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Pesquisa : A11.284.149.450 [Categoria DeCS]
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  1 / 20773 MEDLINE  
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[PMID]:28460485
[Au] Autor:Lv LX; Zhou ZX; Zhou Z; Zhang LJ; Yan R; Zhao Z; Yang LY; Bian XY; Jiang HY; Li YD; Sun YS; Xu QQ; Hu GL; Guan WJ; Li YQ
[Ad] Endereço:Institute of Pharmaceutical Biotechnology and College of Pharmaceutical Sciences, Zhejiang University, 310058 Hangzhou, China.
[Ti] Título:Hispidin induces autophagic and necrotic death in SGC-7901 gastric cancer cells through lysosomal membrane permeabilization by inhibiting tubulin polymerization.
[So] Source:Oncotarget;8(16):26992-27006, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hispidin and its derivatives are widely distributed in edible mushrooms. Hispidin is more cytotoxic to A549, SCL-1, Bel7402 and Capan-1 cancer cells than to MRC5 normal cells; by contrast, hispidin protects H9c2 cardiomyoblast cells from hydrogen peroxide-induced or doxorubicin-induced apoptosis. Consequently, further research on how hispidin affects normal and cancer cells may help treat cancer and reduce chemotherapy-induced side effects. This study showed that hispidin caused caspase-independent death in SGC-7901 cancer cells but not in GES-1 normal cells. Hispidin-induced increases in LC3-II occurred in SGC-7901 cells in a time independent manner. Cell death can be partially inhibited by treatment with ATG5 siRNA but not by autophagy or necroptosis inhibitors. Ultrastructural evidence indicated that hispidin-induced necrotic cell death involved autophagy. Hispidin-induced lysosomal membrane permeabilization (LMP) related to complex cell death occurred more drastically in SGC-7901 cells than in GES-1 cells. Ca2+ rather than cathepsins from LMP contributed more to cell death. Hispidin induced microtubule depolymerization, which can cause LMP, more drastically in SGC-7901 cells than in GES-1 cells. At 4.1 µM, hispidin promoted cell-free tubulin polymerization but at concentrations higher than 41 µM, hispidin inhibited polymerization. Hispidin did not bind to tubulin. Alterations in microtubule regulatory proteins, such as stathmin phosphorylation at Ser16, contributed to hispidin-induced SGC-7901 cell death. In conclusion, hispidin at concentrations higher than 41 µM may inhibit tubulin polymerization by modulating microtubule regulatory proteins, such as stathmin, causing LMP and complex SGC-7901 cell death. This mechanism suggests a promising novel treatment for human cancer.
[Mh] Termos MeSH primário: Autofagia/efeitos dos fármacos
Membranas Intracelulares/efeitos dos fármacos
Lisossomos/metabolismo
Multimerização Proteica/efeitos dos fármacos
Pironas/farmacologia
Tubulina (Proteína)/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Caspases/metabolismo
Morte Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Seres Humanos
Microtúbulos/química
Microtúbulos/metabolismo
Óxido Nítrico/biossíntese
Permeabilidade
Fosforilação
Estatmina/metabolismo
Tubulina (Proteína)/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyrones); 0 (STMN1 protein, human); 0 (Stathmin); 0 (Tubulin); 31C4KY9ESH (Nitric Oxide); EC 3.4.22.- (Caspases); SSJ18CG55E (hispidin)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15935


  2 / 20773 MEDLINE  
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[PMID]:28456980
[Au] Autor:Otomo T; Yoshimori T
[Ad] Endereço:Department of Genetics, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, Japan.
[Ti] Título:Lysophagy: A Method for Monitoring Lysosomal Rupture Followed by Autophagy-Dependent Recovery.
[So] Source:Methods Mol Biol;1594:141-149, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Selective autophagy recognizes specific targets, including damaged mitochondria (mitophagy), aggregated proteins (aggrephagy), and invading bacteria (xenophagy) to engulf by isolation membrane, and degrades toxic materials within lysosomes. We recently revealed that a membrane-damaged lysosome itself also becomes a target of autophagy and named this process lysophagy. In this chapter, we describe methods for monitoring lysophagy; detecting lysosomal damage by staining of galectin and study the subsequent autophagic process in cultured mammalian cells.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Lisossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia/genética
Seres Humanos
Membranas Intracelulares/metabolismo
Degradação Mitocondrial/fisiologia
Fagossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6934-0_8


  3 / 20773 MEDLINE  
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[PMID]:28456977
[Au] Autor:Giraldo AMV; Öllinger K; Loitto V
[Ad] Endereço:Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
[Ti] Título:Microscopic Analysis of Lysosomal Membrane Permeabilization.
[So] Source:Methods Mol Biol;1594:73-92, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysosomes and lysosomal proteases have been found to participate during several forms of cell death pathways including apoptosis. A critical step in the mediation of apoptotic signaling is the release of cathepsins to the cytosol, a process known as lysosomal membrane permeabilization (LMP). In this chapter, we describe immunofluorescence detection of LMP in cell cultures stained for cathepsin B and LAMP-2 using three confocal techniques namely laser scanning, spinning disk, and aperture correlation spinning disk confocal to obtain images. Image analysis is performed using Huygens software for deconvolution. LMP results in a decrease in the fraction of cathepsin B colocalizing with LAMP-2, which is quantified through Manders' colocalization coefficient. Analysis of the images obtained by the three techniques show the same trend but the magnitude of the decrease differs due to the axial resolution. The observations emphasize the use of highest possible resolution when determining colocalization.
[Mh] Termos MeSH primário: Membranas Intracelulares/metabolismo
Lisossomos/metabolismo
Microscopia Confocal/métodos
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Imuno-Histoquímica
Proteína 2 de Membrana Associada ao Lisossomo/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lysosomal-Associated Membrane Protein 2)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6934-0_5


  4 / 20773 MEDLINE  
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[PMID]:28456515
[Au] Autor:Sposini S; Hanyaloglu AC
[Ad] Endereço:Institute of Reproductive and Developmental Biology, Dept. Surgery and Cancer, Imperial College London, UK.
[Ti] Título:Spatial encryption of G protein-coupled receptor signaling in endosomes; Mechanisms and applications.
[So] Source:Biochem Pharmacol;143:1-9, 2017 11 01.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Within any cellular signaling system membrane trafficking is a critical mechanism for cells to translate complex networks into specific downstream responses, including the signal pathways activated by the superfamily of G protein-coupled receptors (GPCRs). Classically, membrane trafficking is viewed as a mechanism to regulate ligand sensitivity of a target tissue by controlling the level of surface receptors. Recent studies, however, have not only highlighted that GPCR trafficking is a tightly regulated process critical for spatio-temporal control of signaling, but that heterotrimeric G protein signaling can also be reactivated or continue to signal from distinct endocytic compartments, and even endosomal microdomains. The significance of spatio-temporal control will be discussed, not only with respect to how these novel molecular pathways impact our basic understanding of cellular regulation, but also our view of how aberrant signaling can result in disease. Furthermore, these mechanisms offer the potential application for novel therapeutic strategies to identify GPCR compounds with high specificity in their actions.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Endossomos/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
[Mh] Termos MeSH secundário: Animais
Endocitose/fisiologia
Seres Humanos
Membranas Intracelulares/metabolismo
Transporte Proteico
Receptores Acoplados a Proteínas-G/genética
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Receptors, G-Protein-Coupled)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


  5 / 20773 MEDLINE  
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[PMID]:29236392
[Au] Autor:Rudnytska MV; Palladina TA
[Ti] Título:Effect of preparations Methyure and Ivine on Са(2+)-ATPases activity in plasma and vacuolar membrane of corn seedling roots under salt stress conditions.
[So] Source:Ukr Biochem J;89(1):76-81, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Ca2+-ATPases regulate the functioning of Ca2+-dependent signaling pathway SOS which provides removal of Na+ from the cytoplasm of cells via Na+/H+-antiporters in saline conditions. The influence of synthetic preparations Methyure and Ivine on the Ca2+-ATPase activity was investigated. It was shown that exposition of corn seedlings in the presence of 0.1 M NaCl rather enhanced hydrolytic than transport activity of Ca2+-ATPases in plasma and vacuolar membrane of root cells. It was found that seed treatment with such preparations, especially Methyure, caused intensification of the both activities of Ca2+-ATPases, mainly in vacuolar membrane. The results indicate than salt protective activity of preparations, especially Methyure, is associated with increased Ca2+-ATPase activity, which regulates the functioning of Na+/H+-antiporters.
[Mh] Termos MeSH primário: ATPases Transportadoras de Cálcio/metabolismo
Membrana Celular/efeitos dos fármacos
Substâncias Protetoras/farmacologia
Pirimidinas/farmacologia
Trocadores de Sódio-Hidrogênio/metabolismo
Vacúolos/efeitos dos fármacos
Zea mays/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Membrana Celular/metabolismo
Membranas Intracelulares/efeitos dos fármacos
Membranas Intracelulares/metabolismo
Transporte de Íons
Células Vegetais/efeitos dos fármacos
Células Vegetais/metabolismo
Raízes de Plantas/efeitos dos fármacos
Raízes de Plantas/metabolismo
Salinidade
Plântulas/efeitos dos fármacos
Plântulas/metabolismo
Cloreto de Sódio/farmacologia
Trocadores de Sódio-Hidrogênio/agonistas
Estresse Fisiológico
Vacúolos/metabolismo
Zea mays/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protective Agents); 0 (Pyrimidines); 0 (Sodium-Hydrogen Exchangers); 451W47IQ8X (Sodium Chloride); EC 3.6.3.8 (Calcium-Transporting ATPases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj89.01.076


  6 / 20773 MEDLINE  
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[PMID]:29227610
[Au] Autor:Kovalenko NO; Palladina TA
[Ti] Título:Gene expression of H+-pumps in plasma and vacuolar membranes of corn root cells under the effect of sodium ions and bioactive preparations.
[So] Source:Ukr Biochem J;88(2):89-97, 2016 Mar-Apr.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Four isoforms of H+-ATPase of plasma membrane: MHA1, MHA2, MHA3, MHA4 are expressed in the corn seedling roots with prevalence of genes MHA3 і MHA4. The exposure of seedlings in the presence of 0.1 M NaCl activated the expression of MHA4 gene isoform, that demonstrates its important role in the processes of adaptation to salinization conditions. In vacuolar membrane, where potential is created by two Н+-pumps, sodium ions activated gene expression of only Н+-АТРase of V-type, taking no effect on the expression of Н+-pyrophosphatase. The seeds pretreatment by synthetic preparations Methyure and Ivine did not affect gene expression of Н+-pumps. Thus we can suppose that the ability of the above preparations to activate functioning of Н+-pumps in the presence of sodium ions is realized at the post-tranlation level.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Proteínas de Plantas/genética
Raízes de Plantas/efeitos dos fármacos
Substâncias Protetoras/farmacologia
Pirimidinas/farmacologia
Cloreto de Sódio/farmacologia
ATPases Vacuolares Próton-Translocadoras/genética
[Mh] Termos MeSH secundário: Adaptação Fisiológica/genética
Membrana Celular/efeitos dos fármacos
Membrana Celular/enzimologia
Membranas Intracelulares/efeitos dos fármacos
Membranas Intracelulares/enzimologia
Isoenzimas/genética
Isoenzimas/metabolismo
Células Vegetais/efeitos dos fármacos
Células Vegetais/enzimologia
Proteínas de Plantas/metabolismo
Raízes de Plantas/enzimologia
Raízes de Plantas/crescimento & desenvolvimento
Salinidade
Plântulas/efeitos dos fármacos
Plântulas/enzimologia
Plântulas/crescimento & desenvolvimento
Sódio/metabolismo
ATPases Vacuolares Próton-Translocadoras/metabolismo
Vacúolos/efeitos dos fármacos
Vacúolos/enzimologia
Zea mays/efeitos dos fármacos
Zea mays/enzimologia
Zea mays/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Plant Proteins); 0 (Protective Agents); 0 (Pyrimidines); 451W47IQ8X (Sodium Chloride); 9NEZ333N27 (Sodium); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.02.089


  7 / 20773 MEDLINE  
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[PMID]:28464022
[Au] Autor:Aydin I; Villalonga-Planells R; Greune L; Bronnimann MP; Calton CM; Becker M; Lai KY; Campos SK; Schmidt MA; Schelhaas M
[Ad] Endereço:Cellular Virology, Institutes of Molecular Virology and Medical Biochemistry, Center for Molecular Biology of Inflammation (ZMBE), University of Münster, Münster, Germany.
[Ti] Título:A central region in the minor capsid protein of papillomaviruses facilitates viral genome tethering and membrane penetration for mitotic nuclear entry.
[So] Source:PLoS Pathog;13(5):e1006308, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Incoming papillomaviruses (PVs) depend on mitotic nuclear envelope breakdown to gain initial access to the nucleus for viral transcription and replication. In our previous work, we hypothesized that the minor capsid protein L2 of PVs tethers the incoming vDNA to mitotic chromosomes to direct them into the nascent nuclei. To re-evaluate how dynamic L2 recruitment to cellular chromosomes occurs specifically during prometaphase, we developed a quantitative, microscopy-based assay for measuring the degree of chromosome recruitment of L2-EGFP. Analyzing various HPV16 L2 truncation-mutants revealed a central chromosome-binding region (CBR) of 147 amino acids that confers binding to mitotic chromosomes. Specific mutations of conserved motifs (IVAL286AAAA, RR302/5AA, and RTR313EEE) within the CBR interfered with chromosomal binding. Moreover, assembly-competent HPV16 containing the chromosome-binding deficient L2(RTR313EEE) or L2(IVAL286AAAA) were inhibited for infection despite their ability to be transported to intracellular compartments. Since vDNA and L2 were not associated with mitotic chromosomes either, the infectivity was likely impaired by a defect in tethering of the vDNA to mitotic chromosomes. However, L2 mutations that abrogated chromatin association also compromised translocation of L2 across membranes of intracellular organelles. Thus, chromatin recruitment of L2 may in itself be a requirement for successful penetration of the limiting membrane thereby linking both processes mechanistically. Furthermore, we demonstrate that the association of L2 with mitotic chromosomes is conserved among the alpha, beta, gamma, and iota genera of Papillomaviridae. However, different binding patterns point to a certain variance amongst the different genera. Overall, our data suggest a common strategy among various PVs, in which a central region of L2 mediates tethering of vDNA to mitotic chromosomes during cell division thereby coordinating membrane translocation and delivery to daughter nuclei.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/metabolismo
Genoma Viral/genética
Papillomavirus Humano 16/genética
Mitose
Proteínas Oncogênicas Virais/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Proteínas do Capsídeo/genética
Núcleo Celular/metabolismo
Núcleo Celular/virologia
Cromatina/genética
Cromossomos/genética
DNA Viral/genética
DNA Viral/metabolismo
Genes Reporter
Papillomavirus Humano 16/fisiologia
Seres Humanos
Membranas Intracelulares/metabolismo
Membranas Intracelulares/virologia
Mutação
Proteínas Oncogênicas Virais/genética
Vírion
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Chromatin); 0 (DNA, Viral); 0 (L2 protein, Human papillomavirus type 16); 0 (Oncogene Proteins, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006308


  8 / 20773 MEDLINE  
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[PMID]:28463755
[Au] Autor:Yu S; Melia TJ
[Ad] Endereço:Department of Cell Biology, Yale University School of Medicine, New Haven, CT, United States.
[Ti] Título:The coordination of membrane fission and fusion at the end of autophagosome maturation.
[So] Source:Curr Opin Cell Biol;47:92-98, 2017 Aug.
[Is] ISSN:1879-0410
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The two major objectives of macroautophagy are to sequester cargo away from the cytoplasm and deliver this material for breakdown in the lysosome. Sequestration is complete when the autophagosome membrane undergoes fission to produce separate inner and outer membranes, while delivery into the lysosome requires fusion of the outer autophagosome membrane with the lysosome membrane. Thus, the merging of membranes through fission and fusion underlies each of the pivotal events in macroautophagic clearance. How these merging events are controlled in the cell is poorly understood. Several recent studies however suggest that the two events may be temporally coordinated and rely upon members of the classic membrane fusion SNARE family as well as the autophagy-specific family of Atg8 proteins.
[Mh] Termos MeSH primário: Autofagossomos/metabolismo
Membranas Intracelulares/metabolismo
Lisossomos/metabolismo
Proteínas SNARE/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia
Família da Proteína 8 Relacionada à Autofagia/metabolismo
Fusão de Membrana
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Autophagy-Related Protein 8 Family); 0 (SNARE Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  9 / 20773 MEDLINE  
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[PMID]:29020039
[Au] Autor:Yan Y; Yu L; Castro L; Dixon D
[Ad] Endereço:Molecular Pathogenesis Group, National Toxicology Program Laboratory (NTPL), National Toxicology Program, National Institute of Environmental Health Sciences (NIEHS), National Institutes of Health (NIH), Research Triangle Park, North Carolina, United States of America.
[Ti] Título:ERα36, a variant of estrogen receptor α, is predominantly localized in mitochondria of human uterine smooth muscle and leiomyoma cells.
[So] Source:PLoS One;12(10):e0186078, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ERα36 is a naturally occurring, membrane-associated, isoform of estrogen receptor α. The expression of ERα36 is due to alternative splicing and different promoter usage. ERα36 is a dominant-negative effector of ERα66-mediated transactivational activities and has the potential to trigger membrane-initiated mitogenic, nongenomic, estrogen signaling; however, the subcellular localization of ERα36 remains controversial. To determine the cellular localization of ERα36 in estrogen-responsive human uterine smooth muscle (ht-UtSMC) and leiomyoma (fibroid; ht-UtLM) cells, we conducted systematic confocal microscopy and subcellular fractionation analysis using ERα36 antibodies. With Image J colocalizaton analysis plugin, confocal images were analyzed to obtain a Pearson's Correlation Coefficient (PCC) to quantify signal colocalization of ERα36 with mitochondrial, endoplasmic reticulum, and cytoskeletal components in both cell lines. When cells were double-stained with an ERα36 antibody and a mitochondrial-specific dye, MitoTracker, the PCC for the two channel signals were both greater than 0.75, indicating strong correlation between ERα36 and mitochondrial signals in the two cell lines. A blocking peptide competition assay confirmed that the mitochondria-associated ERα36 signal detected by confocal analysis was specific for ERα36. In contrast, confocal images double-stained with an ERα36 antibody and endoplasmic reticulum or cytoskeletal markers, had PCCs that were all less than 0.4, indicating no or very weak signal correlation. Fractionation studies showed that ERα36 existed predominantly in membrane fractions, with minimal or undetected amounts in the cytosol, nuclear, chromatin, and cytoskeletal fractions. With isolated mitochondrial preparations, we confirmed that a known mitochondrial protein, prohibitin, was present in mitochondria, and by co-immunoprecipitation analysis that ERα36 was associated with prohibitin in ht-UtLM cells. The distinctive colocalization pattern of ERα36 with mitochondria in ht-UtSMC and ht-UtLM cells, and the association of ERα36 with a mitochondrial-specific protein suggest that ERα36 is localized primarily in mitochondria and may play a pivotal role in non-genomic signaling and mitochondrial functions.
[Mh] Termos MeSH primário: Receptor alfa de Estrogênio/metabolismo
Leiomioma/metabolismo
Mitocôndrias/metabolismo
Miócitos de Músculo Liso/metabolismo
Útero/patologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Linhagem Celular Tumoral
Retículo Endoplasmático/metabolismo
Receptor alfa de Estrogênio/química
Feminino
Seres Humanos
Membranas Intracelulares/metabolismo
Leiomioma/patologia
Miócitos de Músculo Liso/patologia
Peptídeos/metabolismo
Ligação Proteica
Domínios Proteicos
Transporte Proteico
Proteínas Repressoras/metabolismo
Frações Subcelulares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Estrogen Receptor alpha); 0 (Peptides); 0 (Repressor Proteins); 0 (estrogen receptor alpha 36, human); 0 (prohibitin)
[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:171012
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186078


  10 / 20773 MEDLINE  
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[PMID]:28977034
[Au] Autor:Liu GS; Bratton BP; Gitai Z; Shaevitz JW
[Ad] Endereço:Department of Physics, Princeton University, Princeton, NJ, United States of America.
[Ti] Título:The effect of antibiotics on protein diffusion in the Escherichia coli cytoplasmic membrane.
[So] Source:PLoS One;12(10):e0185810, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulating evidence suggests that molecular motors contribute to the apparent diffusion of molecules in cells. However, current literature lacks evidence for an active process that drives diffusive-like motion in the bacterial membrane. One possible mechanism is cell wall synthesis, which involves the movement of protein complexes in the cell membrane circumferentially around the cell envelope and may generate currents in the lipid bilayer that advectively transport other transmembrane proteins. We test this hypothesis in Escherichia coli using drug treatments that slow cell wall synthesis and measure their effect on the diffusion of the transmembrane protein mannitol permease using fluorescence recovery after photobleaching. We found no clear decrease in diffusion in response to vancomycin and no decrease in response to mecillinam treatment. These results suggest that cell wall synthesis is not an active contributor to mobility in the cytoplasmic membrane.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Citoplasma/efeitos dos fármacos
Escherichia coli/efeitos dos fármacos
Membranas Intracelulares/efeitos dos fármacos
[Mh] Termos MeSH secundário: Proteínas de Escherichia coli/metabolismo
Bicamadas Lipídicas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Escherichia coli Proteins); 0 (Lipid Bilayers)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185810



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