Base de dados : MEDLINE
Pesquisa : D08.811.277.040.025.142.750.500 [Categoria DeCS]
Referências encontradas : 348 [refinar]
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[PMID]:28973494
[Au] Autor:Zhao X; Xiu J; Li Y; Ma H; Wu J; Wang B; Guo G
[Ad] Endereço:Department of parasitology, School of Basic Medical Sciences, Guizhou Medical University, Guiyang, University City Guian New District, 550025, China.
[Ti] Título:Characterization and Expression Pattern Analysis of the T-Complex Protein-1 Zeta Subunit in Musca domestica L (Diptera).
[So] Source:J Insect Sci;17(4), 2017 Jul 01.
[Is] ISSN:1536-2442
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chaperonins, belonging to the T-complex protein-1 (TCP-1) family, assist in the correct folding of nascent and misfolded proteins. It is well-known that in mammals, the zeta subunit of the TCP-1 complex (TCP-1ζ) plays a vital role in the folding and assembly of cytoskeleta proteins. This study reported for the first time the cloning, characterization and expression pattern analysis of the TCP-1ζ from Musca domestica, which was named as MdTCP-1ζ. The MdTCP-1ζ cDNA is 1,803 bp long with a 1,596 bp open reading frame that encodes a protein with 531 bp amino acids. The analysis of the transcriptional profile of MdTCP-1ζ using qRT-PCR revealed relatively high expression in the salivary glands and trachea at the tissues while among the developmental stages. The highest expression was observed only in the eggs suggesting that the MdTCP-1ζ may play a role in embryonic development. The expression of MdTCP-1ζ was also significantly induced after exposure to short-term heat shock and infection by Escherichia coli, Staphylococcus aureus, or Candida albicans. This suggested that MdTCP-1ζ may take part in the immune responses of housefly and perhaps contribute to the protection against cellular injury.
[Mh] Termos MeSH primário: Chaperonina com TCP-1/metabolismo
Moscas Domésticas/metabolismo
[Mh] Termos MeSH secundário: Animais
Chaperonina com TCP-1/química
Feminino
Expressão Gênica
Moscas Domésticas/crescimento & desenvolvimento
Moscas Domésticas/imunologia
Proteínas de Insetos/química
Proteínas de Insetos/metabolismo
Larva/imunologia
Larva/metabolismo
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1093/jisesa/iex063


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[PMID]:28375158
[Au] Autor:Ying Z; Tian H; Li Y; Lian R; Li W; Wu S; Zhang HZ; Wu J; Liu L; Song J; Guan H; Cai J; Zhu X; Li J; Li M
[Ti] Título:CCT6A suppresses SMAD2 and promotes prometastatic TGF-ß signaling.
[So] Source:J Clin Invest;127(5):1725-1740, 2017 May 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Paradoxically, during early tumor development in many cancer types, TGF-ß acts as a tumor suppressor, whereas in the advanced stages of these cancers, increased TGF-ß expression is linked to high metastasis and poor prognosis. These findings suggest that unidentified mechanisms may function to rewire TGF-ß signaling toward its prometastatic role in cancer cells. Our current study using non-small-cell lung carcinoma (NSCLC) cell lines, animal models, and clinical specimens demonstrates that suppression of SMAD2, with SMAD3 function intact, switches TGF-ß-induced transcriptional responses to a prometastatic state. Importantly, we identified chaperonin containing TCP1 subunit 6A (CCT6A) as an inhibitor and direct binding protein of SMAD2 and found that CCT6A suppresses SMAD2 function in NSCLC cells and promotes metastasis. Furthermore, selective inhibition of SMAD3 or CCT6A efficiently suppresses TGF-ß-mediated metastasis. Our findings provide a mechanism that directs TGF-ß signaling toward its prometastatic arm and may contribute to the development of therapeutic strategies targeting TGF-ß for NSCLC.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/metabolismo
Chaperonina com TCP-1/metabolismo
Neoplasias Pulmonares/metabolismo
Transdução de Sinais
Proteína Smad2/metabolismo
Fator de Crescimento Transformador beta/metabolismo
[Mh] Termos MeSH secundário: Animais
Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/patologia
Linhagem Celular Tumoral
Chaperonina com TCP-1/genética
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/patologia
Camundongos
Metástase Neoplásica
Proteína Smad2/genética
Proteína Smad3/genética
Proteína Smad3/metabolismo
Fator de Crescimento Transformador beta/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCT6A protein, human); 0 (CCT6A protein, mouse); 0 (SMAD2 protein, human); 0 (SMAD3 protein, human); 0 (Smad2 Protein); 0 (Smad2 protein, mouse); 0 (Smad3 Protein); 0 (Smad3 protein, mouse); 0 (Transforming Growth Factor beta); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE


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[PMID]:27806916
[Au] Autor:Araki K; Suenaga A; Kusano H; Tanaka R; Hatta T; Natsume T; Fukui K
[Ad] Endereço:Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan. Electronic address: k-araki@aist.go.jp.
[Ti] Título:Functional profiling of asymmetrically-organized human CCT/TRiC chaperonin.
[So] Source:Biochem Biophys Res Commun;481(3-4):232-238, 2016 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Molecular organization of the eukaryote chaperonin known as CCT/TRiC complex was recently clarified. Eight distinct subunits are uniquely organized, providing a favorable folding cavity for specific client proteins such as tubulin and actin. Because of its heterogeneous subunit composition, CCT complex has polarized inner faces, which may underlie an essential part of its chaperonin function. In this study, we structurally characterized the closed and open states of CCT complex, using molecular dynamics analyses. Our results showed that the inter-subunit interaction energies were asymmetrically distributed and were remodeled during conformational changes of CCT complex. In addition, exploration of redox related characteristics indicated changes in inner surface properties, including electrostatic potential, pK and exposure of inner cysteine thiol groups, between the closed and open states. Cysteine activation events were experimentally verified by interaction analyses, using tubulin as a model substrate. Our data highlighted the importance of dynamics-based structural profiling of asymmetrically oriented chaperonin function.
[Mh] Termos MeSH primário: Chaperonina com TCP-1/metabolismo
[Mh] Termos MeSH secundário: Chaperonina com TCP-1/química
Simulação por Computador
Cisteína/metabolismo
Células HEK293
Seres Humanos
Modelos Moleculares
Oxirredução
Ligação Proteica
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Eletricidade Estática
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); EC 3.6.1.- (Chaperonin Containing TCP-1); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161104
[St] Status:MEDLINE


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[PMID]:27708139
[Au] Autor:Génier S; Degrandmaison J; Moreau P; Labrecque P; Hébert TE; Parent JL
[Ad] Endereço:Service de Rhumatologie, Département de Médecine, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, Centre de Recherche du Centre Hospitalier Universitaire de Sherbrooke (CR-CHUS), and Institut de Pharmacologie de Sherbrooke, Sherbrooke, QC J1H 5N4, Canada.
[Ti] Título:Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex.
[So] Source:Mol Biol Cell;27(24):3800-3812, 2016 Dec 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mechanisms that prevent aggregation and promote folding of nascent G protein-coupled receptors (GPCRs) remain poorly understood. We identified chaperonin containing TCP-1 subunit eta (CCT7) as an interacting partner of the ß-isoform of thromboxane A receptor (TPß) by yeast two-hybrid screening. CCT7 coimmunoprecipitated with overexpressed TPß and ß -adrenergic receptor (ß AR) in HEK 293 cells, but also with endogenous ß AR. CCT7 depletion by small interfering RNA reduced total and cell-surface expression of both receptors and caused redistribution of the receptors to juxtanuclear aggresomes, significantly more so for TPß than ß AR. Interestingly, Hsp90 coimmunoprecipitated with ß AR but virtually not with TPß, indicating that nascent GPCRs can adopt alternative folding pathways. In vitro pull-down assays showed that both receptors can interact directly with CCT7 through their third intracellular loops and C-termini. We demonstrate that Trp in the TPß C-terminus is critical for the CCT7 interaction and plays an important role in TPß maturation and cell-surface expression. Of note, introducing a tryptophan in the corresponding position of the TPα isoform confers the CCT7-binding and maturation properties of TPß. We show that an interaction with a subunit of the CCT/TCP-1 ring complex (TRiC) chaperonin complex is involved in regulating aggregation of nascent GPCRs and in promoting their proper maturation and expression.
[Mh] Termos MeSH primário: Chaperonina com TCP-1/metabolismo
Receptores de Tromboxano A2 e Prostaglandina H2/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte/metabolismo
Membrana Celular/metabolismo
Chaperonina com TCP-1/fisiologia
Células HEK293
Seres Humanos
Imunoprecipitação
Ligação Proteica
Isoformas de Proteínas/metabolismo
RNA Interferente Pequeno/metabolismo
Receptores Adrenérgicos beta 2/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
Receptores de Tromboxano A2 e Prostaglandina H2/fisiologia
Transdução de Sinais
Transfecção
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCT7 protein, human); 0 (Carrier Proteins); 0 (Protein Isoforms); 0 (RNA, Small Interfering); 0 (Receptors, Adrenergic, beta-2); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Thromboxane A2, Prostaglandin H2); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161007
[St] Status:MEDLINE


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[PMID]:27686496
[Au] Autor:Korobko I; Nadler-Holly M; Horovitz A
[Ad] Endereço:Department of Structural Biology, Weizmann Institute of Science, Rehovot 7610001, Israel.
[Ti] Título:Transient Kinetic Analysis of ATP Hydrolysis by the CCT/TRiC Chaperonin.
[So] Source:J Mol Biol;428(22):4520-4527, 2016 Nov 06.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The chaperonin-containing t-complex polypeptide 1 (CCT, also known as TRiC) assists protein folding in an ATP-dependent manner. CCT/TRiC was mixed rapidly with different concentrations of ATP, and the amount of phosphate formed upon ATP hydrolysis was measured as a function of time using the coumarin-labeled phosphate-binding protein method. Two burst phases were observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis. The phases were assigned by (i) determining their dependence on ATP and K concentrations and (ii) by measuring their sensitivity to the mutation Gly345→Asp in subunit CCT4, which decreases cooperativity in ATP binding. The values of the observed rate constants corresponding to the burst phases are found to decrease with increasing ATP and K concentrations, thereby indicating that the apo state of CCT/TRiC is in equilibrium between several conformations and that "conformational selection" by ATP takes place before hydrolysis. The amplitude of the lag phase, which follows, decreases with increasing ATP concentrations, thus indicating that it reflects a transition between states with low affinity for ATP and a state with high affinity for ATP that is predominant under steady-state conditions. A kinetic model based on the data is suggested, in which CCT/TRiC is in equilibrium between a relatively large number of states that are distinguished kinetically, in agreement with its proposed sequential allosteric mechanism.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Trifosfato de Adenosina/metabolismo
Chaperonina com TCP-1/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Chaperonina com TCP-1/genética
Hidrólise
Cinética
Potássio/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCT4 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (Chaperonin Containing TCP-1); RWP5GA015D (Potassium)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170917
[Lr] Data última revisão:
170917
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161001
[St] Status:MEDLINE


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[PMID]:27489109
[Au] Autor:Chen H; You H; Wang L; Zhang X; Zhang J; He W
[Ad] Endereço:From the Department of Immunology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and School of Basic Medicine, Peking Union Medical College, State Key Laboratory of Medical Molecular Biology, Beijing 100005, China and.
[Ti] Título:Chaperonin-containing T-complex Protein 1 Subunit ζ Serves as an Autoantigen Recognized by Human Vδ2 γδ T Cells in Autoimmune Diseases.
[So] Source:J Biol Chem;291(38):19985-93, 2016 Sep 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human γδ T cells recognize conserved endogenous and stress-induced antigens typically associated with autoimmune diseases. However, the role of γδ T cells in autoimmune diseases is not clear. Few autoimmune disease-related antigens recognized by T cell receptor (TCR) γδ have been defined. In this study, we compared Vδ2 TCR complementarity-determining region 3 (CDR3) between systemic lupus erythematosus (SLE) patients and healthy donors. Results show that CDR3 length distribution differed significantly and displayed oligoclonal characteristics in SLE patients when compared with healthy donors. We found no difference in the frequency of Jδ gene fragment usage between these two groups. According to the dominant CDR3δ sequences in SLE patients, synthesized SL2 peptides specifically bound to human renal proximal tubular epithelial cell line HK-2; SL2-Vm, a mutant V sequence of SL2, did not bind. We identified the putative protein ligand chaperonin-containing T-complex protein 1 subunit ζ (CCT6A) using SL2 as a probe in HK-2 cell protein extracts by affinity chromatography and liquid chromatography-electrospray ionization-tandem mass spectrometry analysis. We found CCT6A expression on the surface of HK-2 cells. Cytotoxicity of only Vδ2 γδ T cells to HK-2 cells was blocked by anti-CCT6A antibody. Finally, we note that CCT6A concentration was significantly increased in plasma of SLE and rheumatoid arthritis patients. These data suggest that CCT6A is a novel autoantigen recognized by Vδ2 γδ T cells, which deepens our understanding of mechanisms in autoimmune diseases.
[Mh] Termos MeSH primário: Autoantígenos/imunologia
Chaperonina com TCP-1/imunologia
Regiões Determinantes de Complementaridade/imunologia
Regulação da Expressão Gênica/imunologia
Lúpus Eritematoso Sistêmico/imunologia
Receptores de Antígenos de Linfócitos T gama-delta/imunologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Autoantígenos/genética
Linhagem Celular
Chaperonina com TCP-1/genética
Regiões Determinantes de Complementaridade/genética
Feminino
Seres Humanos
Lúpus Eritematoso Sistêmico/genética
Masculino
Meia-Idade
Receptores de Antígenos de Linfócitos T gama-delta/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantigens); 0 (CCT6A protein, human); 0 (Complementarity Determining Regions); 0 (Receptors, Antigen, T-Cell, gamma-delta); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170916
[Lr] Data última revisão:
170916
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160805
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.700070


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[PMID]:27276256
[Au] Autor:Roh SH; Kasembeli MM; Galaz-Montoya JG; Chiu W; Tweardy DJ
[Ad] Endereço:Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas.
[Ti] Título:Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.
[So] Source:Biophys J;110(11):2377-2385, 2016 Jun 07.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AML1-ETO is the translational product of a chimeric gene created by the stable chromosome translocation t (8;21)(q22;q22). It causes acute myeloid leukemia (AML) by dysregulating the expression of genes critical for myeloid cell development and differentiation and recently has been reported to bind multiple subunits of the mammalian cytosolic chaperonin TRiC (or CCT), primarily through its DNA binding domain (AML1-175). Through these interactions, TRiC plays an important role in the synthesis, folding, and activity of AML1-ETO. Using single-particle cryo-electron microscopy, we demonstrate here that a folding intermediate of AML1-ETO's DNA-binding domain (AML1-175) forms a stable complex with apo-TRiC. Our structure reveals that AML1-175 associates directly with a specific subset of TRiC subunits in the open conformation.
[Mh] Termos MeSH primário: Chaperonina com TCP-1/metabolismo
Subunidade alfa 2 de Fator de Ligação ao Core/metabolismo
Proteínas de Fusão Oncogênicas/metabolismo
[Mh] Termos MeSH secundário: Western Blotting
Cromatografia em Gel
Microscopia Crioeletrônica
DNA/metabolismo
Compostos de Ouro
Proteínas de Choque Térmico HSP70/metabolismo
Células HeLa
Seres Humanos
Imagem Tridimensional
Espectrometria de Massas
Nanopartículas Metálicas
Domínios Proteicos
Dobramento de Proteína
Multimerização Proteica
Estabilidade Proteica
Proteína 1 Parceira de Translocação de RUNX1
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AML1-ETO fusion protein, human); 0 (Core Binding Factor Alpha 2 Subunit); 0 (Gold Compounds); 0 (HSP70 Heat-Shock Proteins); 0 (Oncogene Proteins, Fusion); 0 (RUNX1 Translocation Partner 1 Protein); 9007-49-2 (DNA); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE


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[PMID]:27101149
[Au] Autor:Yin H; Miao X; Wu Y; Wei Y; Zong G; Yang S; Chen X; Zheng G; Zhu X; Guo Y; Li C; Chen Y; Wang Y; He S
[Ad] Endereço:Department of Pathology, Affiliated Cancer Hospital of Nantong University, Nantong 226361, Jiangsu, China.
[Ti] Título:The role of the Chaperonin containing t-complex polypeptide 1, subunit 8 (CCT8) in B-cell non-Hodgkin's lymphoma.
[So] Source:Leuk Res;45:59-67, 2016 Jun.
[Is] ISSN:1873-5835
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The chaperonin containing t-complex polypeptide 1 (CCT) is known to mediate folding of proteins. CCT, subunit 8 (CCT8), is the θ subunit of CCT complex chaperonin. CCT8 has been reported to be dysregulated in several tumor tissues. In this study, we investigated the role of CCT8 in B-cell non-Hodgkin's lymphoma (NHL). Clinically, the expression levels of CCT8 in reactive lymphoid hyperplasia (RLH) and B-cell NHL specimens were investigated using immunohistochemical analysis. We found that CCT8 was highly expressed in proliferating germinal center cells compared with the quiescent cells of the follicular mantle zone. Furthermore, CCT8 was highly expressed in progressive lymphomas than in indolent lymphomas. Kaplan-Meier curve showed that high expression of CCT8 was significantly associated with shorter overall survival in patients with diffuse large B-cell lymphoma. Moreover, we demonstrated that CCT8 could promote the proliferation of B-cell NHL cells. In addition, we found that CCT8 could accelerate the G1/S transition in B-cell NHL. Finally, we demonstrated that overexpression of CCT8 could reverse cell adhesion-mediated drug resistance (CAM-DR) phenotype. Our study may shed new insights into the important role of CCT8 in cancer development.
[Mh] Termos MeSH primário: Chaperonina com TCP-1/fisiologia
Linfoma de Células B/química
[Mh] Termos MeSH secundário: Idoso
Adesão Celular
Ciclo Celular
Linhagem Celular Tumoral
Proliferação Celular
Chaperonina com TCP-1/análise
Progressão da Doença
Resistência a Medicamentos Antineoplásicos
Feminino
Centro Germinativo/química
Centro Germinativo/patologia
Seres Humanos
Imuno-Histoquímica/métodos
Linfoma de Células B/patologia
Masculino
Meia-Idade
Taxa de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (CCT8 protein, human); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160422
[St] Status:MEDLINE


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[PMID]:26739059
[Au] Autor:Zhang Y; Wang Y; Wei Y; Wu J; Zhang P; Shen S; Saiyin H; Wumaier R; Yang X; Wang C; Yu L
[Ad] Endereço:State Key Laboratory of Genetic Engineering, Collaborative Innovation Center for Genetics and Development, School of Life Sciences, Fudan University, 2005 Songhu Road, Shanghai 200433, China; State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese academy of Sciences, 55
[Ti] Título:Molecular chaperone CCT3 supports proper mitotic progression and cell proliferation in hepatocellular carcinoma cells.
[So] Source:Cancer Lett;372(1):101-9, 2016 Mar 01.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:CCT3 was one of the subunits of molecular chaperone CCT/TRiC complex, which plays a central role in maintaining cellular proteostasis. We demonstrated that expressions of CCT3 mRNA and protein are highly up-regulated in hepatocellular carcinoma (HCC) tissues, and high level of CCT3 is correlated with poor survival in cancer patients. In HCC cell lines, CCT3 depletion suppresses cell proliferation by inducing mitotic arrest at prometaphase and apoptosis eventually. We also identified CCT3 as a novel regulator of spindle integrity and as a requirement for proper kinetochore-microtubule attachment during mitosis. Moreover, we found that CCT3 depletion sensitizes HCC cells to microtubule destabilizing drug Vincristine. Collectively, our study suggests that CCT3 is indispensible for HCC cell proliferation, and provides a potential drug target for treatment of HCC.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/metabolismo
Proliferação Celular
Chaperonina com TCP-1/metabolismo
Neoplasias Hepáticas/metabolismo
Mitose
[Mh] Termos MeSH secundário: Antineoplásicos Fitogênicos/farmacologia
Apoptose
Carcinoma Hepatocelular/tratamento farmacológico
Carcinoma Hepatocelular/genética
Carcinoma Hepatocelular/mortalidade
Carcinoma Hepatocelular/patologia
Pontos de Checagem do Ciclo Celular
Proliferação Celular/efeitos dos fármacos
Chaperonina com TCP-1/genética
Regulação Neoplásica da Expressão Gênica
Células Hep G2
Seres Humanos
Estimativa de Kaplan-Meier
Neoplasias Hepáticas/tratamento farmacológico
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/mortalidade
Neoplasias Hepáticas/patologia
Mitose/efeitos dos fármacos
Interferência de RNA
RNA Mensageiro/metabolismo
Transdução de Sinais
Fatores de Tempo
Transfecção
Moduladores de Tubulina/farmacologia
Vincristina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents, Phytogenic); 0 (CCT3 protein, human); 0 (RNA, Messenger); 0 (Tubulin Modulators); 5J49Q6B70F (Vincristine); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160206
[Lr] Data última revisão:
160206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160108
[St] Status:MEDLINE


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[PMID]:26718209
[Au] Autor:Wei PL; Huang CY; Tai CJ; Batzorig U; Cheng WL; Hunag MT; Chang YJ
[Ad] Endereço:Graduate Institute of Clinical Medicine, College of Medicine, Taipei Medical University, Taipei, Taiwan.
[Ti] Título:Glucose-regulated protein 94 mediates metastasis by CCT8 and the JNK pathway in hepatocellular carcinoma.
[So] Source:Tumour Biol;37(6):8219-27, 2016 Jun.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatocellular carcinoma (HCC) is one of the leading causes of cancer death worldwide. Cancer metastasis is a major obstacle in clinical cancer therapy. The mechanisms underlying the metastasis of HCC remain unclear. Glucose-regulated protein 94 (GRP94) is a key protein involved in mediating cancer progression, and it is highly expressed in HCC specimens. However, the role of GRP94 in cancer metastasis is unclear. A specific short hairpin RNA (shRNA) was employed to knock down GRP94 gene expression in HCC cell lines. Wound-healing migration, transwell migration, and invasion assays were performed to determine the migration and invasive ability of HCC cells. We demonstrated that silencing GRP94 inhibited HCC cell wound healing, migration, and invasion. Furthermore, our findings indicated that GRP94 knockdown might attenuate HCC cell metastasis by inhibiting CCT8/c-Jun/EMT signaling. Our study indicated that silencing GRP94 significantly reduced the migration and invasion abilities of HCC cells. Moreover, depleting GRP94 inhibited cell migration and invasion by downregulating CCT8/c-Jun signaling. Thus, our data suggest that the GRP94/CCT8/c-Jun/EMT signaling cascade might be a new therapeutic target for HCC.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/genética
Chaperonina com TCP-1/metabolismo
Regulação Neoplásica da Expressão Gênica/fisiologia
Proteínas de Choque Térmico HSP70/genética
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Neoplasias Hepáticas/genética
Proteínas de Membrana/genética
[Mh] Termos MeSH secundário: Western Blotting
Carcinoma Hepatocelular/metabolismo
Carcinoma Hepatocelular/secundário
Linhagem Celular Tumoral
Ensaios de Migração Celular
Movimento Celular/genética
Técnicas de Silenciamento de Genes
Inativação Gênica
Seres Humanos
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/patologia
Invasividade Neoplásica/genética
RNA Interferente Pequeno
Cicatrização/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HSP70 Heat-Shock Proteins); 0 (Membrane Proteins); 0 (RNA, Small Interfering); 0 (glucose-regulated proteins); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 3.6.1.- (CCT8 protein, human); EC 3.6.1.- (Chaperonin Containing TCP-1)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160101
[St] Status:MEDLINE
[do] DOI:10.1007/s13277-015-4669-3



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