5beta1); 0 (Receptors, Fibronectin); 0 (Recombinant Proteins)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140802
[St] Status:MEDLINE


  3 / 1335 MEDLINE  
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[PMID]:23517131
[Au] Autor:Moyes KW; Sip CG; Obenza W; Yang E; Horst C; Welikson RE; Hauschka SD; Folch A; Laflamme MA
[Ad] Endereço:Institute for Stem Cell and Regenerative Medicine, University of Washington, Seattle, WA 98109, USA.
[Ti] Título:Human embryonic stem cell-derived cardiomyocytes migrate in response to gradients of fibronectin and Wnt5a.
[So] Source:Stem Cells Dev;22(16):2315-25, 2013 Aug 15.
[Is] ISSN:1557-8534
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An improved understanding of the factors that regulate the migration of human embryonic stem cell-derived cardiomyocytes (hESC-CMs) would provide new insights into human heart development and suggest novel strategies to improve their electromechanical integration after intracardiac transplantation. Since nothing has been reported as to the factors controlling hESC-CM migration, we hypothesized that hESC-CMs would migrate in response to the extracellular matrix and soluble signaling molecules previously implicated in heart morphogenesis. To test this, we screened candidate factors by transwell assay for effects on hESC-CM motility, followed by validation via live-cell imaging and/or gap-closure assays. Fibronectin (FN) elicited a haptotactic response from hESC-CMs, with cells seeded on a steep FN gradient showing nearly a fivefold greater migratory activity than cells on uniform FN. Studies with neutralizing antibodies indicated that adhesion and migration on FN are mediated by integrins α-5 and α-V. Next, we screened 10 soluble candidate factors by transwell assay and found that the noncanonical Wnt, Wnt5a, elicited an approximately twofold increase in migration over controls. This effect was confirmed using the gap-closure assay, in which Wnt5a-treated hESC-CMs showed approximately twofold greater closure than untreated cells. Studies with microfluidic-generated Wnt5a gradients showed that this factor was chemoattractive as well as chemokinetic, and Wnt5a-mediated responses were inhibited by the Frizzled-1/2 receptor antagonist, UM206. In summary, hESC-CMs show robust promigratory responses to FN and Wnt5a, findings that have implications on both cardiac development and cell-based therapies.
[Mh] Termos MeSH primário: Células-Tronco Embrionárias/citologia
Matriz Extracelular/efeitos dos fármacos
Fibronectinas/farmacologia
Miócitos Cardíacos/efeitos dos fármacos
Proteínas Proto-Oncogênicas/farmacologia
Proteínas Wnt/farmacologia
[Mh] Termos MeSH secundário: Anticorpos Neutralizantes/farmacologia
Adesão Celular
Diferenciação Celular
Movimento Celular/efeitos dos fármacos
Cultura em Câmaras de Difusão
Células-Tronco Embrionárias/metabolismo
Matriz Extracelular/genética
Matriz Extracelular/metabolismo
Fibronectinas/genética
Fibronectinas/metabolismo
Expressão Gênica
Seres Humanos
Imagem Molecular
Miócitos Cardíacos/citologia
Miócitos Cardíacos/metabolismo
Proteínas Proto-Oncogênicas/genética
Proteínas Proto-Oncogênicas/metabolismo
Receptores de Fibronectina/antagonistas & inibidores
Receptores de Fibronectina/genética
Receptores de Fibronectina/metabolismo
Transdução de Sinais
Proteínas Wnt/genética
Proteínas Wnt/metabolismo
Proteína Wnt-5a
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Fibronectins); 0 (Proto-Oncogene Proteins); 0 (Receptors, Fibronectin); 0 (WNT5A protein, human); 0 (Wnt Proteins); 0 (Wnt-5a Protein)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130323
[St] Status:MEDLINE
[do] DOI:10.1089/scd.2012.0586


  4 / 1335 MEDLINE  
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[PMID]:23027776
[Au] Autor:Russo E; Salzano M; Postiglione L; Guerra A; Marotta V; Vitale M
[Ad] Endereço:Department of Cellular and Molecular Biology and Pathology, Federico II University, Naples, Italy.
[Ti] Título:Interferon-γ inhibits integrin-mediated extracellular signal-regulated kinase activation stimulated by fibronectin binding in thyroid cells.
[So] Source:J Endocrinol Invest;36(6):375-8, 2013 Jun.
[Is] ISSN:1720-8386
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:Hashimoto's thyroiditis (HT) is an autoimmune disorder characterized by the presence of specific antibodies and by a lymphocytic infiltration of the thyroid secreting inflammatory cytokines. Macrophages, lymphocytes, and cytokines play a pivotal role in both development and progression of Th1-mediated autoimmune diseases, and a direct role in the destruction of thyroid follicles and follicular cell function in autoimmune thyroiditis. Integrins are integral membrane receptors involved in cell-extra-cellular matrix (ECM) interaction with both structural and signaling functions. The integrin- ECM interaction is necessary for the correct function and survival of thyroid follicular cells. The purpose of this study was to determine the effect of cytokine stimulation on integrin expression and signaling in the thyroid cell. Primary cultures from normal thyroids were treated with interferon-γ (IFN-γ), INF-α, tumor necrosis factor-α, interleukin 1a or these cytokines all together. Integrin expression, cell adhesion to fibronectin (FN) and FN-stimulated extracellular signal-regulated kinase (ERK) phosphorylation were determined after cytokine treatment. IFN-γ and IFN-α were the most effective, reducing the expression of the integrin αvß3 and slightly increasing the α3ß1. Cell treatment with IFN-γ strongly impaired cell adhesion to FN. At the same time, the treatment with IFN-γ dramatically inhibited the stimulation of ERK phosphorylation induced by cell adhesion to FN. In conclusion, IFN-γ inhibits the expression of the integrin αvß3, reducing the cell adhesion to FN and the following intracellular signaling in thyroid cells in culture. These results suggest that integrins may be a target of the infiltrating lymphocytes and have a role in the pathogenesis of autoimmune thyroiditis.
[Mh] Termos MeSH primário: MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Fibronectinas/metabolismo
Integrinas/fisiologia
Interferon gama/farmacologia
Glândula Tireoide/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adesão Celular/efeitos dos fármacos
Citocinas/farmacologia
Regulação para Baixo/efeitos dos fármacos
Ativação Enzimática/efeitos dos fármacos
Fibronectinas/farmacologia
Fibronectinas/fisiologia
Seres Humanos
Integrinas/metabolismo
Fosforilação/efeitos dos fármacos
Ligação Proteica/efeitos dos fármacos
Ligação Proteica/fisiologia
Receptores de Fibronectina/metabolismo
Glândula Tireoide/citologia
Glândula Tireoide/metabolismo
Glândula Tireoide/fisiologia
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytokines); 0 (Fibronectins); 0 (Integrins); 0 (Receptors, Fibronectin); 82115-62-6 (Interferon-gamma); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121003
[St] Status:MEDLINE
[do] DOI:10.3275/8649


  5 / 1335 MEDLINE  
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[PMID]:22265966
[Au] Autor:Labat-Robert J
[Ad] Endereço:Laboratoire de recherche ophtalmologique, université Paris-V, hôpital Hôtel-Dieu, 1, place du Parvis-Notre-Dame, 75181 Paris cedex 04, France. lrobert5@wanadoo.fr
[Ti] Título:Cell-Matrix interactions, the role of fibronectin and integrins. A survey.
[So] Source:Pathol Biol (Paris);60(1):15-9, 2012 Feb.
[Is] ISSN:1768-3114
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:In this review, we present several aspects of cell-matrix interactions, especially the role of fibronectin and integrins in the mediation of these interactions. As this field of investigations literally exploded over the last decades, we had to limit this review to some aspects of this field. We cited experiments giving details on the modifications of fibronectin molecules during their interactions with cells as well as on recent progress of the molecular mechanisms of fibronectin-integrin interactions. We insisted on the molecular details which were shown to play a role in the bi-directional signals "sent" by cells to the surrounding matrix (inside-out and outside-in). A number of recent publications confirmed the physiopathological importance of these messages both for the normal function of tissues as well as for the understanding of their pathological modifications. We insist also on the importance of fibronectin-fragments during some pathologies.
[Mh] Termos MeSH primário: Comunicação Celular/fisiologia
Matriz Extracelular/fisiologia
Fibronectinas/fisiologia
Integrinas/fisiologia
[Mh] Termos MeSH secundário: Animais
Coleta de Dados
Matriz Extracelular/metabolismo
Fibronectinas/sangue
Fibronectinas/genética
Fibronectinas/metabolismo
Seres Humanos
Integrinas/genética
Integrinas/metabolismo
Fenômenos Fisiológicos da Nutrição
Receptores de Fibronectina/genética
Receptores de Fibronectina/metabolismo
Receptores de Fibronectina/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Fibronectins); 0 (Integrins); 0 (Receptors, Fibronectin)
[Em] Mês de entrada:1206
[Cu] Atualização por classe:120213
[Lr] Data última revisão:
120213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120124
[St] Status:MEDLINE
[do] DOI:10.1016/j.patbio.2011.10.003


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[PMID]:21567080
[Au] Autor:DE Wever O; Sobczak-Thépot J; Vercoutter-Edouart AS; Michalski JC; Ouelaa-Benslama R; Stupack DG; Bracke M; Wang JYJ; Gespach C; Emami S
[Ad] Endereço:Laboratory of Experimental Cancerology, Ghent University Hospital, Ghent, Belgium.
[Ti] Título:Priming and potentiation of DNA damage response by fibronectin in human colon cancer cells and tumor-derived myofibroblasts.
[So] Source:Int J Oncol;39(2):393-400, 2011 Aug.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:We have previously shown that the genotoxin-induced apoptosis in mouse embryo fibroblasts was enhanced by the extracellular matrix protein fibronectin (FN). In the present study, we tested the hypothesis that FN regulates the DNA damage response (DDR) signaling pathways in HCT116 (p53-wt) and HT29 (p53-mut) human colon cancer cells and tumor-derived myofibroblasts. DNA damage recognition mechanisms were analyzed by immunofluorescence staining, cell cycle analysis and immunoblotting addressed at specific molecular sensors and executors involved in the DDR pathways. The results show that FN, but not collagen type IV or Matrigel, initiates and potentiates the DDR to the anticancer drug cisplatin in an α5 integrin and cell cycle-dependent manner (S and G2/M phases) in human colon cancer cells. Accordingly, we demonstrate that adhesion of HCT116 cells to FN upregulated the expression of α5 integrin FN receptors at the cell surface. These FN-induced DDR pathways include the concerted phosphorylation of histone H2AX on Ser139 detected as nuclear foci (γ-H2AX, 15 and 25 kDa forms), of ataxia telangiectasia mutated (ATM-Ser1981), checkpoint kinase 2 (CHK2-Thr68, 62 and 67 kDa) and p53-Ser15. These FN-induced γ-H2AX signals were interrupted or attenuated by selective inhibitors acting on the DDR pathway kinases, including wortmannin (targeting the phosphatidylinositol-3-kinase-related protein kinases, PIKK), KU55933 (ATM), NU7026 (DNA-dependent protein kinase catalytic subunit, DNA-PK-cs) and SP600125 (JNK2, stress activated protein kinase/c-Jun N-terminal kinase-2). Adhesion to FN also potentiated the γ-H2AX signals and the cytotoxic effects of cisplatin in human colon tumor-derived myofibroblasts. These data provide evidence that FN promotes DNA damage recognition and chemosensitization to cisplatin via the potentiation of the DNA damage signaling responses in human colon cancer cells and tumor-derived myofibroblasts.
[Mh] Termos MeSH primário: Neoplasias do Colo/genética
Neoplasias do Colo/metabolismo
Dano ao DNA/efeitos dos fármacos
Dano ao DNA/genética
Fibronectinas/metabolismo
Fibronectinas/farmacologia
Miofibroblastos/metabolismo
[Mh] Termos MeSH secundário: Adesão Celular/efeitos dos fármacos
Ciclo Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Quinase do Ponto de Checagem 2
Cisplatino/farmacologia
Reagentes para Ligações Cruzadas/farmacologia
Células HCT116
Células HT29
Histonas/metabolismo
Seres Humanos
Miofibroblastos/patologia
Fosforilação/efeitos dos fármacos
Proteínas Serina-Treonina Quinases/metabolismo
Receptores de Fibronectina/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (Fibronectins); 0 (H2AFX protein, human); 0 (Histones); 0 (Receptors, Fibronectin); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.11.1 (CHEK2 protein, human); EC 2.7.11.1 (Chek2 protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1110
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110514
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2011.1034


  7 / 1335 MEDLINE  
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[PMID]:21113146
[Au] Autor:Sanchez-Ruderisch H; Detjen KM; Welzel M; André S; Fischer C; Gabius HJ; Rosewicz S
[Ad] Endereço:Medizinische Klinik m.S. Hepatologie und Gastroenterologie, Charité-Universitätsmedizin Berlin, Campus Virchow-Klinikum, Berlin, Germany.
[Ti] Título:Galectin-1 sensitizes carcinoma cells to anoikis via the fibronectin receptor α5ß1-integrin.
[So] Source:Cell Death Differ;18(5):806-16, 2011 May.
[Is] ISSN:1476-5403
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Anoikis resistance is a hallmark of transformed epithelial cells. Here, we show that treatment of anoikis-resistant carcinoma cell lines with the endogenous lectin galectin-1 (Gal-1) promoted apoptosis via interaction with the unligated fibronectin receptor α(5)ß(1)-integrin. Gal-1 efficiency correlated with expression of α(5)ß(1)-integrin, and transfection of the α(5)-subunit into deficient cell lines conferred Gal-1 binding and anoikis stimulation. Furthermore, Gal-1 and the α(5)- and ß(1)-integrin subunits co-precipitated in Gal-1-stimulated cells undergoing anoikis. Other members of the galectin family failed to be active. The functional interaction between Gal-1 and α(5)ß(1)-integrin was glycan dependent with α2,6-sialylation representing a switch-off signal. Desialylation of cell surface glycans resulted in increased electrophoretic mobility of α(5)ß(1)-integrin and facilitated Gal-1 binding and anoikis stimulation. On the level of signaling, Gal-1-stimulated anoikis was prevented by filipin, which impaired the internalization of α(5)ß(1)-integrin via cholesterol-enriched microdomains, and by pretreatment with a caspase-8 inhibitor. We propose that Gal-1/α(5)ß(1)-integrin interaction participates in the control of epithelial integrity and integrin sialylation may enable carcinoma cells to evade this Gal-1-dependent control mechanism.
[Mh] Termos MeSH primário: Anoikis
Caspase 8/metabolismo
Galectina 1/fisiologia
Integrina alfa5beta1/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Adesão Celular
Linhagem Celular Tumoral
Galectina 1/farmacologia
Galectinas/farmacologia
Seres Humanos
Imunoprecipitação
Microdomínios da Membrana/efeitos dos fármacos
Microdomínios da Membrana/metabolismo
Neoplasias/patologia
Neuraminidase/metabolismo
Oligossacarídeos/metabolismo
Ligação Proteica
Receptores de Fibronectina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Galectin 1); 0 (Galectins); 0 (Integrin alpha5beta1); 0 (LGALS1 protein, human); 0 (Oligosaccharides); 0 (Receptors, Fibronectin); 0 (sialooligosaccharides); EC 3.2.1.18 (Neuraminidase); EC 3.4.22.- (Caspase 8)
[Em] Mês de entrada:1109
[Cu] Atualização por classe:150205
[Lr] Data última revisão:
150205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101130
[St] Status:MEDLINE
[do] DOI:10.1038/cdd.2010.148


  8 / 1335 MEDLINE  
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[PMID]:20570943
[Au] Autor:van der Flier A; Badu-Nkansah K; Whittaker CA; Crowley D; Bronson RT; Lacy-Hulbert A; Hynes RO
[Ad] Endereço:Howard Hughes Medical Institute, Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
[Ti] Título:Endothelial alpha5 and alphav integrins cooperate in remodeling of the vasculature during development.
[So] Source:Development;137(14):2439-49, 2010 Jul.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Integrin cell adhesion receptors and fibronectin, one of their extracellular matrix ligands, have been demonstrated to be important for angiogenesis using functional perturbation studies and complete knockout mouse models. Here, we report on the roles of the alpha5 and alphav integrins, which are the major endothelial fibronectin receptors, in developmental angiogenesis. We generated an integrin alpha5-floxed mouse line and ablated alpha5 integrin in endothelial cells. Unexpectedly, endothelial-specific knockout of integrin alpha5 has no obvious effect on developmental angiogenesis. We provide evidence for genetic interaction between mutations in integrin alpha5 and alphav and for overlapping functions and compensation between these integrins and perhaps others. Nonetheless, in embryos lacking both alpha5 and alphav integrins in their endothelial cells, initial vasculogenesis and angiogenesis proceed normally, at least up to E11.5, including the formation of apparently normal embryonic vasculature and development of the branchial arches. However, in the absence of endothelial alpha5 and alphav integrins, but not of either alone, there are extensive defects in remodeling of the great vessels and heart resulting in death at ~E14.5. We also found that fibronectin assembly is somewhat affected in integrin alpha5 knockout endothelial cells and markedly reduced in integrin alpha5/alphav double-knockout endothelial cell lines. Therefore, neither alpha5 nor alphav integrins are required in endothelial cells for initial vasculogenesis and angiogenesis, although they are required for remodeling of the heart and great vessels. These integrins on other cells, and/or other integrins on endothelial cells, might contribute to fibronectin assembly and vascular development.
[Mh] Termos MeSH primário: Integrina alfa5/metabolismo
Integrina alfa5/fisiologia
Integrina alfaV/metabolismo
Integrina alfaV/fisiologia
Integrinas/fisiologia
[Mh] Termos MeSH secundário: Animais
Vasos Sanguíneos/metabolismo
Adesão Celular
Diferenciação Celular
Linhagem Celular
Endotélio/metabolismo
Matriz Extracelular/metabolismo
Fibronectinas/metabolismo
Fibronectinas/fisiologia
Integrinas/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Óxido Nítrico Sintase Tipo III
Receptores de Fibronectina/metabolismo
Receptores de Fibronectina/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fibronectins); 0 (Integrin alpha5); 0 (Integrin alphaV); 0 (Integrins); 0 (Receptors, Fibronectin); EC 1.14.13.39 (NOS3 protein, human); EC 1.14.13.39 (Nitric Oxide Synthase Type III)
[Em] Mês de entrada:1007
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100624
[St] Status:MEDLINE
[do] DOI:10.1242/dev.049551


  9 / 1335 MEDLINE  
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[PMID]:20505078
[Au] Autor:Messmer-Blust AF; Balasubramanian S; Gorbacheva VY; Jeyaratnam JA; Vestal DJ
[Ad] Endereço:Department of Biological Sciences, University of Toledo, Toledo, OH 43606, USA.
[Ti] Título:The interferon-gamma-induced murine guanylate-binding protein-2 inhibits rac activation during cell spreading on fibronectin and after platelet-derived growth factor treatment: role for phosphatidylinositol 3-kinase.
[So] Source:Mol Biol Cell;21(14):2514-28, 2010 Jul 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exposure of cells to certain cytokines can alter how these same cells respond to later cues from other agents, such as extracellular matrix or growth factors. Interferon (IFN)-gamma pre-exposure inhibits the spreading of fibroblasts on fibronectin. Expression of the IFN-gamma-induced GTPase murine guanylate-binding protein-2 (mGBP-2) can phenocopy this inhibition and small interfering RNA knockdown of mGBP-2 prevents IFN-gamma-mediated inhibition of cell spreading. Either IFN-gamma treatment or mGBP-2 expression inhibits Rac activation during cell spreading. Rac is required for cell spreading. mGBP-2 also inhibits the activation of Akt during cell spreading on fibronectin. mGBP-2 is incorporated into a protein complex containing the catalytic subunit of phosphatidylinositol 3-kinase (PI3-K), p110. The association of mGBP-2 with p110 seems important for the inhibition of cell spreading because S52N mGBP-2, which does not incorporate into the protein complex with p110, is unable to inhibit cell spreading. PI3-K activation during cell spreading on fibronectin was inhibited in the presence of mGBP-2. Both IFN-gamma and mGBP-2 also inhibit cell spreading initiated by platelet-derived growth factor treatment, which is also accompanied by inhibition of Rac activation by mGBP-2. This is the first report of a novel mechanism by which IFN-gamma can alter how cells respond to subsequent extracellular signals, by the induction of mGBP-2.
[Mh] Termos MeSH primário: Movimento Celular/efeitos dos fármacos
Fibronectinas/farmacologia
Proteínas de Ligação ao GTP/metabolismo
Interferon gama/farmacologia
Fosfatidilinositol 3-Quinases/metabolismo
Fator de Crescimento Derivado de Plaquetas/farmacologia
Proteínas rac de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos/genética
Animais
Adesão Celular/efeitos dos fármacos
Linhagem Celular
Ativação Enzimática/efeitos dos fármacos
Fibroblastos/citologia
Fibroblastos/efeitos dos fármacos
Fibroblastos/enzimologia
Seres Humanos
Integrina alfa4/metabolismo
Melanoma/patologia
Camundongos
Proteínas Proto-Oncogênicas c-akt/metabolismo
RNA Interferente Pequeno/metabolismo
Receptores de Fibronectina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fibronectins); 0 (Platelet-Derived Growth Factor); 0 (RNA, Small Interfering); 0 (Receptors, Fibronectin); 143198-26-9 (Integrin alpha4); 82115-62-6 (Interferon-gamma); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.1.- (Gbp2 protein, mouse); EC 3.6.5.2 (rac GTP-Binding Proteins)
[Em] Mês de entrada:1010
[Cu] Atualização por classe:141203
[Lr] Data última revisão:
141203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100528
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E09-04-0344


  10 / 1335 MEDLINE  
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[PMID]:19892014
[Au] Autor:Smith JA; Samayawardhena LA; Craig AW
[Ad] Endereço:Queen's University Cancer Research Institute, Division of Cancer Biology and Genetics, Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6.
[Ti] Título:Fps/Fes protein-tyrosine kinase regulates mast cell adhesion and migration downstream of Kit and beta1 integrin receptors.
[So] Source:Cell Signal;22(3):427-36, 2010 Mar.
[Is] ISSN:1873-3913
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Activation of Kit receptor protein-tyrosine kinase (PTK) by its ligand Stem Cell Factor (SCF) is required for the development of mast cells, and for the regulation of mast cell proliferation, migration and modulation of inflammatory mediator release. Recent studies have implicated the non-receptor PTK Fps/Fes (hereafter referred to as Fes) in signaling downstream of oncogenic Kit, however, the potential role of Fes in regulating Kit signaling is not well defined. In this study, we show that SCF induces transient tyrosine phosphorylation of wild-type Fes as well as kinase-dead Fes in bone marrow-derived mast cells (BMMCs). The latter finding implicates an upstream kinase acting on Fes, which we identified as Fyn PTK. SCF treatment of BMMCs promoted recruitment of Fes to Kit, potentially via direct interaction of the Fes SH2 domain with phosphorylated Kit. While Fes was not required for SCF-induced signaling to Akt and Erk kinases, Fes-deficient (fes-/-) BMMCs displayed a defect in sustained p38 kinase activation, compared to control cells. SCF-treated Fes-deficient BMMCs also displayed elevated beta1 integrin-mediated cell adhesion and spreading on fibronectin, compared to control cells, and a reduction in cell polarization at later times of SCF treatment. Restoring Fes expression in fes-/- BMMCs by retroviral transduction was sufficient to rescue cell spreading and polarization defects. Interestingly, SCF-induced chemotaxis of BMMCs was also defective in Fes-deficient BMMCs, and restored in Fes-rescue BMMCs. Overall, these results implicate Fes in regulating cross-talk between Kit and beta1 integrins to promote cytoskeletal reorganization and motility of mast cells.
[Mh] Termos MeSH primário: Integrina beta1/metabolismo
Mastócitos/enzimologia
Proteínas Proto-Oncogênicas c-fes/metabolismo
Proteínas Proto-Oncogênicas c-kit/metabolismo
Receptores de Fibronectina/metabolismo
[Mh] Termos MeSH secundário: Animais
Adesão Celular
Movimento Celular
Células Cultivadas
Integrina alfa5beta1/metabolismo
Mastócitos/citologia
Mastócitos/imunologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Proto-Oncogênicas c-fes/deficiência
Proteínas Proto-Oncogênicas c-fes/genética
Fator de Células-Tronco/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
Domínios de Homologia de src
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Integrin alpha5beta1); 0 (Integrin beta1); 0 (Receptors, Fibronectin); 0 (Stem Cell Factor); EC 2.7.10.1 (Proto-Oncogene Proteins c-kit); EC 2.7.10.2 (Fes protein, mouse); EC 2.7.10.2 (Proto-Oncogene Proteins c-fes); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1003
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091107
[St] Status:MEDLINE
[do] DOI:10.1016/j.cellsig.2009.10.014



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