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[PMID]:28747506
[Au] Autor:Kim JY; Wang L; Lee J; Ou JJ
[Ad] Endereço:Department of Molecular Microbiology and Immunology, University of Southern California Keck School of Medicine, Los Angeles, California, USA.
[Ti] Título:Hepatitis C Virus Induces the Localization of Lipid Rafts to Autophagosomes for Its RNA Replication.
[So] Source:J Virol;91(20), 2017 Oct 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Autophagy plays important roles in maintaining cellular homeostasis. It uses double- or multiple-membrane vesicles termed autophagosomes to remove protein aggregates and damaged organelles from the cytoplasm for recycling. Hepatitis C virus (HCV) has been shown to induce autophagy to enhance its own replication. Here we describe a procedure that combines membrane flotation and affinity chromatography for the purification of autophagosomes from cells that harbor an HCV subgenomic RNA replicon. The purified autophagosomes had double- or multiple-membrane structures with a diameter ranging from 200 nm to 600 nm. The analysis of proteins associated with HCV-induced autophagosomes by proteomics led to the identification of HCV nonstructural proteins as well as proteins involved in membrane trafficking. Notably, caveolin-1, caveolin-2, and annexin A2, which are proteins associated with lipid rafts, were also identified. The association of lipid rafts with HCV-induced autophagosomes was confirmed by Western blotting, immunofluorescence microscopy, and immunoelectron microscopy. Their association with autophagosomes was also confirmed in HCV-infected cells. The association of lipid rafts with autophagosomes was specific to HCV, as it was not detected in autophagosomes induced by nutrient starvation. Further analysis indicated that the autophagosomes purified from HCV replicon cells could mediate HCV RNA replication in a lipid raft-dependent manner, as the depletion of cholesterol, a major component of lipid rafts, from autophagosomes abolished HCV RNA replication. Our studies thus demonstrated that HCV could specifically induce the association of lipid rafts with autophagosomes for its RNA replication. HCV can cause severe liver diseases, including cirrhosis and hepatocellular carcinoma, and is one of the most important human pathogens. Infection with HCV can lead to the reorganization of membrane structures in its host cells, including the induction of autophagosomes. In this study, we developed a procedure to purify HCV-induced autophagosomes and demonstrated that HCV could induce the localization of lipid rafts to autophagosomes to mediate its RNA replication. This finding provided important information for further understanding the life cycle of HCV and its interaction with the host cells.
[Mh] Termos MeSH primário: Autofagossomos/fisiologia
Hepacivirus/fisiologia
Microdomínios da Membrana/fisiologia
Replicação Viral
[Mh] Termos MeSH secundário: Anexina A2/química
Anexina A2/isolamento & purificação
Autofagossomos/química
Autofagossomos/virologia
Autofagia
Western Blotting
Caveolina 1/química
Caveolina 1/isolamento & purificação
Caveolina 2/química
Caveolina 2/isolamento & purificação
Linhagem Celular
Colesterol/análise
Cromatografia de Afinidade
Interações Hospedeiro-Patógeno
Seres Humanos
Microdomínios da Membrana/química
Microdomínios da Membrana/virologia
Microscopia de Fluorescência
Microscopia Imunoeletrônica
Proteômica
RNA Viral/fisiologia
Replicon
Proteínas não Estruturais Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Caveolin 1); 0 (Caveolin 2); 0 (RNA, Viral); 0 (Viral Nonstructural Proteins); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180124
[Lr] Data última revisão:
180124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE


  2 / 1180 MEDLINE  
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[PMID]:27773721
[Au] Autor:Tajerian M; Hung V; Khan H; Lahey LJ; Sun Y; Birklein F; Krämer HH; Robinson WH; Kingery WS; Clark JD
[Ad] Endereço:Veterans Affairs Palo Alto Health Care System Palo Alto, CA, USA; Department of Anesthesiology, Stanford University School of Medicine, Stanford, CA, USA; Palo Alto Veterans Institute for Research, Palo Alto, CA, USA. Electronic address: maral@stanford.edu.
[Ti] Título:Identification of KRT16 as a target of an autoantibody response in complex regional pain syndrome.
[So] Source:Exp Neurol;287(Pt 1):14-20, 2017 Jan.
[Is] ISSN:1090-2430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Using a mouse model of complex regional pain syndrome (CRPS), our goal was to identify autoantigens in the skin of the affected limb. METHODS: A CRPS-like state was induced using the tibia fracture/cast immobilization model. Three weeks after fracture, hindpaw skin was homogenized, run on 2-d gels, and probed by sera from fracture and control mice. Spots of interest were analyzed by liquid chromatography-mass spectroscopy (LC-MS) and the list of targets validated by examining their abundance and subcellular localization. In order to measure the autoantigenicity of selected protein targets, we quantified the binding of IgM in control and fracture mice sera, as well as in control and CRPS human sera, to the recombinant protein. RESULTS: We show unique binding between fracture skin extracts and fracture sera, suggesting the presence of auto-antigens. LC-MS analysis provided us a list of potential targets, some of which were upregulated after fracture (KRT16, eEF1a1, and PRPH), while others showed subcellular-redistribution and increased membrane localization (ANXA2 and ENO3). No changes in protein citrullination or carbamylation were observed. In addition to increased abundance, KRT16 demonstrated autoantigenicity, since sera from both fracture mice and CRPS patients showed increased autoantibody binding to recombinant kRT16 protein. CONCLUSIONS: Pursuing autoimmune contributions to CRPS provides a novel approach to understanding the condition and may allow the development of mechanism-based therapies. The identification of autoantibodies against KRT16 as a biomarker in mice and in humans is a critical step towards these goals, and towards redefining CRPS as having an autoimmune etiology.
[Mh] Termos MeSH primário: Autoantígenos/metabolismo
Síndromes da Dor Regional Complexa/sangue
Síndromes da Dor Regional Complexa/patologia
Queratina-6/imunologia
Queratina-6/metabolismo
Pele/metabolismo
Pele/ultraestrutura
Regulação para Cima/fisiologia
[Mh] Termos MeSH secundário: Adulto
Animais
Anexina A2/metabolismo
Autoantígenos/genética
Modelos Animais de Doenças
Membro Posterior/inervação
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Meia-Idade
Fator 1 de Elongação de Peptídeos/metabolismo
Periferinas/metabolismo
Fosfopiruvato Hidratase/metabolismo
Frações Subcelulares/metabolismo
Fraturas da Tíbia/sangue
Fraturas da Tíbia/patologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ANXA2 protein, human); 0 (Annexin A2); 0 (Autoantigens); 0 (EEF1A1 protein, human); 0 (KRT6A protein, human); 0 (Keratin-6); 0 (PRPH protein, human); 0 (Peptide Elongation Factor 1); 0 (Peripherins); EC 4.2.1.11 (Phosphopyruvate Hydratase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:180101
[Lr] Data última revisão:
180101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE


  3 / 1180 MEDLINE  
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[PMID]:29187477
[Au] Autor:Lamb DS; Sondhauss S; Dunne JC; Woods L; Delahunt B; Ferguson P; Murray J; Nacey JN; Denham JW; Jordan TW
[Ad] Endereço:Prostate Cancer Trials Unit, Department of Pathology and Molecular Medicine, University of Otago Wellington, Wellington, New Zealand.
[Ti] Título:Proteins Annexin A2 and PSA in Prostate Cancer Biopsies Do Not Predict Biochemical Failure.
[So] Source:Anticancer Res;37(12):6943-6946, 2017 12.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: We previously reported the use of mass spectrometry and western blotting to identify proteins from tumour regions of formalin-fixed paraffin-embedded biopsies from 16 men who presented with apparently localized prostate cancer, and found that annexin A2 (ANXA2) appeared to be a better predictor of subsequent biochemical failure than prostate-specific antigen (PSA). MATERIALS AND METHODS: In this follow-up study, ANXA2 and PSA were measured using western blotting of proteins extracted from biopsies from 37 men from a subsequent prostate cancer trial. RESULTS: No significant differences in ANXA2 and PSA levels were observed between men with and without biochemical failure. The statistical effect sizes were small, d=0.116 for ANXA2, and 0.266 for PSA. CONCLUSION: ANXA2 and PSA proteins measured from biopsy tumour regions are unlikely to be good biomarkers for prediction of the clinical outcome of prostate cancer presenting with apparently localized disease.
[Mh] Termos MeSH primário: Anexina A2/metabolismo
Antígeno Prostático Específico/metabolismo
Próstata/metabolismo
Neoplasias da Próstata/metabolismo
[Mh] Termos MeSH secundário: Biópsia
Western Blotting
Quimiorradioterapia
Seres Humanos
Masculino
Avaliação de Resultados (Cuidados de Saúde)
Prognóstico
Próstata/patologia
Neoplasias da Próstata/patologia
Neoplasias da Próstata/terapia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); EC 3.4.21.77 (Prostate-Specific Antigen)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171211
[Lr] Data última revisão:
171211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE


  4 / 1180 MEDLINE  
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[PMID]:28976984
[Au] Autor:Liu D; Hu Y; Guo Y; Zhu Z; Lu B; Wang X; Huang Y
[Ad] Endereço:Department of Pharmacology, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, China.
[Ti] Título:Mycoplasma-associated multidrug resistance of hepatocarcinoma cells requires the interaction of P37 and Annexin A2.
[So] Source:PLoS One;12(10):e0184578, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycoplasma infection has been reported to be associated with cancer migration, invasion, epithelial-mesenchymal transition as well as the resistance to nucleoside analogues chemotherapeutic drugs. In this study, we found that the sensitivity of hepatocarcinoma cells to Cisplatin, Gemcitabine and Mitoxantrone was increased by mycoplasma elimination. Similar to the effect of anti-mycoplasma agent, interrupting the interaction between Mycoplasma hyorhinis membrane protein P37 and Annexin A2 of host cells using the N-terminal of ANXA2 polypeptide enhanced the sensitivity of HCC97L cells to Gemcitabine and Mitoxantrone. Meanwhile, we did not observe any changes in expression or distribution of multidrug resistance associated transporters, ATP-Binding Cassette protein B1, C1 and G2, on the removal of mycoplasma. These results suggest that mycoplasma induces a resistance to multiple drugs in hepatocarcinoma cells which required the interaction of P37 and Annexin A2. The pathway downstream this interaction needs to be explored.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Anexina A2/metabolismo
Carcinoma Hepatocelular/patologia
Neoplasias Hepáticas/patologia
Mycoplasma hyorhinis/fisiologia
[Mh] Termos MeSH secundário: Antibacterianos/farmacologia
Antineoplásicos/farmacologia
Azitromicina/farmacologia
Carcinoma Hepatocelular/metabolismo
Carcinoma Hepatocelular/microbiologia
Linhagem Celular Tumoral
Desoxicitidina/análogos & derivados
Desoxicitidina/farmacologia
Resistência a Múltiplos Medicamentos
Resistência a Medicamentos Antineoplásicos
Fluoroquinolonas/farmacologia
Seres Humanos
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/microbiologia
Mitoxantrona/farmacologia
Mycoplasma hyorhinis/efeitos dos fármacos
Mycoplasma hyorhinis/genética
Mycoplasma hyorhinis/isolamento & purificação
Ligação Proteica
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Annexin A2); 0 (Anti-Bacterial Agents); 0 (Antineoplastic Agents); 0 (Fluoroquinolones); 0 (p37 protein, human); 0W860991D6 (Deoxycytidine); 83905-01-5 (Azithromycin); B76N6SBZ8R (gemcitabine); BZ114NVM5P (Mitoxantrone); U188XYD42P (moxifloxacin)
[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:171005
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184578


  5 / 1180 MEDLINE  
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[PMID]:28943392
[Au] Autor:Romualdo GR; Grassi TF; Goto RL; Tablas MB; Bidinotto LT; Fernandes AAH; Cogliati B; Barbisan LF
[Ad] Endereço:Department of Pathology, Botucatu Medical School, São Paulo State University (UNESP), Botucatu - SP, Brazil.
[Ti] Título:An integrative analysis of chemically-induced cirrhosis-associated hepatocarcinogenesis: Histological, biochemical and molecular features.
[So] Source:Toxicol Lett;281:84-94, 2017 Nov 05.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This study aimed the integrative characterization of morphological, biochemical and molecular features of chemically-induced cirrhosis-associated hepatocarcinogenesis. Thus, male Wistar rats were submitted to a diethylnitrosamine (DEN)/thioacetamide (TAA)-induced model. Liver tissue was processed for global gene expression, histopathological and collagen evaluations; as well as immunohistochemical and oxidative stress analysis. Gene Ontology and functional analysis showed the upregulation of extracellular matrix deposition genes, such as collagen type I alpha 1 and 2 (Col1α1 and Col1α2) and tissue inhibitor of metalloproteinase 1 and 2 genes (Timp1 and Timp2). In agreement these findings, animals presented extensive liver cirrhosis with increased collagen deposition (Sirius red). Besides, the animals developed many glutathione S-transferase pi (GST-P)-positive preneoplastic lesions showing high cell proliferation (Ki-67), in keeping with the Gstp1 and Gstp2 increased gene expression. DEN/TAA-treated rats also showed the upregulation of tumorigenesis-related annexin A2 gene (Anxa2) and few neoplastic lesions (hepatocellular adenomas, carcinomas, and cholangiocarcinoma). In contrast, gene expression and activity of antioxidant enzymes were decreased (glutathione peroxidase, total glutathione-S-transferase, and catalase). The model featured remarkable similarities to human hepatocarcinogenesis. Our findings could bring up new molecular insights into cirrhosis-associated hepatocarcinogenesis, and provide a suitable animal model for the establishment of further diagnostic, preventive and therapeutic approaches.
[Mh] Termos MeSH primário: Carcinogênese/genética
Regulação Neoplásica da Expressão Gênica
Cirrose Hepática/genética
Neoplasias Hepáticas Experimentais/genética
[Mh] Termos MeSH secundário: Alanina Transaminase/metabolismo
Animais
Anexina A2/genética
Anexina A2/metabolismo
Aspartato Aminotransferases/metabolismo
Carcinogênese/induzido quimicamente
Colágeno/genética
Colágeno/metabolismo
Dietilnitrosamina/toxicidade
Glutationa Peroxidase/genética
Glutationa Peroxidase/metabolismo
Glutationa Transferase/genética
Glutationa Transferase/metabolismo
Cirrose Hepática/induzido quimicamente
Neoplasias Hepáticas Experimentais/induzido quimicamente
Masculino
Metaloproteinases da Matriz/genética
Metaloproteinases da Matriz/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Ratos
Ratos Wistar
Tioacetamida/toxicidade
Inibidores Teciduais de Metaloproteinases/genética
Inibidores Teciduais de Metaloproteinases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Tissue Inhibitor of Metalloproteinases); 075T165X8M (Thioacetamide); 3IQ78TTX1A (Diethylnitrosamine); 9007-34-5 (Collagen); EC 1.11.1.9 (Glutathione Peroxidase); EC 2.5.1.18 (Glutathione Transferase); EC 2.6.1.1 (Aspartate Aminotransferases); EC 2.6.1.2 (Alanine Transaminase); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE


  6 / 1180 MEDLINE  
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[PMID]:28937994
[Au] Autor:Hakobyan D; Gerke V; Heuer A
[Ad] Endereço:Institute of Physical Chemistry, University of Muenster, Muenster, Germany.
[Ti] Título:Modeling of annexin A2-Membrane interactions by molecular dynamics simulations.
[So] Source:PLoS One;12(9):e0185440, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The annexins are a family of Ca2+-regulated phospholipid binding proteins that are involved in membrane domain organization and membrane trafficking. Although they are widely studied and crystal structures are available for several soluble annexins their mode of membrane association has never been studied at the molecular level. Here we obtained molecular information on the annexin-membrane interaction that could serve as paradigm for the peripheral membrane association of cytosolic proteins by Molecular Dynamics simulations. We analyzed systems containing the monomeric annexin A2 (AnxA2), a membrane with negatively charged phosphatidylserine (POPS) lipids as well as Ca2+ ions. On the atomic level we identify the AnxA2 orientations and the respective residues which display the strongest interaction with Ca2+ ions and the membrane. The simulation results fully agree with earlier experimental findings concerning the positioning of bound Ca2+ ions. Furthermore, we identify for the first time a significant interaction between lysine residues of the protein and POPS lipids that occurs independently of Ca2+ suggesting that AnxA2-membrane interactions can also occur in a low Ca2+ environment. Finally, by varying Ca2+ concentrations and lipid composition in our simulations we observe a calcium-induced negative curvature of the membrane as well as an AnxA2-induced lipid ordering.
[Mh] Termos MeSH primário: Anexina A2/metabolismo
Membranas Artificiais
Simulação de Dinâmica Molecular
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Cátions Bivalentes/metabolismo
Citosol/metabolismo
Dimerização
Fosfatidilserinas/química
Ligação Proteica
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Cations, Divalent); 0 (Membranes, Artificial); 0 (Phosphatidylserines); 40290-44-6 (1-palmitoyl-2-oleoylglycero-3-phosphoserine); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185440


  7 / 1180 MEDLINE  
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[PMID]:28729092
[Au] Autor:Liao L; Zheng B; Yi B; Liu C; Chen L; Zeng Z; Gao J
[Ad] Endereço:Department of Anesthesia, People's Hospital of Qijiang District, Chongqing 401420, China.
[Ti] Título:Annexin A2-modulated proliferation of pulmonary arterial smooth muscle cells depends on caveolae and caveolin-1 in hepatopulmonary syndrome.
[So] Source:Exp Cell Res;359(1):266-274, 2017 Oct 01.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have established that annexin A2 (ANXA2) is an important factor in the experimental hepatopulmonary syndrome (HPS) serum-induced proliferation of pulmonary arterial smooth muscle cells (PASMCs). However, the detailed mechanism remains unclear. ANXA2 translocated to the caveolin-enriched microdomains (caveolae) in PASMCs upon HPS serum stimulation. The disruption of caveolae by Methyl-ß-cyclodextrin (MßCD) alleviated the caveolae recruitment of ANXA2 and the ANXA2-mediated activation of ERK1/2 and NF-κB, so that ANXA2-modulated PASMC proliferation was suppressed. The over-expression of Cav-1 resulted in the relocation of ANXA2 from caveolae and negatively regulated ERK1/2 and NF-κB activation, which inhibited the ANXA2-modulated PASMC proliferative behavior. These data indicate that caveolae function as a signaling platform for ANXA2-induced proliferative behavior and Cav-1 participates upstream of ANXA2 in the activation of ERK1/2 and NF-κB.
[Mh] Termos MeSH primário: Anexina A2/metabolismo
Cavéolas/metabolismo
Caveolina 1/metabolismo
Síndrome Hepatopulmonar/metabolismo
Síndrome Hepatopulmonar/patologia
Miócitos de Músculo Liso/patologia
Artéria Pulmonar/patologia
[Mh] Termos MeSH secundário: Animais
Caveolina 1/química
Proliferação Celular
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Síndrome Hepatopulmonar/sangue
Masculino
NF-kappa B/metabolismo
Domínios Proteicos
Ratos Sprague-Dawley
beta-Ciclodextrinas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Caveolin 1); 0 (NF-kappa B); 0 (beta-Cyclodextrins); 0 (methyl-beta-cyclodextrin); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE


  8 / 1180 MEDLINE  
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[PMID]:28697839
[Au] Autor:Shen DD; Yuan F; Hou JH
[Ad] Endereço:Department of Pediatrics, Henan Province Hospital of Traditional Chinese Medicine, Zhengzhou 450002, China. jianghonghoures@163.com.
[Ti] Título:[Effect of annexin A2 on EGFR/NF-κB signal transduction and mucin expression in human airway epithelial cells treated with Mycoplasma pneumoniae].
[So] Source:Zhongguo Dang Dai Er Ke Za Zhi;19(7):820-825, 2017 Jul.
[Is] ISSN:1008-8830
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To investigate the effect of annexin A2 (AnxA2) on epithelial growth factor receptor (EGFR)/nuclear factor-κB (NF-κB) signal transduction and mucin expression in human airway epithelial H292 cells treated with Mycoplasma pneumoniae (MP). METHODS: H292 cells were divided into control group, MP group, NC-siRNA+MP group, and AnxA2 siRNA+MP group. The cells in the MP group were incubated with 5 µg/mL MP antigen for 2 hours. The cells in the NC-siRNA+MP and AnxA2 siRNA+MP groups were transfected with NC-siRNA and AnxA2 siRNA for 24 hours, followed by MP antigen stimulation for 2 hours. The MTT method was used to measure cell viability; quantitative real-time PCR was used to measure the mRNA expression of AnxA2; Western blot was used to measure the protein expression of AnxA2, phosphorylated EGFR (p-EGFR), and phosphorylated p65 NF-κB (p-p65 NF-κB); ELISA was used to measure the secretion of mucin 5AC (MUC5AC) and mucin 5B (MUC5B). RESULTS: The MP and NC-siRNA+MP groups had lower cell viability than the control group (P<0.05). The AnxA2 siRNA+MP group had higher cell viability than the MP and NC-siRNA+MP groups and lower cell viability than the control group (P<0.05). The MP and NC-siRNA+MP groups had significantly higher mRNA and protein expression of AnxA2 than the AnxA2 siRNA+MP group (P<0.05). Compared with the control group, the MP and NC-siRNA+MP groups had significant increases in the protein expression of p-EGFR, p-p65 NF-κB, MUC5AC, and MUC5B (P<0.05); the AnxA2 siRNA+MP group had lower protein expression than the MP and NC-siRNA+MP groups, but higher protein expression than the control group (P<0.05). CONCLUSIONS: AnxA2 is involved in the airway lesion induced by MP antigen via mediating EGFR/NF-κB signaling activation and mucin expression in human airway epithelial cells.
[Mh] Termos MeSH primário: Anexina A2/fisiologia
Brônquios/fisiologia
Mucinas/análise
Mycoplasma pneumoniae/patogenicidade
NF-kappa B/fisiologia
Receptor do Fator de Crescimento Epidérmico/fisiologia
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Células Cultivadas
Células Epiteliais/microbiologia
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Mucins); 0 (NF-kappa B); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE


  9 / 1180 MEDLINE  
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[PMID]:28694388
[Au] Autor:Luo M; Flood EC; Almeida D; Yan L; Berlin DA; Heerdt PM; Hajjar KA
[Ad] Endereço:Department of Pediatrics, Weill Cornell Medical College, New York, NY.
[Ti] Título:Annexin A2 supports pulmonary microvascular integrity by linking vascular endothelial cadherin and protein tyrosine phosphatases.
[So] Source:J Exp Med;214(9):2535-2545, 2017 Sep 04.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Relative or absolute hypoxia activates signaling pathways that alter gene expression and stabilize the pulmonary microvasculature. Alveolar hypoxia occurs in disorders ranging from altitude sickness to airway obstruction, apnea, and atelectasis. Here, we report that the phospholipid-binding protein, annexin A2 (ANXA2) functions to maintain vascular integrity in the face of alveolar hypoxia. We demonstrate that microvascular endothelial cells (ECs) from mice display reduced barrier function and excessive Src-related tyrosine phosphorylation of the adherens junction protein vascular endothelial cadherin (VEC). Moreover, unlike controls, mice develop pulmonary edema and neutrophil infiltration in the lung parenchyma in response to subacute alveolar hypoxia. Mice deficient in the ANXA2-binding partner, S100A10, failed to demonstrate hypoxia-induced pulmonary edema under the same conditions. Further analyses reveal that ANXA2 forms a complex with VEC and its phosphatases, EC-specific protein tyrosine phosphatase (VE-PTP) and Src homology phosphatase 2 (SHP2), both of which are implicated in vascular integrity. In the absence of ANXA2, VEC is hyperphosphorylated at tyrosine 731 in response to vascular endothelial growth factor, which likely contributes to hypoxia-induced extravasation of fluid and leukocytes. We conclude that ANXA2 contributes to pulmonary microvascular integrity by enabling VEC-related phosphatase activity, thereby preventing vascular leak during alveolar hypoxia.
[Mh] Termos MeSH primário: Anexina A2/fisiologia
Antígenos CD/fisiologia
Caderinas/fisiologia
Pulmão/irrigação sanguínea
Microvasos/fisiologia
Proteínas Tirosina Fosfatases/fisiologia
[Mh] Termos MeSH secundário: Animais
Anexina A2/metabolismo
Antígenos CD/metabolismo
Caderinas/metabolismo
Feminino
Hipóxia/fisiopatologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Edema Pulmonar/fisiopatologia
Fator A de Crescimento do Endotélio Vascular/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Antigens, CD); 0 (Cadherins); 0 (Vascular Endothelial Growth Factor A); 0 (cadherin 5); EC 3.1.3.48 (Protein Tyrosine Phosphatases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20160652


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[PMID]:28515087
[Au] Autor:Lubarski-Gotliv I; Dey K; Kuznetsov Y; Kalchenco V; Asher C; Garty H
[Ad] Endereço:Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel; and ira.gotliv@gmail.com.
[Ti] Título:FXYD5 (dysadherin) may mediate metastatic progression through regulation of the ß-Na -K -ATPase subunit in the 4T1 mouse breast cancer model.
[So] Source:Am J Physiol Cell Physiol;313(1):C108-C117, 2017 Jul 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:FXYD5 is a Na -K -ATPase regulator, expressed in a variety of normal epithelia. In parallel, it has been found to be associated with several types of cancer and effect lethal outcome by promoting metastasis. However, the molecular mechanism underlying FXYD5 mediated invasion has not yet been identified. In this study, using in vivo 4T1 murine breast cancer model, we found that FXYD5-specific shRNA significantly inhibited lung cancer metastasis, without having a substantial effect on primary tumor growth. Our study reveals that FXYD5 participates in multiple stages of metastatic development and exhibits more than one mode of E-cadherin regulation. We provide the first evidence that FXYD5-related morphological changes are mediated through its interaction with Na -K -ATPase. Experiments in cultured 4T1 cells have indicated that FXYD5 expression may downregulate the ß1 isoform of the pump. This behavior could have implications on both transcellular interactions and intracellular events. Further studies suggest that differential localization of the adaptor protein Annexin A2 in FXYD5-expressing cells may correlate with matrix metalloproteinase 9 secretion and adhesion changes in 4T1 wild-type cells.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Neoplasias Pulmonares/genética
Neoplasias Mamárias Experimentais/genética
Proteínas de Membrana/genética
Neoplasias Lipomatosas/genética
ATPase Trocadora de Sódio-Potássio/genética
[Mh] Termos MeSH secundário: Animais
Anexina A2/genética
Anexina A2/metabolismo
Caderinas/genética
Caderinas/metabolismo
Adesão Celular
Linhagem Celular Tumoral
Movimento Celular
Modelos Animais de Doenças
Feminino
Neoplasias Pulmonares/metabolismo
Neoplasias Pulmonares/secundário
Glândulas Mamárias Animais/metabolismo
Glândulas Mamárias Animais/patologia
Neoplasias Mamárias Experimentais/metabolismo
Neoplasias Mamárias Experimentais/patologia
Metaloproteinase 9 da Matriz/genética
Metaloproteinase 9 da Matriz/metabolismo
Proteínas de Membrana/antagonistas & inibidores
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos BALB C
Neoplasias Lipomatosas/metabolismo
Neoplasias Lipomatosas/patologia
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
ATPase Trocadora de Sódio-Potássio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Cadherins); 0 (E-cadherin protein, mouse); 0 (FXYD5 protein, mouse); 0 (Membrane Proteins); 0 (Protein Subunits); 0 (RNA, Small Interfering); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 3.4.24.35 (Mmp9 protein, mouse); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00206.2016



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