Base de dados : MEDLINE
Pesquisa : D12.776.934 [Categoria DeCS]
Referências encontradas : 728 [refinar]
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[PMID]:29190611
[Au] Autor:Liu J; Rao J; Lou X; Zhai J; Ni Z; Wang X
[Ad] Endereço:Department of Respiratory Medicine, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
[Ti] Título:Upregulated TRIM11 Exerts its Oncogenic Effects in Hepatocellular Carcinoma Through Inhibition of P53.
[So] Source:Cell Physiol Biochem;44(1):255-266, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: The tripartite motif containing (TRIM) family plays crucial roles in tumor development and progression. However, little is known about the function and mechanism of TRIM11 in hepatocellular carcinoma (HCC). METHODS: The expression levels of TRIM11 were examined by real-time PCR, Western blot and Immunohistochemical (IHC) staining. TRIM11 knockdown cells were produced by lentivirus infection, and functional assays, such as MTT, colony formation assay, migration and invasion assays and a xenograft tumor model were used to investigate the role of TRIM11 in HCC. We also determined the effect of TRIM11 on p53 signaling and its downstream molecules. RESULTS: We found that TRIM11 mRNA and protein levels were significantly increased in HCC tissues as compared with normal tissues; increased levels correlated with poor patient survival. By loss- and gain-of-function investigations, knockdown of TRIM11 suppressed cell proliferation, migration, invasion in vitro and tumor growth in vivo. Moreover, TRIM11 negatively regulated p53 expression. Knockdown of p53 abrogated the in vitro and in vivo biological functions of TRIM11 shRNA in HCC cells. CONCLUSIONS: These data show that TRIM11 exerts its oncogenic effect in HCC by downregulating p53 both in vitro and in vivo. Our data provide new insights into the pathogenesis of HCC and indicate that TRIM11 may serve as a new therapeutic target for HCC treatment.
[Mh] Termos MeSH primário: Proteínas com Motivo Tripartido/genética
Proteínas com Motivo Tripartido/metabolismo
Proteína Supressora de Tumor p53/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/metabolismo
Regulação para Cima
[Mh] Termos MeSH secundário: Animais
Carcinoma Hepatocelular/metabolismo
Carcinoma Hepatocelular/patologia
Movimento Celular
Proliferação Celular
Ciclina D1/genética
Ciclina D1/metabolismo
Inibidor de Quinase Dependente de Ciclina p21/genética
Inibidor de Quinase Dependente de Ciclina p21/metabolismo
Inibidor de Quinase Dependente de Ciclina p27/genética
Inibidor de Quinase Dependente de Ciclina p27/metabolismo
Regulação para Baixo
Transição Epitelial-Mesenquimal
Células Hep G2
Seres Humanos
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/patologia
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Transplante Heterólogo
Proteínas com Motivo Tripartido/antagonistas & inibidores
Proteína Supressora de Tumor p53/antagonistas & inibidores
Proteína Supressora de Tumor p53/genética
Ubiquitina-Proteína Ligases/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (RNA, Small Interfering); 0 (TP53 protein, human); 0 (Tripartite Motif Proteins); 0 (Tumor Suppressor Protein p53); 136601-57-5 (Cyclin D1); 147604-94-2 (Cyclin-Dependent Kinase Inhibitor p27); EC 2.3.2.27 (TRIM11 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1159/000484678


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[PMID]:29217190
[Au] Autor:Unuma K; Aki T; Nagano S; Watanabe R; Uemura K
[Ad] Endereço:Department of Forensic Medicine, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, 1-5-45, Yushima, Bunkyo-ku, Tokyo, 113-8519, Japan.
[Ti] Título:The down-regulation of cardiac contractile proteins underlies myocardial depression during sepsis and is mitigated by carbon monoxide.
[So] Source:Biochem Biophys Res Commun;495(2):1668-1674, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aim of this study is to investigate the mechanism underling cardiac dysfunction during sepsis, as well as the possible amelioration of this dysfunction by exogenous carbon monoxide (CO) administration. For this purpose, rats (six-week-old, male, Sprague-Dawley) were administered LPS (15 mg/kg body weight, i.p. 6 h) and/or CORM (30 mg/kg, i.p.). The decreased left ventricular ejection fraction (EF) observed in LPS group rats was recovered in the LSP + CORM group, confirming the protective role of CO against sepsis-induced myocardial depression. Proteomic as well as immunoblot analysis showed that the levels of myosin heavy and light chains (MHC and MLC) as well as α-cardiac actin (ACTC) were decreased in the LPS group, and these decreases were mitigated in the LSP + CORM group, suggesting that the amounts of major contractile proteins are decreased in depressed myocardium. Not only LPS-induced inflammatory cytokine (TNFα and IL-1ß) production but also the decrease in myofilament proteins was mitigated by CORM. These results confirm the protective action of exogenously administered CO against myocardial depression during sepsis, and reveal a novel mechanism underling cardiac dysfunction during sepsis.
[Mh] Termos MeSH primário: Monóxido de Carbono/metabolismo
Proteínas Musculares/metabolismo
Miocárdio/metabolismo
Sepse/metabolismo
[Mh] Termos MeSH secundário: Actinas/genética
Actinas/metabolismo
Animais
Miosinas Cardíacas/genética
Miosinas Cardíacas/metabolismo
Cardiotônicos/farmacologia
Linhagem Celular
Citocinas/genética
Modelos Animais de Doenças
Regulação para Baixo
Expressão Gênica/efeitos dos fármacos
Lipopolissacarídeos/toxicidade
Masculino
Proteínas Musculares/genética
Contração Miocárdica/efeitos dos fármacos
Contração Miocárdica/fisiologia
Miocárdio/patologia
Compostos Organometálicos/farmacologia
Ratos
Ratos Sprague-Dawley
Proteínas Ligases SKP Culina F-Box/metabolismo
Sepse/tratamento farmacológico
Sepse/patologia
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Cardiotonic Agents); 0 (Cytokines); 0 (Lipopolysaccharides); 0 (Muscle Proteins); 0 (Organometallic Compounds); 0 (Tripartite Motif Proteins); 0 (tricarbonylchloro(glycinato)ruthenium(II)); 7U1EE4V452 (Carbon Monoxide); EC 2.3.2.27 (Fbxo32 protein, rat); EC 2.3.2.27 (SKP Cullin F-Box Protein Ligases); EC 2.3.2.27 (Trim63 protein, rat); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.6.1.- (Cardiac Myosins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


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[PMID]:29227681
[Au] Autor:Duan Y; Li F; Guo Q; Wang W; Zhang L; Wen C; Chen X; Yin Y
[Ad] Endereço:Laboratory of Animal Nutritional Physiology and Metabolic Process, Institute of Subtropical Agriculture Chinese Academy of Sciences; Key Laboratory of Agro-ecological Processes in Subtropical Region; Hunan Provincial Engineering Research Center for Healthy Livestock and Poultry Production; Scientifi
[Ti] Título:ß-Hydroxy-ß-methyl Butyrate Is More Potent Than Leucine in Inhibiting Starvation-Induced Protein Degradation in C2C12 Myotubes.
[So] Source:J Agric Food Chem;66(1):170-176, 2018 Jan 10.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Leucine (Leu) and its metabolites α-ketoisocaproate (KIC) and ß-hydroxy-ß-methyl butyrate (HMB) are potent regulators of protein turnover. The aim of this study was to compare the inhibitory effects of Leu, KIC, and HMB on protein degradation and to investigate the mechanisms involved. The results showed that the inhibitory effect of HMB (0.38 ± 0.04) was more potent than that of Leu (0.76 ± 0.04) and KIC (0.56 ± 0.04, P < 0.01), and was significantly abolished in the presence of LY294002 (1.48 ± 0.02) and rapamycin (1.96 ± 0.02, P < 0.01). In the presence of insulin, the inhibitory effect of HMB (0.34 ± 0.03) was still more effective than that of Leu (0.60 ± 0.04) and KIC (0.57 ± 0.08, P < 0.05). Interestingly, LY294002 treatment markedly attenuated the effect of HMB, while rapamycin treatment failed to exert the same effect. Thus, HMB appears to be more potent than Leu and KIC in inhibiting protein degradation in the absence or presence of insulin, and this inhibitory effect may be dependent on PI3K/Akt signaling pathway regardless of insulin, and mTOR signaling was only involved in this effect of HMB in the absence of insulin.
[Mh] Termos MeSH primário: Leucina/farmacologia
Fibras Musculares Esqueléticas/efeitos dos fármacos
Proteólise/efeitos dos fármacos
Valeratos/farmacologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Insulina/farmacologia
Cetoácidos/farmacologia
Camundongos
Fibras Musculares Esqueléticas/metabolismo
Proteínas Musculares/genética
Proteínas Musculares/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Ligases SKP Culina F-Box/genética
Proteínas Ligases SKP Culina F-Box/metabolismo
Serina-Treonina Quinases TOR/metabolismo
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insulin); 0 (Keto Acids); 0 (Muscle Proteins); 0 (Tripartite Motif Proteins); 0 (Valerates); 3F752311CD (beta-hydroxyisovaleric acid); 816-66-0 (alpha-ketoisocaproic acid); EC 2.3.2.27 (Fbxo32 protein, mouse); EC 2.3.2.27 (SKP Cullin F-Box Protein Ligases); EC 2.3.2.27 (Trim63 protein, mouse); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.1.1 (mTOR protein, mouse); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); GMW67QNF9C (Leucine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04841


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[PMID]:29277369
[Au] Autor:Reddy SS; Shruthi K; Prabhakar YK; Sailaja G; Reddy GB
[Ad] Endereço:Biochemistry Division, National Institute of Nutrition, Hyderabad, India.
[Ti] Título:Implication of altered ubiquitin-proteasome system and ER stress in the muscle atrophy of diabetic rats.
[So] Source:Arch Biochem Biophys;639:16-25, 2018 02 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Skeletal muscle is adversely affected in type-1 diabetes, and excessively stimulated ubiquitin-proteasome system (UPS) was found to be a leading cause of muscle wasting or atrophy. The role of endoplasmic reticulum (ER) stress in muscle atrophy of type-1 diabetes is not known. Hence, we investigated the role of UPS and ER stress in the muscle atrophy of chronic diabetes rat model. METHODS: Diabetes was induced with streptozotocin (STZ) in male Sprague-Dawley rats and were sacrificed 2- and 4-months thereafter to collect gastrocnemius muscle. In another experiment, 2-months post-STZ-injection diabetic rats were treated with MG132, a proteasome inhibitor, for the next 2-months and gastrocnemius muscle was collected. RESULTS: The muscle fiber cross-sectional area was diminished in diabetic rats. The expression of UPS components: E1, MURF1, TRIM72, UCHL1, UCHL5, ubiquitinated proteins, and proteasome activity were elevated in the diabetic rats indicating activated UPS. Altered expression of ER-associated degradation (ERAD) components and increased ER stress markers were detected in 4-months diabetic rats. Proteasome inhibition by MG132 alleviated alterations in the UPS and ER stress in diabetic rat muscle. CONCLUSION: Increased UPS activity and ER stress were implicated in the muscle atrophy of diabetic rats and proteasome inhibition exhibited beneficiary outcome.
[Mh] Termos MeSH primário: Diabetes Mellitus Experimental/metabolismo
Estresse do Retículo Endoplasmático
Músculo Esquelético/metabolismo
Atrofia Muscular/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Animais
Diabetes Mellitus Experimental/tratamento farmacológico
Diabetes Mellitus Experimental/patologia
Leupeptinas/farmacologia
Masculino
Proteínas Musculares/metabolismo
Músculo Esquelético/patologia
Atrofia Muscular/induzido quimicamente
Atrofia Muscular/tratamento farmacológico
Atrofia Muscular/patologia
Inibidores de Proteassoma/farmacologia
Ratos
Ratos Sprague-Dawley
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina Tiolesterase/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
Proteínas Ubiquitinadas/metabolismo
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Leupeptins); 0 (MG53 protein, rat); 0 (Muscle Proteins); 0 (Proteasome Inhibitors); 0 (Tripartite Motif Proteins); 0 (Ubiquitin); 0 (Ubiquitinated Proteins); 0 (Vesicular Transport Proteins); EC 2.3.2.27 (Trim63 protein, rat); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.4.19.12 (UCHL1 protein, rat); EC 3.4.19.12 (Ubiquitin Thiolesterase); EC 3.4.25.1 (Proteasome Endopeptidase Complex); RF1P63GW3K (benzyloxycarbonylleucyl-leucyl-leucine aldehyde)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


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[PMID]:28465407
[Au] Autor:Lu T; Sun X; Li Y; Chai Q; Wang XL; Lee HC
[Ad] Endereço:Department of Cardiovascular Diseases, Mayo Clinic, Rochester, MN lu.tong@mayo.edu.
[Ti] Título:Role of Nrf2 Signaling in the Regulation of Vascular BK Channel ß1 Subunit Expression and BK Channel Function in High-Fat Diet-Induced Diabetic Mice.
[So] Source:Diabetes;66(10):2681-2690, 2017 10.
[Is] ISSN:1939-327X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The large conductance Ca -activated K (BK) channel ß1-subunit (BK-ß1) is a key modulator of BK channel electrophysiology and the downregulation of BK-ß1 protein expression in vascular smooth muscle cells (SMCs) underlies diabetic vascular dysfunction. In this study, we hypothesized that the nuclear factor erythroid-2-related factor 2 (Nrf2) signaling pathway plays a significant role in the regulation of coronary BK channel function and vasodilation in high-fat diet (HFD)-induced obese/diabetic mice. We found that the protein expressions of BK-ß1 and Nrf2 were markedly downregulated, whereas those of the nuclear factor-κB (NF-κB) and the muscle ring finger protein 1 (MuRF1 [a ubiquitin E3 ligase for BK-ß1]) were significantly upregulated in HFD mouse arteries. Adenoviral expression of Nrf2 suppressed the protein expressions of NF-κB and MuRF1 but enhanced BK-ß1 mRNA and protein expressions in cultured coronary SMCs. Knockdown of Nrf2 resulted in reciprocal changes of these proteins. Patch-clamp studies showed that coronary BK-ß1-mediated channel activation was diminished in HFD mice. Importantly, the activation of Nrf2 by dimethyl fumarate significantly reduced the body weight and blood glucose levels of HFD mice, enhanced BK-ß1 transcription, and attenuated MuRF1-dependent BK-ß1 protein degradation, which in turn restored coronary BK channel function and BK channel-mediated coronary vasodilation in HFD mice. Hence, Nrf2 is a novel regulator of BK channel function with therapeutic implications in diabetic vasculopathy.
[Mh] Termos MeSH primário: Diabetes Mellitus Experimental/metabolismo
Dieta Hiperlipídica/efeitos adversos
Canais de Potássio Ativados por Cálcio de Condutância Alta/metabolismo
Fator 2 Relacionado a NF-E2/metabolismo
[Mh] Termos MeSH secundário: Adenoviridae/genética
Animais
Diabetes Mellitus Experimental/etiologia
Fumarato de Dimetilo/farmacologia
Canais de Potássio Ativados por Cálcio de Condutância Alta/genética
Masculino
Camundongos
Proteínas Musculares/genética
Proteínas Musculares/metabolismo
Fator 2 Relacionado a NF-E2/genética
Transdução de Sinais/efeitos dos fármacos
Transdução de Sinais/genética
Proteínas com Motivo Tripartido/genética
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/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 (Large-Conductance Calcium-Activated Potassium Channels); 0 (Muscle Proteins); 0 (NF-E2-Related Factor 2); 0 (Nfe2l2 protein, mouse); 0 (Tripartite Motif Proteins); EC 2.3.2.27 (Trim63 protein, mouse); EC 2.3.2.27 (Ubiquitin-Protein Ligases); FO2303MNI2 (Dimethyl Fumarate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.2337/db17-0181


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[PMID]:28465353
[Au] Autor:Borlepawar A; Rangrez AY; Bernt A; Christen L; Sossalla S; Frank D; Frey N
[Ad] Endereço:From the Department of Internal Medicine III (Cardiology, Angiology, Intensive Care), University Medical Center Kiel and.
[Ti] Título:TRIM24 protein promotes and TRIM32 protein inhibits cardiomyocyte hypertrophy via regulation of dysbindin protein levels.
[So] Source:J Biol Chem;292(24):10180-10196, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have previously shown that dysbindin is a potent inducer of cardiomyocyte hypertrophy via activation of Rho-dependent serum-response factor (SRF) signaling. We have now performed a yeast two-hybrid screen using dysbindin as bait against a cardiac cDNA library to identify the cardiac dysbindin interactome. Among several putative binding proteins, we identified tripartite motif-containing protein 24 (TRIM24) and confirmed this interaction by co-immunoprecipitation and co-immunostaining. Another tripartite motif (TRIM) family protein, TRIM32, has been reported earlier as an E3 ubiquitin ligase for dysbindin in skeletal muscle. Consistently, we found that TRIM32 also degraded dysbindin in neonatal rat ventricular cardiomyocytes as well. Surprisingly, however, TRIM24 did not promote dysbindin decay but rather protected dysbindin against degradation by TRIM32. Correspondingly, TRIM32 attenuated the activation of SRF signaling and hypertrophy due to dysbindin, whereas TRIM24 promoted these effects in neonatal rat ventricular cardiomyocytes. This study also implies that TRIM32 is a key regulator of cell viability and apoptosis in cardiomyocytes via simultaneous activation of p53 and caspase-3/-7 and inhibition of X-linked inhibitor of apoptosis. In conclusion, we provide here a novel mechanism of post-translational regulation of dysbindin and hypertrophy via TRIM24 and TRIM32 and show the importance of TRIM32 in cardiomyocyte apoptosis .
[Mh] Termos MeSH primário: Cardiomiopatia Dilatada/metabolismo
Cardiomiopatia Hipertrófica/metabolismo
Proteínas de Transporte/metabolismo
Proteínas Associadas à Distrofina/metabolismo
Miócitos Cardíacos/metabolismo
Fator de Resposta Sérica/metabolismo
Fatores de Transcrição/metabolismo
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Apoptose
Cardiomiopatia Dilatada/patologia
Cardiomiopatia Hipertrófica/patologia
Proteínas de Transporte/antagonistas & inibidores
Proteínas de Transporte/genética
Células Cultivadas
Disbindina
Proteínas Associadas à Distrofina/química
Proteínas Associadas à Distrofina/genética
Células HEK293
Seres Humanos
Miócitos Cardíacos/citologia
Miócitos Cardíacos/patologia
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Estabilidade Proteica
Proteólise
Interferência de RNA
Ratos
Ratos Wistar
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Fator de Resposta Sérica/agonistas
Fator de Resposta Sérica/antagonistas & inibidores
Fator de Resposta Sérica/genética
Transdução de Sinais
Fatores de Transcrição/antagonistas & inibidores
Fatores de Transcrição/genética
Proteínas com Motivo Tripartido/antagonistas & inibidores
Proteínas com Motivo Tripartido/genética
Ubiquitina-Proteína Ligases/antagonistas & inibidores
Ubiquitina-Proteína Ligases/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (DTNBP1 protein, human); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (SRF protein, human); 0 (Serum Response Factor); 0 (TRIM24 protein, human); 0 (Transcription Factors); 0 (Tripartite Motif Proteins); EC 2.3.2.27 (TRIM32 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.752543


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[PMID]:28461211
[Au] Autor:Luo K; Li Y; Xia L; Hu W; Gao W; Guo L; Tian G; Qi Z; Yuan H; Xu Q
[Ad] Endereço:Engineering Research Centre of Ecology and Agricultural Use of Wetland, Ministry of Education, Jingzhou 434020, China.
[Ti] Título:Analysis of the expression patterns of the novel large multigene TRIM gene family (finTRIM) in zebrafish.
[So] Source:Fish Shellfish Immunol;66:224-230, 2017 Jul.
[Is] ISSN:1095-9947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Tripartite motif (TRIM) proteins are receiving increased research interest because of their roles in a wide range of cellular biological processes in innate immunity. In zebrafish (Danio rerio), the functions of the finTRIM (ftr) family are unclear. In the present study, we investigated the expression pattern of ftr12, ftr51, ftr67, ftr82, ftr83, and ftr84 in zebrafish for the first time. The results showed that ftr12, ftr67, and ftr84 are maternally expressed in the oocyte and highly expressed at the early stage (0-4 hpf) of embryo (P < 0.05), suggesting their involvement in the embryonic innate defense system. The ftr82 gene was highly expressed at 8 hpf (P < 0.05), which implied that the embryos could synthesize their own immunity-related mRNAs. However, ftr51 and ftr83 were highest at 8 hpf (2.33 and 51.53 relative to ß-actin respectively) and might mediate embryonic development. The expression levels of ftr12, ftr51, and ftr67 were highest in the gill, intestines, and liver, respectively. Ftr82, ftr83, and ftr84 were predominantly expressed in the kidney, suggesting that these finTRIMs might play roles in both immunity and non-immunity-related tissue compartments. Zebrafish embryonic fibroblast (ZF4) cells were infected with Grass carp reovirus (GCRV) and Spring viremia of carp virus (SVCV). During GCRV infection, the expression of ftr12 was significantly upregulated from 12 h to 24 h; and ftr51 and ftr67 increased from 3 h to 12 h. The expressions of ftr82, ftr83, and ftr84 were only upregulated at 12 h, 12 h, and 24 h, respectively. All of these genes were significantly downregulated at 48 h (P < 0.05). Challenge with SVCV upregulated the expressions of ftr12 and ftr51 at 12 h and 48 h (P < 0.05), respectively, and ftr67 reached its highest expression level at 3 h. ftr82 showed only a slight upregulation at 6 h and 48 h, and ftr83 and ftr84 were consecutively increased, reaching their highest levels at 12 h (P < 0.05). Meanwhile, ftr67 and ftr83 were significantly downregulated at 48 h (P < 0.05). Our research demonstrated that ftr12, ftr51, ftr67, ftr82, ftr83, and ftr84 probably have important roles in innate immune responses and in non-immunity-related tissues.
[Mh] Termos MeSH primário: Doenças dos Peixes/genética
Expressão Gênica
Imunidade Inata/genética
Família Multigênica
Proteínas com Motivo Tripartido/genética
Proteínas de Peixe-Zebra/genética
Peixe-Zebra
[Mh] Termos MeSH secundário: Animais
Doenças dos Peixes/imunologia
Doenças dos Peixes/virologia
Expressão Gênica/imunologia
Perfilação da Expressão Gênica/veterinária
Reoviridae/fisiologia
Infecções por Reoviridae/genética
Infecções por Reoviridae/imunologia
Infecções por Reoviridae/veterinária
Rhabdoviridae/fisiologia
Infecções por Rhabdoviridae/genética
Infecções por Rhabdoviridae/imunologia
Infecções por Rhabdoviridae/veterinária
Análise de Sequência de DNA/veterinária
Proteínas com Motivo Tripartido/metabolismo
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Tripartite Motif Proteins); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171215
[Lr] Data última revisão:
171215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:28954259
[Au] Autor:Cui H; Liu Y; Huang Y
[Ad] Endereço:Department of Ophthalmology, Chinese PLA General Hospital, Beijing, China.
[Ti] Título:Roles of TRIM32 in Corneal Epithelial Cells After Infection with Herpes Simplex Virus.
[So] Source:Cell Physiol Biochem;43(2):801-811, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Epithelial cells play important roles as a critical barrier in protecting the cornea from microbial pathogens infection. METHODS: In this study, we were aiming to investigate the role of E3 ubiquitin ligase tripartite motif protein 32 (TRIM32) in corneal epithelial cells in response to Herpes Simplex Virus type 1 (HSV-1) infection and to elucidate the underlying mechanisms. RESULTS: We found the expression of TRIM32 was increased after infected with HSV-1 both in murine corneas and cultured human epithelial (HCE) cells. Furthermore, knockdown of the expression of TRIM32 significantly aggravated HSV-1 induced herpetic stromal keratitis (HSK) in mice and promoted the replication of HSV-1 in cultured HCE cells. We also observed that silencing of TRIM32 resulted in the decreased expression of IFN-ß and suppressed activation of interferon regulatory factor 3 (IRF3) both in vivo and in vitro. Finally, we found TRIM32 positively regulate IFN-ß production in corneal epithelial cells through promoting K63-linked polyubiquitination of stimulator of interferon genes (STING). CONCLUSION: In conclusion, our data suggested that TRIM32 as a crucial positive regulator of HSV-1 induced IFN-ß production in corneal epithelial cells, and it played a predominant role in clearing HSV-1 from the cornea.
[Mh] Termos MeSH primário: Córnea/virologia
Herpesvirus Humano 1/fisiologia
Ceratite Herpética/metabolismo
Fatores de Transcrição/metabolismo
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Córnea/metabolismo
Córnea/patologia
Regulação para Baixo
Feminino
Seres Humanos
Fator Regulador 3 de Interferon/metabolismo
Interferon beta/genética
Interferon beta/metabolismo
Ceratite Herpética/genética
Ceratite Herpética/patologia
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Poliubiquitina/metabolismo
Fatores de Transcrição/genética
Proteínas com Motivo Tripartido/genética
Ubiquitina-Proteína Ligases/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interferon Regulatory Factor-3); 0 (MPYS protein, mouse); 0 (Membrane Proteins); 0 (Transcription Factors); 0 (Tripartite Motif Proteins); 120904-94-1 (Polyubiquitin); 77238-31-4 (Interferon-beta); EC 2.3.2.27 (TRIM32 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 6.3.2.19 (TRIM32 protein, mouse)
[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:170928
[St] Status:MEDLINE
[do] DOI:10.1159/000481563


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[PMID]:28899845
[Au] Autor:Fuentes EN; Zuloaga R; Almarza O; Mendez K; Valdés JA; Molina A; Pulgar J
[Ad] Endereço:Interdisciplinary Center for Aquaculture Research (INCAR), Víctor Lamas 1290, PO Box 160-C, Concepción 4030000, Chile.
[Ti] Título:Upwelling-derived oceanographic conditions impact growth performance and growth-related gene expression in intertidal fish.
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;214:12-18, 2017 Dec.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Growth is one of the main biological processes in aquatic organisms that is affected by environmental fluctuations such as upwelling (characterized by food-rich waters). In fish, growth is directly related with skeletal muscle increase; which represents the largest tissue of body mass. However, the effects of upwelling on growth, at the physiological and molecular level, are unknown. This study used Girella laevifrons (one of the most abundant intertidal fish in Eastern South Pacific) as a biological model, considering animals from upwelling (U) and non-upwelling (NU) areas. Here, we evaluated the effect of nutritional composition and food availability on growth performance and expression of key growth-related genes (insulin-kike growth factor 1 (igf1) and myosin heavy-chain (myhc)) and atrophy-related genes (muscle ring-finger 1 (murf1), F-box only protein 32 (atrogin-1) and BCL2/adenovirus E1B 19kDa-interacting protein 3 (bnip3)). We reported that, among zones, U fish displayed higher growth performance in response to nutritional composition, specifically between protein- and fiber-rich diets (~1g). We also found in NU fish that atrophy-related genes were upregulated with fiber-rich diet and during fasting (~2-fold at minimum respect U). In conclusion, our results suggest that the growth potential of upwelling fish may be a consequence of differential muscle gene expression. Our data provide a preliminary approach contributing on how upwelling influence fish growth at the physiological and molecular levels. Future studies are required to gain further knowledge about molecular differences between U and NU animals, as well as the possible applications of this knowledge in the aquaculture industry.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica no Desenvolvimento
Proteínas Musculares/genética
Músculo Esquelético/metabolismo
Perciformes/crescimento & desenvolvimento
Perciformes/genética
[Mh] Termos MeSH secundário: Animais
Dieta da Carga de Carboidratos
Ecossistema
Cadeia Alimentar
Fator de Crescimento Insulin-Like I/genética
Fator de Crescimento Insulin-Like I/metabolismo
Proteínas Musculares/metabolismo
Músculo Esquelético/crescimento & desenvolvimento
Perciformes/metabolismo
Proteínas Proto-Oncogênicas/genética
Proteínas Proto-Oncogênicas/metabolismo
Rios/química
Proteínas Ligases SKP Culina F-Box/genética
Proteínas Ligases SKP Culina F-Box/metabolismo
Água do Mar/química
Proteínas com Motivo Tripartido/genética
Proteínas com Motivo Tripartido/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Muscle Proteins); 0 (Proto-Oncogene Proteins); 0 (Tripartite Motif Proteins); 67763-96-6 (Insulin-Like Growth Factor I); EC 2.3.2.27 (SKP Cullin F-Box Protein Ligases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE


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[PMID]:28898289
[Au] Autor:Yang Q; Liu TT; Lin H; Zhang M; Wei J; Luo WW; Hu YH; Zhong B; Hu MM; Shu HB
[Ad] Endereço:Medical Research Institute, School of Medicine, Wuhan University, Wuhan, China.
[Ti] Título:TRIM32-TAX1BP1-dependent selective autophagic degradation of TRIF negatively regulates TLR3/4-mediated innate immune responses.
[So] Source:PLoS Pathog;13(9):e1006600, 2017 Sep.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Toll-like receptor (TLR)-mediated signaling are critical for host defense against pathogen invasion. However, excessive responses would cause harmful damages to the host. Here we show that deficiency of the E3 ubiquitin ligase TRIM32 increases poly(I:C)- and LPS-induced transcription of downstream genes such as type I interferons (IFNs) and proinflammatory cytokines in both primary mouse immune cells and in mice. Trim32-/- mice produced higher levels of serum inflammatory cytokines and were more sensitive to loss of body weight and inflammatory death upon Salmonella typhimurium infection. TRIM32 interacts with and mediates the degradation of TRIF, a critical adaptor protein for TLR3/4, in an E3 activity-independent manner. TRIM32-mediated as well as poly(I:C)- and LPS-induced degradation of TRIF is inhibited by deficiency of TAX1BP1, a receptor for selective autophagy. Furthermore, TRIM32 links TRIF and TAX1BP1 through distinct domains. These findings suggest that TRIM32 negatively regulates TLR3/4-mediated immune responses by targeting TRIF to TAX1BP1-mediated selective autophagic degradation.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Autofagia
Imunidade Inata
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas de Neoplasias/metabolismo
Receptor 3 Toll-Like/metabolismo
Receptor 4 Toll-Like/metabolismo
Fatores de Transcrição/metabolismo
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Citocinas/metabolismo
Seres Humanos
Imunidade Inata/efeitos dos fármacos
Imunidade Inata/imunologia
Peptídeos e Proteínas de Sinalização Intracelular/genética
Lipopolissacarídeos/farmacologia
Macrófagos/imunologia
Proteínas de Neoplasias/genética
Receptor 3 Toll-Like/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Adaptor Proteins, Vesicular Transport); 0 (Cytokines); 0 (Intracellular Signaling Peptides and Proteins); 0 (Lipopolysaccharides); 0 (Neoplasm Proteins); 0 (TAX1BP1 protein, human); 0 (TICAM1 protein, human); 0 (TLR3 protein, human); 0 (TLR4 protein, human); 0 (Toll-Like Receptor 3); 0 (Toll-Like Receptor 4); 0 (Transcription Factors); 0 (Tripartite Motif Proteins); EC 2.3.2.27 (TRIM32 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[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:170913
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006600



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