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[PMID]:29408396
[Au] Autor:Wang W; Zhang H; Wei X; Yang L; Yang B; Zhang L; Li J; Jiang YQ
[Ad] Endereço:State Key Laboratory of Crop Stress Biology for Arid Areas, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China.
[Ti] Título:Functional characterization of calcium-dependent protein kinase (CPK) 2 gene from oilseed rape (Brassica napus L.) in regulating reactive oxygen species signaling and cell death control.
[So] Source:Gene;651:49-56, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Calcium-dependent protein kinases (CPKs), being Ser/Thr protein kinases found only in plants and some protozoans are calcium sensors that regulate diverse biological processes. However, the function and mode of CPKs in oilseed rape (Brassica napus) remain elusive. In this study, we identified CPK2 from oilseed rape as a novel regulator of reactive oxygen species (ROS) and cell death. BnaCPK2 was identified to be located at the endoplasmic reticulum membrane. Expression of BnaCPK2 was induced during Bax-induced cell death. Overexpression of the constitutively active form of BnaCPK2 led to significantly more accumulation of ROS and cell death than the full-length CPK2, which is supported by various measurements of physiological data. In addition, a quantitative RT-PCR survey revealed that the expression levels of a few marker genes are significantly changed as a result of CPK2 expression. Mating-based split ubiquitin system (mbSUS) and bimolecular fluorescence complementation (BiFC) were used to screen and confirm the BnaCPK2 interacting proteins. We identified and confirmed that CPK2 interacted with NADPH oxidase-like respiratory burst oxidase homolog D (RbohD), but not with RbohF. Based on its function and interacting partners, we propose that BnaCPK2 plays an important role in ROS and cell death control through interacting with RbohD.
[Mh] Termos MeSH primário: Brassica napus/genética
Morte Celular/genética
Proteínas de Plantas/genética
Proteínas Quinases/genética
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Brassica napus/enzimologia
Clonagem Molecular
DNA de Plantas
Proteínas de Plantas/metabolismo
Proteínas Quinases/metabolismo
Análise de Sequência de DNA
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Plant); 0 (Plant Proteins); 0 (Reactive Oxygen Species); EC 2.7.- (Protein Kinases); EC 2.7.1.- (calcium-dependent protein kinase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180207
[St] Status:MEDLINE


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Registro de Ensaios Clínicos
Registro de Ensaios Clínicos
Registro de Ensaios Clínicos
Registro de Ensaios Clínicos
Registro de Ensaios Clínicos
Registro de Ensaios Clínicos
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[PMID]:29466156
[Au] Autor:Drilon A; Laetsch TW; Kummar S; DuBois SG; Lassen UN; Demetri GD; Nathenson M; Doebele RC; Farago AF; Pappo AS; Turpin B; Dowlati A; Brose MS; Mascarenhas L; Federman N; Berlin J; El-Deiry WS; Baik C; Deeken J; Boni V; Nagasubramanian R; Taylor M; Rudzinski ER; Meric-Bernstam F; Sohal DPS; Ma PC; Raez LE; Hechtman JF; Benayed R; Ladanyi M; Tuch BB; Ebata K; Cruickshank S; Ku NC; Cox MC; Hawkins DS; Hong DS; Hyman DM
[Ad] Endereço:From Memorial Sloan Kettering Cancer Center (A. Drilon, J.F.H., R.B., M.L., D.M.H.) and Weill Cornell Medical College (A. Drilon, D.M.H.), New York; University of Texas Southwestern Medical Center-Children's Health, Dallas (T.W.L.); Stanford Cancer Center, Stanford University, Palo Alto (S.K.), Chil
[Ti] Título:Efficacy of Larotrectinib in TRK Fusion-Positive Cancers in Adults and Children.
[So] Source:N Engl J Med;378(8):731-739, 2018 02 22.
[Is] ISSN:1533-4406
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Fusions involving one of three tropomyosin receptor kinases (TRK) occur in diverse cancers in children and adults. We evaluated the efficacy and safety of larotrectinib, a highly selective TRK inhibitor, in adults and children who had tumors with these fusions. METHODS: We enrolled patients with consecutively and prospectively identified TRK fusion-positive cancers, detected by molecular profiling as routinely performed at each site, into one of three protocols: a phase 1 study involving adults, a phase 1-2 study involving children, or a phase 2 study involving adolescents and adults. The primary end point for the combined analysis was the overall response rate according to independent review. Secondary end points included duration of response, progression-free survival, and safety. RESULTS: A total of 55 patients, ranging in age from 4 months to 76 years, were enrolled and treated. Patients had 17 unique TRK fusion-positive tumor types. The overall response rate was 75% (95% confidence interval [CI], 61 to 85) according to independent review and 80% (95% CI, 67 to 90) according to investigator assessment. At 1 year, 71% of the responses were ongoing and 55% of the patients remained progression-free. The median duration of response and progression-free survival had not been reached. At a median follow-up of 9.4 months, 86% of the patients with a response (38 of 44 patients) were continuing treatment or had undergone surgery that was intended to be curative. Adverse events were predominantly of grade 1, and no adverse event of grade 3 or 4 that was considered by the investigators to be related to larotrectinib occurred in more than 5% of patients. No patient discontinued larotrectinib owing to drug-related adverse events. CONCLUSIONS: Larotrectinib had marked and durable antitumor activity in patients with TRK fusion-positive cancer, regardless of the age of the patient or of the tumor type. (Funded by Loxo Oncology and others; ClinicalTrials.gov numbers, NCT02122913 , NCT02637687 , and NCT02576431 .).
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Neoplasias/tratamento farmacológico
Pirazóis/uso terapêutico
Pirimidinas/uso terapêutico
Receptores Proteína Tirosina Quinases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Criança
Pré-Escolar
Intervalo Livre de Doença
Feminino
Seres Humanos
Lactente
Estimativa de Kaplan-Meier
Masculino
Meia-Idade
Neoplasias/química
Proteínas de Fusão Oncogênicas/análise
Proteínas Quinases/análise
Proteínas Quinases/genética
Adulto Jovem
[Pt] Tipo de publicação:CLINICAL TRIAL, PHASE I; CLINICAL TRIAL, PHASE II; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ARRY-470); 0 (Antineoplastic Agents); 0 (Oncogene Proteins, Fusion); 0 (Pyrazoles); 0 (Pyrimidines); EC 2.7.- (Protein Kinases); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases); EC 2.7.11.28 (tropomyosin kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180222
[Cl] Clinical Trial:ClinicalTrial
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMoa1714448


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[PMID]:29228003
[Au] Autor:Crawley O; Giles AC; Desbois M; Kashyap S; Birnbaum R; Grill B
[Ad] Endereço:Department of Neuroscience, The Scripps Research Institute, Scripps Florida, Jupiter, Florida, United States of America.
[Ti] Título:A MIG-15/JNK-1 MAP kinase cascade opposes RPM-1 signaling in synapse formation and learning.
[So] Source:PLoS Genet;13(12):e1007095, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Pam/Highwire/RPM-1 (PHR) proteins are conserved intracellular signaling hubs that regulate synapse formation and axon termination. The C. elegans PHR protein, called RPM-1, acts as a ubiquitin ligase to inhibit the DLK-1 and MLK-1 MAP kinase pathways. We have identified several kinases that are likely to form a new MAP kinase pathway that suppresses synapse formation defects, but not axon termination defects, in the mechanosensory neurons of rpm-1 mutants. This pathway includes: MIG-15 (MAP4K), NSY-1 (MAP3K), JKK-1 (MAP2K) and JNK-1 (MAPK). Transgenic overexpression of kinases in the MIG-15/JNK-1 pathway is sufficient to impair synapse formation in wild-type animals. The MIG-15/JNK-1 pathway functions cell autonomously in the mechanosensory neurons, and these kinases localize to presynaptic terminals providing further evidence of a role in synapse development. Loss of MIG-15/JNK-1 signaling also suppresses defects in habituation to repeated mechanical stimuli in rpm-1 mutants, a behavioral deficit that is likely to arise from impaired glutamatergic synapse formation. Interestingly, habituation results are consistent with the MIG-15/JNK-1 pathway functioning as a parallel opposing pathway to RPM-1. These findings indicate the MIG-15/JNK-1 pathway can restrict both glutamatergic synapse formation and short-term learning.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Sistema de Sinalização das MAP Quinases
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Axônios/metabolismo
Caenorhabditis elegans/genética
Caenorhabditis elegans/crescimento & desenvolvimento
Proteínas de Caenorhabditis elegans/genética
Fatores de Troca do Nucleotídeo Guanina/genética
Proteínas Quinases Ativadas por Mitógeno/genética
Mutação
Neurogênese
Neurônios/metabolismo
Terminações Pré-Sinápticas/metabolismo
Proteínas Quinases/genética
Proteínas Quinases/metabolismo
Proteínas Serina-Treonina Quinases/genética
Transdução de Sinais
Sinapses/enzimologia
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 (Caenorhabditis elegans Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (RPM-1 protein, C elegans); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.- (Protein Kinases); EC 2.7.1.- (jkk-1 protein, C elegans); EC 2.7.11.1 (Mig-15 protein, C elegans); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.24 (JNK-1 protein, C elegans); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007095


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[PMID]:28468956
[Au] Autor:Jasnovidova O; Krejcikova M; Kubicek K; Stefl R
[Ad] Endereço:CEITEC - Central European Institute of Technology, Masaryk University, Brno, Czech Republic olga.jasnovidova@ceitec.muni.cz richard.stefl@ceitec.muni.cz.
[Ti] Título:Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p.
[So] Source:EMBO Rep;18(6):906-913, 2017 Jun.
[Is] ISSN:1469-3178
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phosphorylation patterns of the C-terminal domain (CTD) of largest subunit of RNA polymerase II (called the CTD code) orchestrate the recruitment of RNA processing and transcription factors. Recent studies showed that not only serines and tyrosines but also threonines of the CTD can be phosphorylated with a number of functional consequences, including the interaction with yeast transcription termination factor, Rtt103p. Here, we report the solution structure of the Rtt103p CTD-interacting domain (CID) bound to Thr4 phosphorylated CTD, a poorly understood letter of the CTD code. The structure reveals a direct recognition of the phospho-Thr4 mark by Rtt103p CID and extensive interactions involving residues from three repeats of the CTD heptad. Intriguingly, Rtt103p's CID binds equally well Thr4 and Ser2 phosphorylated CTD A doubly phosphorylated CTD at Ser2 and Thr4 diminishes its binding affinity due to electrostatic repulsion. Our structural data suggest that the recruitment of a CID-containing CTD-binding factor may be coded by more than one letter of the CTD code.
[Mh] Termos MeSH primário: RNA Polimerase II/química
Proteínas de Saccharomyces cerevisiae/química
Treonina/química
Fatores de Transcrição/química
[Mh] Termos MeSH secundário: Fosforilação
Ligação Proteica
Proteínas Quinases/metabolismo
Estrutura Terciária de Proteína
Proteólise
RNA Polimerase II/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Serina/metabolismo
Treonina/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Rtt103 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 2ZD004190S (Threonine); 42HK56048U (Tyrosine); 452VLY9402 (Serine); EC 2.7.- (Protein Kinases); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.15252/embr.201643723


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[PMID]:29287725
[Au] Autor:Cates C; Rousselle T; Wang J; Quan N; Wang L; Chen X; Yang L; Rezaie AR; Li J
[Ad] Endereço:Department of Physiology and Biophysics, Mississippi Center for Heart Research, University of Mississippi Medical Center, Jackson, MS 39216, USA.
[Ti] Título:Activated protein C protects against pressure overload-induced hypertrophy through AMPK signaling.
[So] Source:Biochem Biophys Res Commun;495(4):2584-2594, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We found that the anticoagulant plasma protease, activated protein C (APC), stimulates the energy sensor kinase, AMPK, in the stressed heart by activating protease-activated receptor 1 (PAR1) on cardiomyocytes. Wild-type (WT) and AMPK-kinase dead (KD) transgenic mice were subjected to transverse aortic constriction (TAC) surgery. The results demonstrated that while no phenotypic differences can be observed between WT and AMPK-KD mice under normal physiological conditions, AMPK-KD mice exhibit significantly larger hearts after 4 weeks of TAC surgery. Analysis by echocardiography suggested that the impairment in the cardiac function of AMPK-KD hearts is significantly greater than that of WT hearts. Immunohistochemical staining revealed increased macrophage infiltration and ROS generation in AMPK-KD hearts after 4 weeks of TAC surgery. Immunoblotting results demonstrated that the redox markers, pShc , 4-hydroxynonenal and ERK, were all up-regulated at a higher extent in AMPK-KD hearts after 4 weeks of TAC surgery. Administration of APC-WT and the signaling selective APC-2Cys mutant, but not the anticoagulant selective APC-E170A mutant, significantly attenuated pressure overload-induced hypertrophy and fibrosis. Macrophage infiltration and pShc activation caused by pressure overload were also inhibited by APC and APC-2Cys but not by APC-E170A. Therefore, the cardiac AMPK protects against pressure overload-induced hypertrophy and the signaling selective APC-2Cys may have therapeutic potential for treating hypertension-related hypertrophy without increasing the risk of bleeding.
[Mh] Termos MeSH primário: Pressão Sanguínea
Cardiomegalia/fisiopatologia
Hipertensão/fisiopatologia
Proteína C/metabolismo
Proteínas Quinases/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Resistência à Proteína C Ativada
Animais
Cardiomegalia/patologia
Hipertensão/patologia
Camundongos
Camundongos Endogâmicos C57BL
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein C); EC 2.7.- (Protein Kinases); EC 2.7.1.- (AMP-activated protein kinase kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE


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[PMID]:29254294
[Au] Autor:Bednarczyk M; Muc-Wierzgon M; Waniczek D; Fatyga E; Klakla K; Mazurek U; Wierzgon J
[Ad] Endereço:School of Pharmacy with the Division of Laboratory Medicine in Sosnowiec, Medical University of Silesia, Department of Molecular Biology, Sosnowiec, Poland.
[Ti] Título:Autophagy-related gene expression in colorectal cancer patients.
[So] Source:J Biol Regul Homeost Agents;31(4):923-927, 2017 Oct-Dec.
[Is] ISSN:0393-974X
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:There is evidence that autophagy can play a dual role in tumor cells – as a tumor suppressor, and a process involved in tumor cell survival. The aim of this work was to assess the expression of the genes engaged in the autophagy process in biopsies taken from the colon, confirmed as adenocarcinoma, and normal tissue and to relate them to the clinical stage of the tumor. A total of 20 pairs of surgically removed tumors and healthy (marginal) tissue samples from colorectal cancer patients at clinical stages (CS) I-IV were analyzed. Gene expression profile analysis was performed using HG-U133A microarrays. Differentially expressed genes were identified, using the PL-Grid Infrastructure. Only for CSI, there were two specific genes: FOXO1 and BNIP1; further in CSII – LAMP2, MET and BCL2L, in CSIII – HIF1A and 2 ID mRNAs for HGF and 18 genes were specific for CSIV in comparison to controls. PINK1 is the only gene that differentiates all transcriptome groups from controls. Furthermore, examination of the expression of genes associated with the autophagy process may allow for better knowledge and understanding of the processes occurring during the development of colon cancer. The presented genes may be used as prognostic markers of clinical stages of colorectal cancer, contributing to the development of new lines of therapy focused on reducing metastasis of the primary tumor.
[Mh] Termos MeSH primário: Adenocarcinoma/genética
Autofagia/genética
Colo/metabolismo
Neoplasias Colorretais/genética
Regulação Neoplásica da Expressão Gênica
Transcriptoma
[Mh] Termos MeSH secundário: Adenocarcinoma/metabolismo
Adenocarcinoma/patologia
Adulto
Idoso
Idoso de 80 Anos ou mais
Colo/patologia
Neoplasias Colorretais/metabolismo
Neoplasias Colorretais/patologia
Feminino
Proteína Forkhead Box O1/genética
Proteína Forkhead Box O1/metabolismo
Perfilação da Expressão Gênica
Seres Humanos
Subunidade alfa do Fator 1 Induzível por Hipóxia/genética
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Proteína 2 de Membrana Associada ao Lisossomo/genética
Proteína 2 de Membrana Associada ao Lisossomo/metabolismo
Masculino
Meia-Idade
Estadiamento de Neoplasias
Análise de Sequência com Séries de Oligonucleotídeos
Proteínas Quinases/genética
Proteínas Quinases/metabolismo
Proteínas Proto-Oncogênicas c-bcl-2/genética
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Proteínas Proto-Oncogênicas c-met/genética
Proteínas Proto-Oncogênicas c-met/metabolismo
Proteína bcl-X/genética
Proteína bcl-X/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BCL2L1 protein, human); 0 (BNIP1 protein, human); 0 (FOXO1 protein, human); 0 (Forkhead Box Protein O1); 0 (HIF1A protein, human); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (LAMP2 protein, human); 0 (Lysosomal-Associated Membrane Protein 2); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (bcl-X Protein); EC 2.7.- (Protein Kinases); EC 2.7.10.1 (MET protein, human); EC 2.7.10.1 (Proto-Oncogene Proteins c-met); EC 2.7.11.1 (PTEN-induced putative kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


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[PMID]:29241732
[Au] Autor:Park YS; Choi SE; Koh HC
[Ad] Endereço:Department of Pharmacology, College of Medicine, Hanyang University, Seoul, Republic of Korea; Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul, Republic of Korea.
[Ti] Título:PGAM5 regulates PINK1/Parkin-mediated mitophagy via DRP1 in CCCP-induced mitochondrial dysfunction.
[So] Source:Toxicol Lett;284:120-128, 2018 Mar 01.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondrial dynamics and mitophagy are critical processes for regulating mitochondrial homeostasis. Phosphoglycerate mutase family member 5 (PGAM5) is a mitochondrial protein that plays crucial roles in apoptosis and necroptosis, but the roles of PGAM5 in mitochondrial dynamics and mitophagy remain unclear. In this study, we investigated the role of PGAM5 in carbonyl cyanide m-chlorophenylhydrazone (CCCP)-induced mitochondrial damage and the correlation between mitochondrial dynamics and mitophagy using SH-SY5Y cells. We found that CCCP decreased mitochondrial membrane potential, resulting in mitochondrial dysfunction. CCCP increased PGAM5, dynamin-related protein 1 (DRP1), and optic atrophy 1 (OPA1) expression of the mitochondrial fraction in a time-dependent manner. Knockdown of PGAM5 inhibited DRP1 translocation without a change in OPA1 expression in CCCP-treated cells. Furthermore, knockdown of PGAM5 and DRP1 significantly blocked the increase of PTEN-induced putative protein kinase 1 (PINK1) and Parkin expression in the mitochondrial fraction of CCCP-treated cells. Interestingly, CCCP did not alter PINK1/Parkin expression in the mitochondrial fraction of OPA1 knockdown cells. Inhibiting mitophagy by PGAM5 knockdown accelerated CCCP-induced apoptosis. CCCP treatment also results in PINK1 stabilization on the mitochondrial membrane, which subsequently increases Parkin recruitment from the cytosol to abnormal mitochondria. In addition, we found that CCCP increased the level of mitochondrial LC3II, indicating that Parkin recruitment of PINK1 is a result of mitophagy. We propose that activation of PGAM5 is associated with DRP1 recruitment and PINK1 stabilization, which contribute to the modulation of mitophagy in CCCP-treated cells with mitochondrial dysfunction. In conclusion, we demonstrated that PGAM5 regulates PINK1-Parkin-mediated mitophagy, which can exert a neuroprotective effect against CCCP-induced apoptosis.
[Mh] Termos MeSH primário: Carbonil Cianeto m-Clorofenil Hidrazona/toxicidade
GTP Fosfo-Hidrolases/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Degradação Mitocondrial/efeitos dos fármacos
Proteínas Mitocondriais/metabolismo
Fosfoproteínas Fosfatases/metabolismo
Proteínas Quinases/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
GTP Fosfo-Hidrolases/genética
Técnicas de Silenciamento de Genes
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Proteínas Associadas aos Microtúbulos/genética
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Mitocôndrias/patologia
Proteínas Mitocondriais/genética
Fosfoproteínas Fosfatases/genética
Proteínas Quinases/genética
Ubiquitina-Proteína Ligases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins); 0 (Mitochondrial Proteins); 555-60-2 (Carbonyl Cyanide m-Chlorophenyl Hydrazone); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (parkin protein); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (PTEN-induced putative kinase); EC 3.1.3.16 (PGAM5 protein, human); EC 3.1.3.16 (Phosphoprotein Phosphatases); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.5 (DNM1L protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE


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[PMID]:28467943
[Au] Autor:Tian X; Seluanov A; Gorbunova V
[Ad] Endereço:Department of Biology, University of Rochester, Rochester, NY 14627, USA.
[Ti] Título:Beyond Making Ends Meet: DNA-PK, Metabolism, and Aging.
[So] Source:Cell Metab;25(5):991-992, 2017 May 02.
[Is] ISSN:1932-7420
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA-dependent protein kinase (DNA-PK), a central player in DNA double-strand break (DSB) repair, shows emerging roles in metabolic regulation. In this issue of Cell Metabolism, Park et al. (2017) elucidate a molecular mechanism whereby DNA-PK negatively regulates AMPK, contributing to metabolic and fitness decline during aging.
[Mh] Termos MeSH primário: Envelhecimento
Dano ao DNA
Proteína Quinase Ativada por DNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Quebras de DNA de Cadeia Dupla
Proteínas de Choque Térmico HSP90/metabolismo
Seres Humanos
Redes e Vias Metabólicas
Proteínas Quinases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HSP90 Heat-Shock Proteins); EC 2.7.- (Protein Kinases); EC 2.7.1.- (AMP-activated protein kinase kinase); EC 2.7.11.1 (DNA-Activated Protein Kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


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[PMID]:28462528
[Au] Autor:Tonnus W; Linkermann A
[Ad] Endereço:Division of Nephrology, Department of Internal Medicine III, University Hospital Carl Gustav Carus at the Technische Universität Dresden, Dresden, Germany.
[Ti] Título:The in vivo evidence for regulated necrosis.
[So] Source:Immunol Rev;277(1):128-149, 2017 05.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Necrosis is a hallmark of several widespread diseases or their direct complications. In the past decade, we learned that necrosis can be a regulated process that is potentially druggable. RIPK3- and MLKL-mediated necroptosis represents by far the best studied pathway of regulated necrosis. During necroptosis, the release of damage-associated molecular patterns (DAMPs) drives a phenomenon referred to as necroinflammation, a common consequence of necrosis. However, most studies of regulated necrosis investigated cell lines in vitro in a cell autonomous manner, which represents a non-physiological situation. Conclusions based on such work might not necessarily be transferrable to disease states in which synchronized, non-cell autonomous effects occur. Here, we summarize the current knowledge of the pathophysiological relevance of necroptosis in vivo, and in light of this understanding, we reassess the morphological classification of necrosis that is generally used by pathologists. Along these lines, we discuss the paucity of data implicating necroptosis in human disease. Finally, the in vivo relevance of non-necroptotic forms of necrosis, such as ferroptosis, is addressed.
[Mh] Termos MeSH primário: Inflamação
Ferro/metabolismo
Necrose
[Mh] Termos MeSH secundário: Animais
Microambiente Celular
Colágeno
Seres Humanos
Proteínas Quinases/metabolismo
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Receptores de Reconhecimento de Padrão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Receptors, Pattern Recognition); 9007-34-5 (Collagen); E1UOL152H7 (Iron); EC 2.7.- (MLKL protein, human); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (RIPK3 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
[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:170503
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12551


  10 / 38271 MEDLINE  
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[PMID]:28462524
[Au] Autor:Upton JW; Shubina M; Balachandran S
[Ad] Endereço:Department of Molecular Biosciences, LaMontagne Center for Infectious Disease, University of Texas, Austin, TX, USA.
[Ti] Título:RIPK3-driven cell death during virus infections.
[So] Source:Immunol Rev;277(1):90-101, 2017 05.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The programmed self-destruction of infected cells is a powerful antimicrobial strategy in metazoans. For decades, apoptosis represented the dominant mechanism by which the virus-infected cell was thought to undergo programmed cell death. More recently, however, new mechanisms of cell death have been described that are also key to host defense. One such mechanism in vertebrates is programmed necrosis, or "necroptosis", driven by receptor-interacting protein kinase 3 (RIPK3). Once activated by innate immune stimuli, including virus infections, RIPK3 phosphorylates the mixed lineage kinase domain-like protein (MLKL), which then disrupts cellular membranes to effect necroptosis. Emerging evidence demonstrates that RIPK3 can also mediate apoptosis and regulate inflammasomes. Here, we review studies on the mechanisms by which viruses activate RIPK3 and the pathways engaged by RIPK3 that drive cell death.
[Mh] Termos MeSH primário: Inflamassomos/metabolismo
Proteínas Quinases/metabolismo
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Viroses/imunologia
Vírus/imunologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Seres Humanos
Imunidade Inata
Necrose
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Inflammasomes); EC 2.7.- (MLKL protein, human); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (RIPK3 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
[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:170503
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12539



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