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[PMID]:28893092
[Au] Autor:Yuan T; Chen Y; Zhang H; Fang L; Du G
[Ad] Endereço:* Beijing Key Laboratory of Drug Targets Identification and Drug Screening, Union Medical College, Beijing 100050, China.
[Ti] Título:Salvianolic Acid A, a Component of Salvia miltiorrhiza, Attenuates Endothelial-Mesenchymal Transition of HPAECs Induced by Hypoxia.
[So] Source:Am J Chin Med;45(6):1185-1200, 2017.
[Is] ISSN:0192-415X
[Cp] País de publicação:Singapore
[La] Idioma:eng
[Ab] Resumo:Salvianolic acid A (SAA), a polyphenols acid, is a bioactive ingredient from a traditional Chinese medicine called Dan shen (Salvia Miltiorrhiza Bunge). According to previous studies, it was shown to have various effects such as anti-oxidative stress, antidiabetic complications and antipulmonary hypertension. This study aimed to investigate the effect of SAA on pulmonary arterial endothelial-mesenchymal transition (EndoMT) induced by hypoxia and the underlying mechanisms. Primary cultured human pulmonary arterial endothelial cells (HPAECs) were exposed to 1% O for 48[Formula: see text]h with or without SAA treatment. SAA treatment improved the morphology of HPAECs and inhibited the cytoskeleton remodeling. A total of 3[Formula: see text][Formula: see text]M SAA reduced migration distances from 262.2[Formula: see text][Formula: see text]m to 198.4[Formula: see text][Formula: see text]m at 24[Formula: see text]h and 344.8[Formula: see text][Formula: see text]m to 109.3[Formula: see text][Formula: see text]m at 48[Formula: see text]h. It was observed that the production of ROS in cells was significantly reduced by the treatment of 3[Formula: see text][Formula: see text]M SAA. Meanwhile, SAA alleviated the loss of CD31 and slightly inhibited the expression of [Formula: see text]-SMA. The mechanisms study shows that SAA treatment increased the phosphorylation levels of Smad1/5, but inhibited that of Smad2/3. Furthermore, SAA attenuated the phosphorylation levels of ERK and Cofilin, which were enhanced by hypoxia. Based on these results, our study indicated that SAA treatment can protect HPAECs from endoMT induced by hypoxia, which may perform via the inhibition on ROS production and further through the downstream effectors of BMPRs or TGF[Formula: see text]R including Smads, ERK and ROCK/cofilin pathways.
[Mh] Termos MeSH primário: Ácidos Cafeicos/farmacologia
Células Endoteliais/patologia
Transição Epitelial-Mesenquimal/efeitos dos fármacos
Hipóxia/patologia
Lactatos/farmacologia
Salvia miltiorrhiza/química
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo
Movimento Celular/efeitos dos fármacos
Células Cultivadas
Citoesqueleto/patologia
Células Endoteliais/citologia
Células Endoteliais/metabolismo
Seres Humanos
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Fosforilação/efeitos dos fármacos
Artéria Pulmonar/citologia
Espécies Reativas de Oxigênio/metabolismo
Proteína Smad1/metabolismo
Proteína Smad2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Caffeic Acids); 0 (Lactates); 0 (Reactive Oxygen Species); 0 (SMAD1 protein, human); 0 (SMAD2 protein, human); 0 (Smad1 Protein); 0 (Smad2 Protein); 51622542XO (salvianolic acid A); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE
[do] DOI:10.1142/S0192415X17500653


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[PMID]:28826686
[Au] Autor:Peverelli E; Catalano R; Giardino E; Treppiedi D; Morelli V; Ronchi CL; Vaczlavik A; Fusco N; Ferrero S; Bertherat J; Beuschlein F; Chiodini I; Arosio M; Spada A; Mantovani G
[Ad] Endereço:Endocrine Unit, Fondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico, Milan, Italy; Department of Clinical Sciences and Community Health, University of Milan, Milan, Italy. Electronic address: erika.peverelli@guest.unimi.it.
[Ti] Título:Cofilin is a cAMP effector in mediating actin cytoskeleton reorganization and steroidogenesis in mouse and human adrenocortical tumor cells.
[So] Source:Cancer Lett;406:54-63, 2017 Oct 10.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:cAMP pathway plays a major role in the pathogenesis of cortisol-producing adrenocortical adenomas (CPA). cAMP-induced steroidogenesis is preceded by actin cytoskeleton reorganization, a process regulated by cofilin activity. In this study we investigated cofilin role in mediating cAMP effects on cell morphology and steroidogenesis in adrenocortical tumor cells. We demonstrated that forskolin induced cell rounding and strongly reduced phosphorylated (P)-cofilin/total cofilin ratio in Y1 (-52 ± 16%, p < 0.001) and human CPA cells (-53 ± 18%, p < 0.05). Cofilin silencing significantly reduced both forskolin-induced morphological changes and progesterone production (1.3-fold vs 1.8-fold in controls, p < 0.05), whereas transfection of wild-type or S3A (active), but not S3D (inactive) cofilin, potentiated forskolin effects on cell rounding and increased 3-fold progesterone synthesis with respect to control (p < 0.05). Furthermore, cofilin dephosphorylation by a ROCK inhibitor potentiated forskolin-induced cell rounding and steroidogenesis (2-fold increase vs forskolin alone). Finally, we found a reduced P-cofilin/total cofilin ratio and increased cofilin expression in CPA vs endocrine inactive adenomas by western blot and immunohistochemistry. Overall, these results identified cofilin as a mediator of cAMP effects on both morphological changes and steroidogenesis in mouse and human adrenocortical tumor cells.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Fatores de Despolimerização de Actina/metabolismo
Neoplasias do Córtex Suprarrenal/metabolismo
Adenoma Adrenocortical/metabolismo
AMP Cíclico/farmacologia
Esteroides/biossíntese
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/antagonistas & inibidores
Fatores de Despolimerização de Actina/genética
Neoplasias do Córtex Suprarrenal/tratamento farmacológico
Neoplasias do Córtex Suprarrenal/patologia
Adenoma Adrenocortical/tratamento farmacológico
Adenoma Adrenocortical/patologia
Animais
Colforsina/farmacologia
Seres Humanos
Hidrocortisona/metabolismo
Camundongos
Fosforilação/efeitos dos fármacos
RNA Interferente Pequeno/genética
Células Tumorais Cultivadas
Vasodilatadores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (RNA, Small Interfering); 0 (Steroids); 0 (Vasodilator Agents); 1F7A44V6OU (Colforsin); E0399OZS9N (Cyclic AMP); WI4X0X7BPJ (Hydrocortisone)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE


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[PMID]:28789972
[Au] Autor:Zhao Y; He L; Zhang Y; Zhao J; Liu Z; Xing F; Liu M; Feng Z; Li W; Zhang J
[Ad] Endereço:Department of Neurobiology, Chongqing Key Laboratory of Neurobiology, Third Military Medical University, Chongqing 400038, China.
[Ti] Título:Estrogen receptor alpha and beta regulate actin polymerization and spatial memory through an SRC-1/mTORC2-dependent pathway in the hippocampus of female mice.
[So] Source:J Steroid Biochem Mol Biol;174:96-113, 2017 Nov.
[Is] ISSN:1879-1220
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aging-related decline of estrogens, especially 17ß-estradiol (E2), has been shown to play an important role in the impairment of learning and memory in dementias, such as Alzheimer's disease (AD), but the underlying molecular mechanisms are poorly understood. In this study, we first demonstrated decreases in E2 signaling (aromatase, classic estrogen receptor ERα and ERß and their coactivator SRC-1), mTORC2 signaling (Rictor and phospho-AKTser473) and actin polymerization (phospho-Cofilin, Profilin-1 and the F-actin/G-actin ratio) in the hippocampus of old female mice compared with those levels detected in the adult hippocampus. We then showed that ERα and ERß antagonists induced a significant decrease in SRC-1, mTORC2 signaling, actin polymerization, and CA1 spine density, as well as impairments of learning and memory; however, ovariectomy-induced changes of these parameters could be significantly reversed by treatment with ER agonists. We further showed that expression of SRC-1, mTORC2 signaling and actin polymerization could be upregulated by E2 treatment, and the effects of E2 were blocked by the ER antagonists but mimicked by the agonists. We also showed that the lentivirus-mediated SRC-1 knockdown significantly inhibited the agonist-activated mTORC2 signaling and actin polymerization, and the lentivirus-mediated Rictor knockdown also significantly inhibited the agonist-activated actin polymerization. Finally, we demonstrated that the ERα and ERß antagonists induced a disruption in actin polymerization and an impairment of spatial memory, which were rescued by activation of mTORC2. Taken together, the above results clearly demonstrated an mTORC2-dependent regulation of actin polymerization that contributed to the effects of ERα and ERß on spatial learning, which may provide a novel target for the prevention and treatment of E2-related dementia in the aged population.
[Mh] Termos MeSH primário: Actinas/metabolismo
Receptor alfa de Estrogênio/metabolismo
Receptor beta de Estrogênio/metabolismo
Hipocampo/metabolismo
Complexos Multiproteicos/metabolismo
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo
Animais
Aromatase/metabolismo
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Linhagem Celular
Estradiol/farmacologia
Estrogênios/farmacologia
Feminino
Alvo Mecanístico do Complexo 2 de Rapamicina
Camundongos Endogâmicos C57BL
Coativador 1 de Receptor Nuclear/genética
Coativador 1 de Receptor Nuclear/metabolismo
Ovariectomia
Polimerização
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteína Companheira de mTOR Insensível à Rapamicina
Memória Espacial/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Actins); 0 (Carrier Proteins); 0 (Estrogen Receptor alpha); 0 (Estrogen Receptor beta); 0 (Estrogens); 0 (Multiprotein Complexes); 0 (Rapamycin-Insensitive Companion of mTOR Protein); 0 (rictor protein, mouse); 4TI98Z838E (Estradiol); EC 1.14.14.1 (Aromatase); EC 2.3.1.48 (Ncoa1 protein, mouse); EC 2.3.1.48 (Nuclear Receptor Coactivator 1); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 2); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE


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[PMID]:28787434
[Au] Autor:Shi C; Ren L; Sun C; Yu L; Bian X; Zhou X; Wen Y; Hua D; Zhao S; Luo W; Wang R; Rao C; Wang Q; Yu S
[Ad] Endereço:Department of Neuropathology, Tianjin Neurological Institute, Tianjin Medical University General Hospital, Tianjin 300052, China.
[Ti] Título:miR-29a/b/c function as invasion suppressors for gliomas by targeting CDC42 and predict the prognosis of patients.
[So] Source:Br J Cancer;117(7):1036-1047, 2017 Sep 26.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The lethality and poor outcome of high-grade gliomas result from the tumour relentless invasion. miR-29a/b/c downexpressions contribute to several human tumourigenesis. However, their relevance to prognosis and invasion in gliomas remains unclear. METHODS: Relationships of miR-29a/b/c and CDC42 expressions to grade and survival-time in 147 human gliomas were analysed by in situ hybridisation and immunohistochemistry. Dual-luciferase reporter assay was used to identify CDC42 as a target of miR-29a/b/c. Underlining mechanisms by which miR-29a/b/c inhibited glioma cell migration and invasion were studied by in vitro and in vivo assays. RESULTS: miR-29a/b/c expressions were inversely correlated with glioma grades, but positively correlated with patients' survival. Two distinct subgroups of grade I-IV glioma patients with different prognoses were identified according to miR-29a/b/c expressions. miR-29a/b/c overexpressions suppressed glioma cell migration and invasion through targeting CDC42 and subsequently decreasing phosphorylated PAK1/2/3, LIMK1/2 and cofilin, the pivotal downstream effectors of CDC42. Moreover, CDC42 expression was positively correlated with glioma grades, but inversely correlated with miR-29a/b/c expressions and patients' survival. In glioblastoma cell lines, CDC42-knockdown could mimic the anti-tumour effects of miR-29a/b/c. CONCLUSIONS: miR-29a/b/c are important tumour suppressors and novel prognostic biomarkers of gliomas, and miR-29a/b/c and CDC42 are potential therapeutic candidates for malignant gliomas.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/genética
Glioma/genética
MicroRNAs/análise
MicroRNAs/genética
Proteína cdc42 de Ligação ao GTP/análise
Proteína cdc42 de Ligação ao GTP/genética
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo
Animais
Química Encefálica
Neoplasias Encefálicas/química
Neoplasias Encefálicas/metabolismo
Linhagem Celular Tumoral
Movimento Celular/genética
Intervalo Livre de Doença
Expressão Gênica
Inativação Gênica
Glioma/química
Glioma/metabolismo
Seres Humanos
Quinases Lim/metabolismo
Camundongos
Gradação de Tumores
Invasividade Neoplásica
Transplante de Neoplasias
Taxa de Sobrevida
Transfecção
Quinases Ativadas por p21/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (MIRN29 microRNA, human); 0 (MicroRNAs); EC 2.7.11.1 (Lim Kinases); EC 2.7.11.1 (p21-Activated Kinases); EC 3.6.5.2 (cdc42 GTP-Binding Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.255


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[PMID]:28720653
[Au] Autor:Dimri M; Bilogan C; Pierce LX; Naegele G; Vasanji A; Gibson I; McClendon A; Tae K; Sakaguchi TF
[Ad] Endereço:Department of Stem Cell Biology and Regenerative Medicine, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
[Ti] Título:Three-dimensional structural analysis reveals a Cdk5-mediated kinase cascade regulating hepatic biliary network branching in zebrafish.
[So] Source:Development;144(14):2595-2605, 2017 07 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The intrahepatic biliary network is a highly branched three-dimensional network lined by biliary epithelial cells, but how its branching patterns are precisely established is not clear. We designed a new computer-based algorithm that quantitatively computes the structural differences of the three-dimensional networks. Utilizing the algorithm, we showed that inhibition of Cyclin-dependent kinase 5 (Cdk5) led to reduced branching in the intrahepatic biliary network in zebrafish. Further, we identified a previously unappreciated downstream kinase cascade regulated by Cdk5. Pharmacological manipulations of this downstream kinase cascade produced a crowded branching defect in the intrahepatic biliary network and influenced actin dynamics in biliary epithelial cells. We generated larvae carrying a mutation in ( ), an essential activator of Cdk5. mutant larvae show similar branching defects as those observed in Cdk5 inhibitor-treated larvae. A small-molecule compound that interferes with the downstream kinase cascade rescued the mutant phenotype. These results provide new insights into branching morphogenesis of the intrahepatic biliary network.
[Mh] Termos MeSH primário: Ductos Biliares Intra-Hepáticos/enzimologia
Ductos Biliares Intra-Hepáticos/crescimento & desenvolvimento
Quinase 5 Dependente de Ciclina/metabolismo
Proteínas de Peixe-Zebra/metabolismo
Peixe-Zebra/crescimento & desenvolvimento
Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo
Algoritmos
Animais
Animais Geneticamente Modificados
Simulação por Computador
Quinase 5 Dependente de Ciclina/antagonistas & inibidores
Quinase 5 Dependente de Ciclina/genética
Técnicas de Inativação de Genes
Imagem Tridimensional
Larva/crescimento & desenvolvimento
Larva/metabolismo
Quinases Lim/metabolismo
Modelos Anatômicos
Morfogênese/efeitos dos fármacos
Morfogênese/genética
Morfogênese/fisiologia
Mutação
Inibidores de Proteínas Quinases/farmacologia
Transdução de Sinais
Peixe-Zebra/genética
Proteínas de Peixe-Zebra/antagonistas & inibidores
Proteínas de Peixe-Zebra/genética
Quinases Ativadas por p21/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Protein Kinase Inhibitors); 0 (Zebrafish Proteins); EC 2.7.11.1 (Cyclin-Dependent Kinase 5); EC 2.7.11.1 (Lim Kinases); EC 2.7.11.1 (p21-Activated Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE
[do] DOI:10.1242/dev.147397


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[PMID]:28636918
[Au] Autor:Schramm AC; Hocky GM; Voth GA; Blanchoin L; Martiel JL; De La Cruz EM
[Ad] Endereço:Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut.
[Ti] Título:Actin Filament Strain Promotes Severing and Cofilin Dissociation.
[So] Source:Biophys J;112(12):2624-2633, 2017 Jun 20.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Computational and structural studies have been indispensable in investigating the molecular origins of actin filament mechanical properties and modulation by the regulatory severing protein cofilin. All-atom molecular dynamics simulations of cofilactin filament structures determined by electron cryomicroscopy reveal how cofilin enhances the bending and twisting compliance of actin filaments. Continuum mechanics models suggest that buckled cofilactin filaments localize elastic energy at boundaries between bare and cofilin-decorated segments because of their nonuniform elasticity, thereby accelerating filament severing. Here, we develop mesoscopic length-scale (cofil)actin filament models and evaluate the effects of compressive and twisting loads on strain energy distribution at specific interprotein interfaces. The models reliably capture the filament bending and torsional rigidities and intersubunit torsional flexibility measured experimentally with purified protein components. Buckling is predicted to enhance cofilactin filament severing with minimal effects on cofilin occupancy, whereas filament twisting enhances cofilin dissociation without compromising filament integrity. Preferential severing at actin-cofilactin boundaries of buckled filaments is more prominent than predicted by continuum models because of the enhanced spatial resolution. The models developed here will be valuable for evaluating the effects of filament shape deformations on filament stability and interactions with regulatory proteins, and analysis of single filament manipulation assays.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Fatores de Despolimerização de Actina/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/química
Fatores de Despolimerização de Actina/química
Actinas/química
Actinas/metabolismo
Microscopia Crioeletrônica
Elasticidade
Simulação de Dinâmica Molecular
Ligação Proteica
Rotação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Actins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170823
[Lr] Data última revisão:
170823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE


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[PMID]:28586109
[Au] Autor:Ramírez-Valadez KA; Vázquez-Victorio G; Macías-Silva M; González-Espinosa C
[Ad] Endereço:Departamento de Farmacobiología, Centro de Investigación y de Estudios Avanzados del IPN, México.
[Ti] Título:Fyn kinase mediates cortical actin ring depolymerization required for mast cell migration in response to TGF-ß in mice.
[So] Source:Eur J Immunol;47(8):1305-1316, 2017 Aug.
[Is] ISSN:1521-4141
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Transforming growth factor-ß (TGF-ß) is a potent mast cell (MC) chemoattractant able to modulate local inflammatory reactions. The molecular mechanism leading to TGF-ß-directed MC migration is not fully described. Here we analyzed the role of the Src family protein kinase Fyn on the main TGF-ß-induced cytoskeletal changes leading to MC migration. Utilizing bone marrow-derived mast cells (BMMCs) from WT and Fyn-deficient mice we found that BMMC migration to TGF-ß was impaired in the absence of the kinase. TGF-ß caused depolymerization of the cortical actin ring and changes on the phosphorylation of cofilin, LIMK and CAMKII only in WT cells. Defective cofilin activation and phosphorylation of regulatory proteins was detected in Fyn-deficient BMMCs and this finding correlated with a lower activity of the catalytic subunit of the phosphatase PP2A. Diminished TGF-ß-induced chemotaxis of Fyn-deficient cells was also observed in an in vivo model of MC migration (bleomycin-induced scleroderma). Our results show that Fyn kinase is an important positive effector of TGF-ß-induced chemotaxis through the control of PP2A activity and this is relevant to pathological processes that are related to TGF-ß-dependent mast cell migration.
[Mh] Termos MeSH primário: Actinas/metabolismo
Quimiotaxia
Mastócitos/fisiologia
Proteínas Proto-Oncogênicas c-fyn/metabolismo
Fator de Crescimento Transformador beta/fisiologia
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo
Animais
Mastócitos/imunologia
Camundongos
Ácido Okadáico/farmacologia
Fosforilação
Proteína Fosfatase 2/metabolismo
Proteínas Proto-Oncogênicas c-fyn/genética
Transdução de Sinais
Proteína Smad2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Actins); 0 (Smad2 Protein); 0 (Smad2 protein, mouse); 0 (Transforming Growth Factor beta); 1W21G5Q4N2 (Okadaic Acid); EC 2.7.10.2 (Fyn protein, mouse); EC 2.7.10.2 (Proto-Oncogene Proteins c-fyn); EC 3.1.3.16 (Protein Phosphatase 2)
[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:170607
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201646876


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[PMID]:28513458
[Au] Autor:Ostrowska Z; Moraczewska J
[Ad] Endereço:Zaklad Biochemii i Biologii Komórki, Wydzial Nauk Przyrodniczych, Uniwersytet Kazimierza Wielkiego w Bydgoszczy.
[Ti] Título:Cofilin - a protein controlling dynamics of actin filaments.
[So] Source:Postepy Hig Med Dosw (Online);71(0):339-351, 2017 May 05.
[Is] ISSN:1732-2693
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Cofilins are evolutionary conserved proteins present in all Eukaryotic cells. Their primary function is dynamic reorganization of actin cytoskeleton. Two cofilin isoforms are known: cofilin 1, present in all studied non-muscle cells and in embryonic muscle cells, and cofilin 2, which dominates in mature skeletal and cardiac muscles. Polypeptide chains of both isoforms fold into a structure homological to a conservative ADF (actin depolymerizing factor) domain, which is characteristic of actin depolymerizing factor. In cofilin molecule two actin-binding sites were found. One site binds monomeric and filamentous actin, the second one interacts only with the filament. Binding of cofilin to actin filament causes a change in the orientation of subunits, which results in filament severing. This increases number of ends which can either elongate or shorten the filament, depending on the conditions. Cofilin interactions with monomeric actin decreases availability of polymerization-competent actin subunits. Cofilin activity is controlled by phosphorylation, binding membrane phospholipids, local pH and oxidative stress. Under conditions of oxidative stress oxidation of cysteine residues leads to formation of dimers, which are able to cross-link actin filaments. Stable actin-cofilin rods save cellular ATP, which is not used during active polymerization process. This facilitates faster cell recovery from the stress. The final cellular reaction on the environmental stimuli is a resultant of cofilin activity and activities of other actin-binding proteins, which function either synergistically or antagonistically. Due to the central role in the regulation of actin filaments dynamics, cofilin is involved in development of cancer, neurodegenerative diseases, congenital myopathies and cardiomyopathies.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Fatores de Despolimerização de Actina/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Seres Humanos
Polimerização
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Actins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE


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[PMID]:28487281
[Au] Autor:Wang H; Guo J; Lin Z; Namgoong S; Oh JS; Kim NH
[Ad] Endereço:Department of Animal Sciences, Chungbuk National University, Cheongju, South Korea.
[Ti] Título:Filamin A is required for spindle migration and asymmetric division in mouse oocytes.
[So] Source:FASEB J;31(8):3677-3688, 2017 Aug.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dynamic changes in the actin network are crucial for the cortical migration of spindles and establishment of polarity, to ensure asymmetric division during meiotic maturation. In this study, filamin A (FLNA) was found to be an essential actin regulator that controlled spindle migration and asymmetric division during oocyte meiosis. FLNA was localized in the cytoplasm and enriched at the cortex and near the chromosomes. Knockdown of FLNA impaired meiotic asymmetric division and spindle migration with a decrease in the amount of cytoplasmic actin mesh and cortical actin levels. Moreover, FLNA knockdown reduced the phosphorylation of cofilin and Rho kinase (ROCK) near the spindle. Similar phenotypes, such as decreased filament actin levels, impaired spindle migration and polar body extrusion, were observed when active cofilin (S3A) was overexpressed or ROCK was inhibited. Notably, we found that FLNA and ROCK interacted directly in mouse oocytes. Taken together, our results show that FLNA plays crucial roles in asymmetric division during meiotic maturation by regulating ROCK-cofilin-mediated actin reorganization.-Wang, H., Guo J., Lin, Z., Namgoong, S., Oh, J. S., Kim, N.-H. Filamin A is required for spindle migration and asymmetric division in mouse oocytes.
[Mh] Termos MeSH primário: Divisão Celular/fisiologia
Filaminas/metabolismo
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Oócitos/fisiologia
Fuso Acromático/fisiologia
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/genética
Fatores de Despolimerização de Actina/metabolismo
Actinas/metabolismo
Animais
Clonagem Molecular
Citoplasma/química
Feminino
Filaminas/genética
Técnicas de Silenciamento de Genes
Camundongos
Oócitos/citologia
Transporte Proteico
Quinases Associadas a rho/genética
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Actins); 0 (Filamins); EC 2.7.11.1 (rho-Associated Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170511
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201700056R


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[PMID]:28422872
[Au] Autor:Zhang Y; Wang J; Ji H; Lu H; Lu L; Wang J; Li Y
[Ad] Endereço:Department of General Surgery, The Second Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi, China.
[Ti] Título:Effect of HSP27 and Cofilin in the injury of hypoxia/reoxygenation on hepatocyte membrane F-actin microfilaments.
[So] Source:Medicine (Baltimore);96(16):e6658, 2017 Apr.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hypoxia-reoxygenation (H/R) injury hepatocyte models were established to simulate the ischemia/reperfusion injury of transplanted organ. Through the study of the molecular mechanism of H/R on the F-actin damage of the liver cytomembrane, the mechanism of F-actin damage induced by ischemia and reperfusion was studied from the level of cell and molecule.The hypoxic environment of cells in vitro was simulated by chemical hypoxia agent CoCl2. Liver cells were detected by MTT, H/R group was subdivided into 3 subgroups: H/R 2, 4, and 6 h. Changes of cell shape and the growth state, apoptosis, ultrastructural changes, and the changes in F-actin microfilament content were observed. Heat shock protein 27 (HSP27), Cofilin, and F-actin gene and protein levels were determined by real-time polymerase chain reaction and western blot assay, respectively.Cells showed circular adherence growth under normal circumstances, while the spindle cells and shedding cells were significantly increased in H/R groups. Apoptosis cells in H/R group were increased significantly with the extension of hypoxia time. The number of endoplasmic reticulum was decreased significantly in the H/R group, the mitochondrion hydropic was degenerated and the glycogen was disappeared. The F-actin fibers in the H/R group were disordered, the morphology of the fibers was obviously decreased, and the fluorescence staining decreased obviously (P < .05). The transcription and expression levels of HSP27, Cofilin, and F-actin were significantly lower than those in the control group (P < .05).These results demonstrate that H/R can affect the correct assembly of F-actin microfilaments and weakens the normal cycle of F-actin microfilaments through inhibiting the protein expression and gene transcription of HSP27 and Cofilin in hepatocytes, thereby changing the skeleton of F-actin microfilaments.
[Mh] Termos MeSH primário: Fatores de Despolimerização de Actina/biossíntese
Actinas/biossíntese
Proteínas de Choque Térmico HSP27/biossíntese
Hepatócitos/efeitos dos fármacos
Traumatismo por Reperfusão/patologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Crescimento Celular
Forma Celular
Modelos Animais de Doenças
Hepatócitos/metabolismo
Hepatócitos/ultraestrutura
Seres Humanos
RNA Mensageiro
Ratos
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Actin Depolymerizing Factors); 0 (Actins); 0 (HSP27 Heat-Shock Proteins); 0 (RNA, Messenger)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000006658



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