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Pesquisa : D12.776.395.550.200.537.750 [Categoria DeCS]
Referências encontradas : 18 [refinar]
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  1 / 18 MEDLINE  
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[PMID]:29028806
[Au] Autor:Fukuhara T; Kim J; Hokaiwado S; Nawa M; Okamoto H; Kogiso T; Watabe T; Hattori N
[Ad] Endereço:Department of Neurology, Juntendo University School of Medicine, Bunkyo-ku, Tokyo, Japan.
[Ti] Título:A novel immunotoxin reveals a new role for CD321 in endothelial cells.
[So] Source:PLoS One;12(10):e0181502, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There are currently several antibody therapies that directly target tumors, and antibody-drug conjugates represent a novel moiety as next generation therapeutics. Here, we used a unique screening probe, DT3C, to identify functional antibodies that recognized surface molecules and functional epitopes, and which provided toxin delivery capability. Accordingly, we generated the 90G4 antibody, which induced DT3C-dependent cytotoxicity in endothelial cells. Molecular analysis revealed that 90G4 recognized CD321, a protein localized at tight junctions. Although CD321 plays a pivotal role in inflammation and lymphocyte trans-endothelial migration, little is known about its mechanism of action in endothelial cells. Targeting of CD321 by the 90G4 immunotoxin induced cell death. Moreover, 90G4 immunotoxin caused cytotoxicity primarily in migratory endothelial cells, but not in those forming sheets, suggesting a critical role for CD321 in tumor angiogenesis. We also found that hypoxia triggered redistribution of CD321 to a punctate localization on the basal side of cells, resulting in functional impairment of tight junctions and increased motility. Thus, our findings raise the intriguing possibility that endothelial CD321 presented cellular localization in tight junction as well as multifunctional dynamics in several conditions, leading to illuminate the importance of widely-expressed CD321 as a potential target for antitumor therapy.
[Mh] Termos MeSH primário: Células Endoteliais/efeitos dos fármacos
Células Endoteliais/metabolismo
Imunotoxinas/toxicidade
Molécula A de Adesão Juncional/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Morte Celular/efeitos dos fármacos
Linhagem Celular
Movimento Celular/efeitos dos fármacos
Células Endoteliais/citologia
Seres Humanos
Imunotoxinas/imunologia
Molécula A de Adesão Juncional/química
Molécula A de Adesão Juncional/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunotoxins); 0 (Junctional Adhesion Molecule A)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181502


  2 / 18 MEDLINE  
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[PMID]:28069576
[Au] Autor:Ciccia F; Guggino G; Rizzo A; Alessandro R; Luchetti MM; Milling S; Saieva L; Cypers H; Stampone T; Di Benedetto P; Gabrielli A; Fasano A; Elewaut D; Triolo G
[Ad] Endereço:Dipartimento Biomedico di Medicina Interna e Specialistica, Sezione di Reumatologia, University of Palermo, Palermo, Italy.
[Ti] Título:Dysbiosis and zonulin upregulation alter gut epithelial and vascular barriers in patients with ankylosing spondylitis.
[So] Source:Ann Rheum Dis;76(6):1123-1132, 2017 Jun.
[Is] ISSN:1468-2060
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Dysbiosis has been recently demonstrated in patients with ankylosing spondylitis (AS) but its implications in the modulation of intestinal immune responses have never been studied. The aim of this study was to investigate the role of ileal bacteria in modulating local and systemic immune responses in AS. METHODS: Ileal biopsies were obtained from 50 HLA-B27 patients with AS and 20 normal subjects. Silver stain was used to visualise bacteria. Ileal expression of tight and adherens junction proteins was investigated by TaqMan real-time (RT)-PCR and immunohistochemistry. Serum levels of lipopolysaccharide (LPS), LPS-binding protein (LPS-BP), intestinal fatty acid-BP (iFABP) and zonulin were assayed by ELISA. Monocyte immunological functions were studied in in vitro experiments. In addition the effects of antibiotics on tight junctions in human leukocyte antigen (HLA)-B27 transgenic (TG) rats were assessed. RESULTS: Adherent and invasive bacteria were observed in the gut of patients with AS with the bacterial scores significantly correlated with gut inflammation. Impairment of the gut vascular barrier (GVB) was also present in AS, accompanied by significant upregulation of zonulin, and associated with high serum levels of LPS, LPS-BP, iFABP and zonulin. In in vitro studies zonulin altered endothelial tight junctions while its epithelial release was modulated by isolated AS ileal bacteria. AS circulating monocytes displayed an anergic phenotype partially restored by ex vivo stimulation with LPS+sCD14 and their stimulation with recombinant zonulin induced a clear M2 phenotype. Antibiotics restored tight junction function in HLA-B27 TG rats. CONCLUSIONS: Bacterial ileitis, increased zonulin expression and damaged intestinal mucosal barrier and GVB, characterises the gut of patients with AS and are associated with increased blood levels of zonulin, and bacterial products. Bacterial products and zonulin influence monocyte behaviour.
[Mh] Termos MeSH primário: Toxina da Cólera/sangue
Disbiose/imunologia
Endotélio/metabolismo
Ileíte/imunologia
Mucosa Intestinal/imunologia
Mucosa Intestinal/metabolismo
Espondilite Anquilosante/imunologia
[Mh] Termos MeSH secundário: Doença Aguda
Proteínas da Fase Aguda
Junções Aderentes/genética
Animais
Antibacterianos/farmacologia
Antígenos CD/genética
Bactérias/isolamento & purificação
Células CACO-2
Caderinas/genética
Proteínas de Transporte/sangue
Proteínas de Transporte/genética
Estudos de Casos e Controles
Toxina da Cólera/genética
Doença Crônica
Disbiose/microbiologia
Proteínas de Ligação a Ácido Graxo/sangue
Expressão Gênica
Antígeno HLA-B27/genética
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Ileíte/sangue
Íleo/imunologia
Íleo/microbiologia
Interleucina-8
Mucosa Intestinal/microbiologia
Molécula A de Adesão Juncional/genética
Lipopolissacarídeos/sangue
Glicoproteínas de Membrana/sangue
Proteínas de Membrana/genética
Monócitos/imunologia
Permeabilidade
RNA Mensageiro/metabolismo
Ratos
Ratos Transgênicos
Junções Íntimas/efeitos dos fármacos
Junções Íntimas/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acute-Phase Proteins); 0 (Anti-Bacterial Agents); 0 (Antigens, CD); 0 (Cadherins); 0 (Carrier Proteins); 0 (Fatty Acid-Binding Proteins); 0 (HLA-B27 Antigen); 0 (Interleukin-8); 0 (Junctional Adhesion Molecule A); 0 (Lipopolysaccharides); 0 (Membrane Glycoproteins); 0 (Membrane Proteins); 0 (PLVAP protein, human); 0 (RNA, Messenger); 0 (cadherin 5); 0 (lipopolysaccharide-binding protein); 0 (zonulin); 9012-63-9 (Cholera Toxin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170111
[St] Status:MEDLINE
[do] DOI:10.1136/annrheumdis-2016-210000


  3 / 18 MEDLINE  
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[PMID]:27600198
[Au] Autor:Ahn C; Shin DH; Lee D; Kang SM; Seok JH; Kang HY; Jeung EB
[Ad] Endereço:Laboratory of Veterinary Biochemistry and Molecular Biology, College of Veterinary Medicine, Chungbuk National University, Cheongju, Chungbuk 28644, Republic of Korea.
[Ti] Título:Expression of claudins, occludin, junction adhesion molecule A and zona occludens 1 in canine organs.
[So] Source:Mol Med Rep;14(4):3697-703, 2016 Oct.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Tight junctions are the outermost structures of intercellular junctions and are classified as transmembrane proteins. These factors form selective permeability barriers between cells, act as paracellular transporters and regulate structural and functional polarity of cells. Although tight junctions have been previously studied, comparison of the transcriptional­translational levels of these molecules in canine organs remains to be investigated. In the present study, organ­specific expression of the tight junction proteins, claudin, occludin, junction adhesion molecule A and zona occludens 1 was examined in the canine duodenum, lung, liver and kidney. Results of immunohistochemistry analysis demonstrated that the tight junctions were localized in intestinal villi and glands of the duodenum, bronchiolar epithelia and alveolar walls of the lung, endometrium and myometrium of the hepatocytes, and the distal tubules and glomeruli of the kidney. These results suggest that tight junctions are differently expressed in organs, and therefore may be involved in organ­specific functions to maintain physiological homeostasis.
[Mh] Termos MeSH primário: Claudinas/análise
Cães/genética
Molécula A de Adesão Juncional/análise
Ocludina/análise
Proteína da Zônula de Oclusão-1/genética
[Mh] Termos MeSH secundário: Animais
Claudinas/genética
Duodeno/metabolismo
Duodeno/ultraestrutura
Feminino
Expressão Gênica
Molécula A de Adesão Juncional/genética
Rim/metabolismo
Rim/ultraestrutura
Fígado/metabolismo
Fígado/ultraestrutura
Pulmão/metabolismo
Pulmão/ultraestrutura
Ocludina/genética
RNA Mensageiro/análise
RNA Mensageiro/genética
Proteína da Zônula de Oclusão-1/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Claudins); 0 (Junctional Adhesion Molecule A); 0 (Occludin); 0 (RNA, Messenger); 0 (Zonula Occludens-1 Protein)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160908
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2016.5725


  4 / 18 MEDLINE  
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[PMID]:27341697
[Au] Autor:Tian Y; Cai L; Tian Y; Tu Y; Qiu H; Xie G; Huang D; Zheng R; Zhang W
[Ad] Endereço:Department of Radiation Oncology, Cancer Center of Guangzhou Medical University, Guangzhou, Guangdong Province, People's Republic of China.
[Ti] Título:miR156a Mimic Represses the Epithelial-Mesenchymal Transition of Human Nasopharyngeal Cancer Cells by Targeting Junctional Adhesion Molecule A.
[So] Source:PLoS One;11(6):e0157686, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:MicroRNAs (miRNAs) have been documented as having an important role in the development of cancer. Broccoli is very popular in large groups of the population and has anticancer properties. Junctional adhesion molecule A (JAMA) is preferentially concentrated at tight junctions and influences cell morphology and migration. Epithelial-mesenchymal transition (EMT) is a developmental program associated with cancer progression and metastasis. In this study we aimed to investigate the role of miRNAs from broccoli in human nasopharyngeal cancer (NPC). We demonstrated that a total of 84 conserved miRNAs and 184 putative novel miRNAs were found in broccoli by sequencing technology. Among these, miR156a was expressed the most. In addition, synthetic miR156a mimic inhibited the EMT of NPC cells in vitro. Furthermore, it was confirmed that JAMA was the target of miR156a mimic as validated by 3' UTR luciferase reporter assays and western blotting. Knockdown of JAMA was consistent with the effects of miR156a mimic on the EMT of NPC, and the up-regulation of JAMA could partially restore EMT repressed by miR156a mimic. In conclusion, these results indicate that the miR156a mimic inhibits the EMT of NPC cells by targeting the 3' UTR of JAMA. These miRNA profiles of broccoli provide a fundamental basis for further research. Moreover, the discovery of miR156a may have clinical implications for the treatment of patients with NPC.
[Mh] Termos MeSH primário: Transição Epitelial-Mesenquimal/genética
Molécula A de Adesão Juncional/genética
MicroRNAs/genética
Neoplasias Nasofaríngeas/genética
Neoplasias Nasofaríngeas/patologia
Interferência de RNA
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Sítios de Ligação
Brassica/genética
Linhagem Celular Tumoral
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Molécula A de Adesão Juncional/metabolismo
Neoplasias Nasofaríngeas/metabolismo
Fenótipo
Proteínas Proto-Oncogênicas c-akt/metabolismo
RNA de Plantas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Junctional Adhesion Molecule A); 0 (MicroRNAs); 0 (RNA, Plant); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[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:160625
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0157686


  5 / 18 MEDLINE  
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[PMID]:27107077
[Au] Autor:El-Battrawy I; Tülümen E; Lang S; Akin I; Behnes M; Zhou X; Mavany M; Bugert P; Bieback K; Borggrefe M; Elmas E
[Ad] Endereço:Division of Experimental Cardiology, Medical Faculty Mannheim, University Heidelberg, Mannheim, Germany First Department of Medicine, Medical Faculty Mannheim, University Heidelberg, Mannheim, Germany German Center for Cardiovascular Research, Partner Site, Heidelberg-Mannheim, Mannheim, Germany Ibr
[Ti] Título:Expression of Inflammation-related Intercellular Adhesion Molecules in Cardiomyocytes In Vitro and Modulation by Pro-inflammatory Agents.
[So] Source:In Vivo;30(3):213-7, 2016 May-Jun.
[Is] ISSN:1791-7549
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cell-surface adhesion molecules regulate multiple intercellular and intracellular processes and play important roles in inflammation by facilitating leukocyte endothelial transmigration. Whether cardiomyocytes express surface-adhesion molecules related to inflammation and the effect of pro-inflammatory mediators remain unknown. MATERIALS AND METHODS: In the present study, the expression of different cell-adhesion molecules (CD11a, CD11b, CD31, CD62P, CD162, F11 receptor and mucosal vascular addressin cell adhesion molecule 1 (MADCAM1)) and the effect of pro-inflammatory mediators were investigated in an in vitro model of human cardiomyocytes. Cells were supplied as a primary culture of cardiac alpha actin-positive cells from human heart tissue. The cells were incubated for 24 h with 1 U/ml thrombin or 700 ng/ml lipopolysaccharide (LPS) or with a combination of both. The expression of the cell adhesion molecules was measured by flow cytometry. RESULTS: In cultured human cardiomyocytes, 22.8% of cells expressed CD31, 7.1% MADCAM1 and 2.6% F11R. CD11a, CD11b, CD62P and CD162 were expressed by fewer than 2% of the cells at baseline. CD31 expression increased on incubation of cardiomyocytes with thrombin by 26% (p<0.05) and with LPS by 26% (p=0.06). The combination of thrombin and LPS did not result in increased levels of CD31 (p>0.10). The pro-inflammatory agents LPS and thrombin had no effect on the expression of MADCAM1 and F11R. CONCLUSION: Inflammation-related cell-adhesion molecules CD31, MADCAM1 and F11R were shown to be expressed on the surface of human cardiomyocytes in an in vitro model. Incubation with LPS or thrombin resulted in increased expression of CD31, however, it did not modify the expression of the cell adhesion molecules MADCAM1 and F11R.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/metabolismo
Lipopolissacarídeos/farmacologia
Miócitos Cardíacos/efeitos dos fármacos
Trombina/farmacologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Adulto
Antígeno CD11a/metabolismo
Antígeno CD11b/metabolismo
Células Cultivadas
Citometria de Fluxo
Seres Humanos
Imunoglobulinas/metabolismo
Inflamação/metabolismo
Molécula A de Adesão Juncional/metabolismo
Glicoproteínas de Membrana/metabolismo
Mucoproteínas/metabolismo
Miócitos Cardíacos/citologia
Miócitos Cardíacos/metabolismo
Selectina-P/metabolismo
Molécula-1 de Adesão Celular Endotelial de Plaquetas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (CD11a Antigen); 0 (CD11b Antigen); 0 (Cell Adhesion Molecules); 0 (Immunoglobulins); 0 (Junctional Adhesion Molecule A); 0 (Lipopolysaccharides); 0 (MADCAM1 protein, human); 0 (Membrane Glycoproteins); 0 (Mucoproteins); 0 (P-Selectin); 0 (P-selectin ligand protein); 0 (Platelet Endothelial Cell Adhesion Molecule-1); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160424
[St] Status:MEDLINE


  6 / 18 MEDLINE  
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[PMID]:26985018
[Au] Autor:Scott DW; Tolbert CE; Burridge K
[Ad] Endereço:Department of Cell Biology and Physiology and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 dwscott@email.unc.edu.
[Ti] Título:Tension on JAM-A activates RhoA via GEF-H1 and p115 RhoGEF.
[So] Source:Mol Biol Cell;27(9):1420-30, 2016 05 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Junctional adhesion molecule A (JAM-A) is a broadly expressed adhesion molecule that regulates cell-cell contacts and facilitates leukocyte transendothelial migration. The latter occurs through interactions with the integrin LFA-1. Although we understand much about JAM-A, little is known regarding the protein's role in mechanotransduction or as a modulator of RhoA signaling. We found that tension imposed on JAM-A activates RhoA, which leads to increased cell stiffness. Activation of RhoA in this system depends on PI3K-mediated activation of GEF-H1 and p115 RhoGEF. These two GEFs are further regulated by FAK/ERK and Src family kinases, respectively. Finally, we show that phosphorylation of JAM-A at Ser-284 is required for RhoA activation in response to tension. These data demonstrate a direct role of JAM-A in mechanosignaling and control of RhoA and implicate Src family kinases in the regulation of p115 RhoGEF.
[Mh] Termos MeSH primário: Molécula A de Adesão Juncional/metabolismo
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Moléculas de Adesão Celular
Técnicas de Cultura de Células
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Seres Humanos
Molécula A de Adesão Juncional/genética
Molécula A de Adesão Juncional/fisiologia
Mecanotransdução Celular/fisiologia
Fosfatidilinositol 3-Quinases/metabolismo
Fosforilação
Fatores de Troca de Nucleotídeo Guanina Rho/metabolismo
Transdução de Sinais
Quinases da Família src
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (ARHGEF1 protein, human); 0 (ARHGEF2 protein, human); 0 (Cell Adhesion Molecules); 0 (Guanine Nucleotide Exchange Factors); 0 (Junctional Adhesion Molecule A); 0 (Rho Guanine Nucleotide Exchange Factors); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.10.2 (src-Family Kinases); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160318
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-12-0833


  7 / 18 MEDLINE  
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[PMID]:26912257
[Au] Autor:Bogert NV; Werner I; Kornberger A; Meybohm P; Moritz A; Keller T; Stock UA; Beiras-Fernandez A
[Ad] Endereço:Department of Thoracic and Cardiovascular Surgery, University Hospital Frankfurt, Goethe University, Frankfurt/Main, Germany.
[Ti] Título:Influence of hypothermia and subsequent rewarming upon leukocyte-endothelial interactions and expression of Junctional-Adhesion-Molecules A and B.
[So] Source:Sci Rep;6:21996, 2016 Feb 25.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Patients with risks of ischemic injury, e.g. during circulatory arrest in cardiac surgery, or after resuscitation are subjected to therapeutic hypothermia. For aortic surgery, the body is traditionally cooled down to 18 °C and then rewarmed to body temperature. The role of hypothermia and the subsequent rewarming process on leukocyte-endothelial interactions and expression of junctional-adhesion-molecules is not clarified yet. Thus, we investigated in an in-vitro model the influence of temperature modulation during activation and transendothelial migration of leukocytes through human endothelial cells. Additionally, we investigated the expression of JAMs in the rewarming phase. Exposure to low temperatures alone during transmigration scarcely affects leukocyte extravasation, whereas hypothermia during treatment and transendothelial migration improves leukocyte-endothelial interactions. Rewarming causes a significant up-regulation of transmigration with falling temperatures. JAM-A is significantly modulated during rewarming. Our data suggest that transendothelial migration of leukocytes is not only modulated by cell-activation itself. Activation temperatures and the rewarming process are essential. Continued hypothermia significantly inhibits transendothelial migration, whereas the rewarming process enhances transmigration strongly. The expression of JAMs, especially JAM-A, is strongly modulated during the rewarming process. Endothelial protection prior to warm reperfusion and mild hypothermic conditions reducing the difference between hypothermia and rewarming temperatures should be considered.
[Mh] Termos MeSH primário: Comunicação Celular
Células Endoteliais/fisiologia
Hipotermia
Molécula A de Adesão Juncional/metabolismo
Molécula B de Adesão Juncional/metabolismo
Leucócitos/fisiologia
Reaquecimento
[Mh] Termos MeSH secundário: Membrana Celular/metabolismo
Expressão Gênica
Seres Humanos
Interleucina-10/metabolismo
Interleucina-6/metabolismo
Molécula A de Adesão Juncional/genética
Molécula B de Adesão Juncional/genética
Migração Transendotelial e Transepitelial
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-6); 0 (Junctional Adhesion Molecule A); 0 (Junctional Adhesion Molecule B); 130068-27-8 (Interleukin-10)
[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:160226
[St] Status:MEDLINE
[do] DOI:10.1038/srep21996


  8 / 18 MEDLINE  
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[PMID]:26306570
[Au] Autor:Tuncay H; Brinkmann BF; Steinbacher T; Schürmann A; Gerke V; Iden S; Ebnet K
[Ad] Endereço:Institute-Associated Research Group 'Cell Adhesion and Cell Polarity', University of Münster, 48149 Münster, Germany.
[Ti] Título:JAM-A regulates cortical dynein localization through Cdc42 to control planar spindle orientation during mitosis.
[So] Source:Nat Commun;6:8128, 2015 Aug 26.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Planar spindle orientation in polarized epithelial cells depends on the precise localization of the dynein-dynactin motor protein complex at the lateral cortex. The contribution of cell adhesion molecules to the cortical localization of the dynein-dynactin complex is poorly understood. Here we find that junctional adhesion molecule-A (JAM-A) regulates the planar orientation of the mitotic spindle during epithelial morphogenesis. During mitosis, JAM-A triggers a transient activation of Cdc42 and PI(3)K, generates a gradient of PtdIns(3,4,5)P3 at the cortex and regulates the formation of the cortical actin cytoskeleton. In the absence of functional JAM-A, dynactin localization at the cortex is reduced, the mitotic spindle apparatus is misaligned and epithelial morphogenesis in three-dimensional culture is compromised. Our findings indicate that a PI(3)K- and cortical F-actin-dependent pathway of planar spindle orientation operates in polarized epithelial cells to regulate epithelial morphogenesis, and we identify JAM-A as a junctional regulator of this pathway.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Dineínas/metabolismo
Molécula A de Adesão Juncional/genética
Fosfatidilinositol 3-Quinases/metabolismo
Fosfatos de Fosfatidilinositol/metabolismo
Fuso Acromático/metabolismo
Proteína cdc42 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Polaridade Celular
Cães
Complexo Dinactina
Técnicas de Silenciamento de Genes
Células HEK293
Células HeLa
Seres Humanos
Molécula A de Adesão Juncional/metabolismo
Células Madin Darby de Rim Canino
Microscopia de Fluorescência
Proteínas Associadas aos Microtúbulos/metabolismo
Mitose/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Dynactin Complex); 0 (Junctional Adhesion Molecule A); 0 (Microtubule-Associated Proteins); 0 (Phosphatidylinositol Phosphates); 0 (phosphatidylinositol 3,4,5-triphosphate); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 3.6.4.2 (Dyneins); EC 3.6.5.2 (cdc42 GTP-Binding Protein)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150827
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms9128


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[PMID]:26246869
[Au] Autor:Liu X; Sun W; Zhao Y; Chen B; Wu W; Bao L; Qi R
[Ad] Endereço:Beijing Institute of Geriatrics, Beijing Hospital and Key Laboratory of Geriatrics Ministry of Health, Beijing 100730, China.
[Ti] Título:Ginkgolide B Inhibits JAM-A, Cx43, and VE-Cadherin Expression and Reduces Monocyte Transmigration in Oxidized LDL-Stimulated Human Umbilical Vein Endothelial Cells.
[So] Source:Oxid Med Cell Longev;2015:907926, 2015.
[Is] ISSN:1942-0994
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIM: To investigate the effect of ginkgolide B on junction proteins and the reduction of monocyte migration in oxidized low-density lipoprotein- (ox-LDL-) treated endothelial cells. METHODS: Human umbilical vein endothelial cells (HUVECs) were used in the present study. Immunofluorescence and Western blot were performed to determine the expression of junctional adhesion molecule-A (JAM-A), connexin 43 (Cx43), and vascular endothelial cadherin (VE-cadherin). Monocyte migration was detected by the Transwell assay. RESULTS: ox-LDL stimulation increased JAM-A expression by 35%, Cx43 expression by 24%, and VE-cadherin expression by 37% in HUVECs. Ginkgolide B (0.2, 0.4, and 0.6 mg/mL) dose-dependently abolished the expression of these junction proteins. The monocyte transmigration experiments showed that the level of monocyte migration was sixfold higher in the ox-LDL-treated group than in the control group. Ginkgolide B (0.6 mg/mL) nearly completely abolished monocyte migration. Both ginkgolide B and LY294002 suppressed Akt phosphorylation and the expression of these junction proteins in ox-LDL-treated endothelial cells. These results suggest that the ginkgolide B-induced inhibition of junction protein expression is associated with blockade of the PI3K/Akt pathway. CONCLUSION: Ginkgolide B suppressed junction protein expression and reduced monocyte transmigration that was induced by ox-LDL. Ginkgolide B may improve vascular permeability in atherosclerosis.
[Mh] Termos MeSH primário: Antígenos CD/metabolismo
Caderinas/metabolismo
Conexina 43/metabolismo
Regulação da Expressão Gênica/efeitos dos fármacos
Ginkgolídeos/farmacologia
Molécula A de Adesão Juncional/metabolismo
Lactonas/farmacologia
Lipoproteínas LDL/toxicidade
[Mh] Termos MeSH secundário: Movimento Celular/efeitos dos fármacos
Células Cultivadas
Cromonas/farmacologia
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Monócitos/citologia
Monócitos/efeitos dos fármacos
Monócitos/metabolismo
Morfolinas/farmacologia
Fosforilação/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-akt/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Cadherins); 0 (Chromones); 0 (Connexin 43); 0 (Ginkgolides); 0 (Junctional Adhesion Molecule A); 0 (Lactones); 0 (Lipoproteins, LDL); 0 (Morpholines); 0 (cadherin 5); 0 (oxidized low density lipoprotein); 31M2U1DVID (2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one); DF149B9460 (ginkgolide B); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150807
[St] Status:MEDLINE
[do] DOI:10.1155/2015/907926


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[PMID]:25810543
[Au] Autor:Stettner E; Dietrich MH; Reiss K; Dermody TS; Stehle T
[Ad] Endereço:Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
[Ti] Título:Structure of Serotype 1 Reovirus Attachment Protein σ1 in Complex with Junctional Adhesion Molecule A Reveals a Conserved Serotype-Independent Binding Epitope.
[So] Source:J Virol;89(11):6136-40, 2015 Jun.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian orthoreoviruses use glycans and junctional adhesion molecule A (JAM-A) as attachment receptors. We determined the structure of serotype 1 reovirus attachment protein σ1 alone and in complex with JAM-A. Comparison with the structure of serotype 3 reovirus σ1 bound to JAM-A reveals that both σ1 proteins engage JAM-A with similar affinities and via conserved binding epitopes. Thus, σ1-JAM-A interactions are unlikely to explain the differences in pathogenesis displayed by these reovirus serotypes.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/química
Molécula A de Adesão Juncional/química
Receptores Virais/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Cristalografia por Raios X
Modelos Moleculares
Dados de Sequência Molecular
Ligação Proteica
Conformação Proteica
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Junctional Adhesion Molecule A); 0 (Receptors, Virus); 0 (sigma 1 protein, reovirus)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150327
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00433-15



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