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Pesquisa : D12.776.157 [Categoria DeCS]
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[PMID]:29351317
[Au] Autor:Merrick BA; Chang JS; Phadke DP; Bostrom MA; Shah RR; Wang X; Gordon O; Wright GM
[Ad] Endereço:Biomolecular Screening Branch, Division National Toxicology Program, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina, United States of America.
[Ti] Título:HAfTs are novel lncRNA transcripts from aflatoxin exposure.
[So] Source:PLoS One;13(1):e0190992, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The transcriptome can reveal insights into precancer biology. We recently conducted RNA-Seq analysis on liver RNA from male rats exposed to the carcinogen, aflatoxin B1 (AFB1), for 90 days prior to liver tumor onset. Among >1,000 differentially expressed transcripts, several novel, unannotated Cufflinks-assembled transcripts, or HAfTs (Hepatic Aflatoxin Transcripts) were found. We hypothesized PCR-cloning and RACE (rapid amplification of cDNA ends) could further HAfT identification. Sanger data was obtained for 6 transcripts by PCR and 16 transcripts by 5'- and 3'-RACE. BLAST alignments showed, with two exceptions, HAfT transcripts were lncRNAs, >200nt without apparent long open reading frames. Six rat HAfT transcripts were classified as 'novel' without RefSeq annotation. Sequence alignment and genomic synteny showed each rat lncRNA had a homologous locus in the mouse genome and over half had homologous loci in the human genome, including at least two loci (and possibly three others) that were previously unannotated. While HAfT functions are not yet clear, coregulatory roles may be possible from their adjacent orientation to known coding genes with altered expression that include 8 HAfT-gene pairs. For example, a unique rat HAfT, homologous to Pvt1, was adjacent to known genes controlling cell proliferation. Additionally, PCR and RACE Sanger sequencing showed many alternative splice variants and refinements of exon sequences compared to Cufflinks assembled transcripts and gene prediction algorithms. Presence of multiple splice variants and short tandem repeats found in some HAfTs may be consequential for secondary structure, transcriptional regulation, and function. In summary, we report novel, differentially expressed lncRNAs after exposure to the genotoxicant, AFB1, prior to neoplastic lesions. Complete cloning and sequencing of such transcripts could pave the way for a new set of sensitive and early prediction markers for chemical hepatocarcinogens.
[Mh] Termos MeSH primário: Aflatoxina B1/toxicidade
Proteínas de Transporte/genética
Fígado/metabolismo
RNA Longo não Codificante/genética
RNA Mensageiro/genética
[Mh] Termos MeSH secundário: Aflatoxina B1/metabolismo
Animais
Seres Humanos
Masculino
Camundongos
Reação em Cadeia da Polimerase
Ratos
Ratos Endogâmicos F344
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (RNA, Long Noncoding); 0 (RNA, Messenger); 9N2N2Y55MH (Aflatoxin B1)
[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:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190992


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[PMID]:29346429
[Au] Autor:Ferrigno A; Di Pasqua LG; Berardo C; Siciliano V; Rizzo V; Adorini L; Richelmi P; Vairetti M
[Ad] Endereço:Department of Internal Medicine and Therapeutics, University of Pavia, Pavia, Italy.
[Ti] Título:The farnesoid X receptor agonist obeticholic acid upregulates biliary excretion of asymmetric dimethylarginine via MATE-1 during hepatic ischemia/reperfusion injury.
[So] Source:PLoS One;13(1):e0191430, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: We previously showed that increased asymmetric dimethylarginine (ADMA) biliary excretion occurs during hepatic ischemia/reperfusion (I/R), prompting us to study the effects of the farnesoid X receptor (FXR) agonist obeticholic acid (OCA) on bile, serum and tissue levels of ADMA after I/R. MATERIAL AND METHODS: Male Wistar rats were orally administered 10mg/kg/day of OCA or vehicle for 5 days and were subjected to 60 min partial hepatic ischemia or sham-operated. After a 60 min reperfusion, serum, tissue and bile ADMA levels, liver mRNA and protein expression of ADMA transporters (CAT-1, CAT-2A, CAT-2B, OCT-1, MATE-1), and enzymes involved in ADMA synthesis (protein-arginine-N-methyltransferase-1, PRMT-1) and metabolism (dimethylarginine-dimethylaminohydrolase-1, DDAH-1) were measured. RESULTS: OCA administration induced a further increase in biliary ADMA levels both in sham and I/R groups, with no significant changes in hepatic ADMA content. A reduction in CAT-1, CAT-2A or CAT-2B transcripts was found in OCA-treated sham-operated rats compared with vehicle. Conversely, OCA administration did not change CAT-1, CAT-2A or CAT-2B expression, already reduced by I/R. However, a marked decrease in OCT-1 and increase in MATE-1 expression was observed. A similar trend occurred with protein expression. CONCLUSION: The reduced mRNA expression of hepatic CAT transporters suggests that the increase in serum ADMA levels is probably due to decreased liver uptake of ADMA from the systemic circulation. Conversely, the mechanism involved in further increasing biliary ADMA levels in sham and I/R groups treated with OCA appears to be MATE-1-dependent.
[Mh] Termos MeSH primário: Antiporters/metabolismo
Arginina/análogos & derivados
Sistema Biliar/efeitos dos fármacos
Ácido Quenodesoxicólico/análogos & derivados
Hepatopatias/metabolismo
Proteínas de Transporte de Cátions Orgânicos/metabolismo
Receptores Citoplasmáticos e Nucleares/antagonistas & inibidores
Traumatismo por Reperfusão/metabolismo
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Arginina/sangue
Arginina/metabolismo
Arginina/secreção
Sistema Biliar/metabolismo
Sistema Biliar/secreção
Western Blotting
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Ácido Quenodesoxicólico/farmacologia
Masculino
Óxido Nítrico Sintase/metabolismo
Proteína-Arginina N-Metiltransferases/genética
RNA Mensageiro/genética
Ratos
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antiporters); 0 (Carrier Proteins); 0 (MATE1 protein, rat); 0 (Organic Cation Transport Proteins); 0 (RNA, Messenger); 0 (Receptors, Cytoplasmic and Nuclear); 0 (farnesoid X-activated receptor); 0462Z4S4OZ (obeticholic acid); 0GEI24LG0J (Chenodeoxycholic Acid); 63CV1GEK3Y (N,N-dimethylarginine); 94ZLA3W45F (Arginine); EC 1.14.13.39 (Nitric Oxide Synthase); EC 2.1.1.319 (PRMT1 protein, rat); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
[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:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191430


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[PMID]:28468915
[Au] Autor:Mei Y; Zhao L; Liu Y; Gong H; Song Y; Lei L; Zhu Y; Jin Z; Ma S; Hu B; Sun Q; Liu H
[Ad] Endereço:Institute of Blood and Marrow Transplantation, Department of Hematology, Collaborative Innovation Center of Hematology, the First Affiliated Hospital of Soochow University, Suzhou, P.R. China.
[Ti] Título:Combining DNA Vaccine and AIDA-1 in Attenuated Activates Tumor-Specific CD4 and CD8 T-cell Responses.
[So] Source:Cancer Immunol Res;5(6):503-514, 2017 Jun.
[Is] ISSN:2326-6074
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stimulation of tumor-specific responses in both CD4 and CD8 T cells has been a challenge for effective tumor vaccines. We designed a vaccine vector containing the AIDA-1 autotransporter and DNA vaccine elements, generating a murine melanoma vaccine that was delivered by the attenuated strain SL7207. Growth of murine subcutaneous melanoma was significantly inhibited by intranasal immunization with the tumor vaccine. The vaccine activated tumor-specific CD4 and CD8 T-cell responses, with increased T-cell proliferation, tumor antigen-specific Th1 cytokine production, increased percentages of tetramer positive cells, and cytotoxicity. CD4 or CD8 T-cell depletion resulted in the loss of antitumor activity of the tumor vaccine, suggesting that the efficacy of the vaccine was dependent on both CD4 and CD8 T cells. Lung metastasis of the tumor was also inhibited by vaccine treatment. Similarly, the percentages of tumor-specific Th1 cytokine production by CD4 and CD8 T cells in the spleen, tumor, and bronchoalveolar lavage were increased after vaccine treatment. Tumor-specific proliferation of CD4 and CD8 T cells was also promoted by the vaccine. Tetramer staining and cytotoxicity assay showed enhanced tumor-specific CD8 T-cell response after vaccine treatment. Therefore, the tumor vaccine could activate both tumor-specific CD4 and CD8 T-cell responses. This vaccine strategy may be widely applicable to the development of oral or nasal vaccines against tumors. .
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos/imunologia
Linfócitos T CD8-Positivos/imunologia
Vacinas Anticâncer/administração & dosagem
Neoplasias/imunologia
Salmonella
Vacinas de DNA/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte
Linhagem Celular Tumoral
Feminino
Camundongos Endogâmicos C57BL
Neoplasias/patologia
Neoplasias/terapia
Salmonella/genética
Carga Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ANKS1B protein, human); 0 (Cancer Vaccines); 0 (Carrier Proteins); 0 (Vaccines, DNA)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1158/2326-6066.CIR-16-0240-T


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[PMID]:29028222
[Au] Autor:Choi HJ; Joo HS; Won HY; Min KW; Kim HY; Son T; Oh YH; Lee JY; Kong G
[Ad] Endereço:Department of Pathology, College of Medicine, Hanyang University, Seoul, Republic of Korea; Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Republic of Korea; Institute for Bioengineering and Biopharmaceutical Research (IBBR), Hanyang University,
[Ti] Título:Role of RBP2-Induced ER and IGF1R-ErbB Signaling in Tamoxifen Resistance in Breast Cancer.
[So] Source:J Natl Cancer Inst;110(4), 2018 Apr 01.
[Is] ISSN:1460-2105
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Background: Despite the benefit of endocrine therapy, acquired resistance during or after treatment still remains a major challenge in estrogen receptor (ER)-positive breast cancer. We investigated the potential role of histone demethylase retinoblastoma-binding protein 2 (RBP2) in endocrine therapy resistance of breast cancer. Methods: Survival of breast cancer patients according to RBP2 expression was analyzed in three different breast cancer cohorts including METABRIC (n = 1980) and KM plotter (n = 1764). RBP2-mediated tamoxifen resistance was confirmed by invitro sulforhodamine B (SRB) colorimetric, colony-forming assays, and invivo xenograft models (n = 8 per group). RNA-seq analysis and receptor tyrosine kinase assay were performed to identify the tamoxifen resistance mechanism by RBP2. All statistical tests were two-sided. Results: RBP2 was associated with poor prognosis to tamoxifen therapy in ER-positive breast cancer (P = .04 in HYU cohort, P = .02 in KM plotter, P = .007 in METABRIC, log-rank test). Furthermore, RBP2 expression was elevated in patients with tamoxifen-resistant breast cancer (P = .04, chi-square test). Knockdown of RBP2 conferred tamoxifen sensitivity, whereas overexpression of RBP2 induced tamoxifen resistance invitro and invivo (MCF7 xenograft: tamoxifen-treated control, mean [SD] tumor volume = 70.8 [27.9] mm3, vs tamoxifen-treated RBP2, mean [SD] tumor volume = 387.9 [85.1] mm3, P < .001). Mechanistically, RBP2 cooperated with ER co-activators and corepressors and regulated several tamoxifen resistance-associated genes, including NRIP1, CCND1, and IGFBP4 and IGFBP5. Furthermore, epigenetic silencing of IGFBP4/5 by RBP2-ER-NRIP1-HDAC1 complex led to insulin-like growth factor-1 receptor (IGF1R) activation. RBP2 also increased IGF1R-ErbB crosstalk and subsequent PI3K-AKT activation via demethylase activity-independent ErbB protein stabilization. Combinational treatment with tamoxifen and PI3K inhibitor could overcome RBP2-mediated tamoxifen resistance (RBP2-overexpressing cells: % cell viability [SD], tamoxifen = 89.0 [3.8]%, vs tamoxifen with BKM120 = 41.3 [5.6]%, P < .001). Conclusions: RBP2 activates ER-IGF1R-ErbB signaling cascade in multiple ways to induce tamoxifen resistance, suggesting that RBP2 is a potential therapeutic target for ER-driven cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Carcinoma Ductal de Mama/metabolismo
Resistência a Medicamentos Antineoplásicos
Proteínas de Neoplasias/fisiologia
Receptores Estrogênicos/metabolismo
Proteína 2 de Ligação ao Retinoblastoma/fisiologia
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Análise de Variância
Animais
Antineoplásicos Hormonais/uso terapêutico
Neoplasias da Mama/química
Neoplasias da Mama/tratamento farmacológico
Neoplasias da Mama/patologia
Carcinoma Ductal de Mama/química
Carcinoma Ductal de Mama/tratamento farmacológico
Carcinoma Ductal de Mama/patologia
Proteínas de Transporte/metabolismo
Estudos de Coortes
Colorimetria
Intervalo Livre de Doença
Resistência a Medicamentos Antineoplásicos/genética
Feminino
Xenoenxertos
Seres Humanos
Estimativa de Kaplan-Meier
Células MCF-7
Camundongos
Camundongos Endogâmicos NOD
Camundongos SCID
Proteínas de Neoplasias/metabolismo
Células-Tronco Neoplásicas
Proteínas Nucleares/metabolismo
Fosfatidilinositol 3-Quinases/antagonistas & inibidores
Fosfatidilinositol 3-Quinases/metabolismo
Receptor ErbB-2/metabolismo
Receptor IGF Tipo 1/metabolismo
Proteína 2 de Ligação ao Retinoblastoma/metabolismo
Tamoxifeno/uso terapêutico
Carga Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Antineoplastic Agents, Hormonal); 0 (Carrier Proteins); 0 (IGFBP5-interacting protein, human); 0 (Neoplasm Proteins); 0 (Nuclear Proteins); 0 (Receptors, Estrogen); 0 (nuclear receptor interacting protein 1); 094ZI81Y45 (Tamoxifen); EC 1.14.11.27 (Retinoblastoma-Binding Protein 2); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.10.1 (Receptor, ErbB-2); EC 2.7.10.1 (Receptor, IGF Type 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1093/jnci/djx207


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[PMID]:28460636
[Au] Autor:Saugier-Veber P; Marguet F; Lecoquierre F; Adle-Biassette H; Guimiot F; Cipriani S; Patrier S; Brasseur-Daudruy M; Goldenberg A; Layet V; Capri Y; Gérard M; Frébourg T; Laquerrière A
[Ad] Endereço:Department of Genetics, Normandie Univ, UNIROUEN, INSERM U1245, Normandy Centre for Genomic and Personalized Medicine, Rouen University Hospital, F76000, Rouen, France.
[Ti] Título:Hydrocephalus due to multiple ependymal malformations is caused by mutations in the MPDZ gene.
[So] Source:Acta Neuropathol Commun;5(1):36, 2017 05 01.
[Is] ISSN:2051-5960
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Congenital hydrocephalus is considered as either acquired due to haemorrhage, infection or neoplasia or as of developmental nature and is divided into two subgroups, communicating and obstructive. Congenital hydrocephalus is either syndromic or non-syndromic, and in the latter no cause is found in more than half of the patients. In patients with isolated hydrocephalus, L1CAM mutations represent the most common aetiology. More recently, a founder mutation has also been reported in the MPDZ gene in foetuses presenting massive hydrocephalus, but the neuropathology remains unknown. We describe here three novel homozygous null mutations in the MPDZ gene in foetuses whose post-mortem examination has revealed a homogeneous phenotype characterized by multiple ependymal malformations along the aqueduct of Sylvius, the third and fourth ventricles as well as the central canal of the medulla, consisting in multifocal rosettes with immature cell accumulation in the vicinity of ependymal lining early detached from the ventricular zone. MPDZ also named MUPP1 is an essential component of tight junctions which are expressed from early brain development in the choroid plexuses and ependyma. Alterations in the formation of tight junctions within the ependyma very likely account for the lesions observed and highlight for the first time that primary multifocal ependymal malformations of the ventricular system is genetically determined in humans. Therefore, MPDZ sequencing should be performed when neuropathological examination reveals multifocal ependymal rosette formation within the aqueduct of Sylvius, of the third and fourth ventricles and of the central canal of the medulla.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
Epêndima/anormalidades
Doenças Fetais/genética
Hidrocefalia/genética
Mutação com Perda de Função
[Mh] Termos MeSH secundário: Adulto
Epêndima/diagnóstico por imagem
Família
Feminino
Doenças Fetais/diagnóstico por imagem
Doenças Fetais/etiologia
Doenças Fetais/patologia
Homozigoto
Seres Humanos
Hidrocefalia/diagnóstico por imagem
Hidrocefalia/etiologia
Hidrocefalia/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (MPDZ protein, human)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1186/s40478-017-0438-4


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[PMID]:29311697
[Au] Autor:Qureshi BM; Schmidt A; Behrmann E; Bürger J; Mielke T; Spahn CMT; Heck M; Scheerer P
[Ad] Endereço:Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, D-10117, Berlin, Germany.
[Ti] Título:Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6.
[So] Source:Nat Commun;9(1):90, 2018 01 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Isoprenylated proteins are associated with membranes and their inter-compartmental distribution is regulated by solubilization factors, which incorporate lipid moieties in hydrophobic cavities and thereby facilitate free diffusion during trafficking. Here we report the crystal structure of a solubilization factor, the prenyl-binding protein (PrBP/δ), at 1.81 Å resolution in its ligand-free apo-form. Apo-PrBP/δ harbors a preshaped, deep hydrophobic cavity, capacitating apo-PrBP/δ to readily bind its prenylated cargo. To investigate the molecular mechanism of cargo solubilization we analyzed the PrBP/δ-induced membrane dissociation of rod photoreceptor phosphodiesterase (PDE6). The results suggest that PrBP/δ exclusively interacts with the soluble fraction of PDE6. Depletion of soluble species in turn leads to dissociation of membrane-bound PDE6, as both are in equilibrium. This "solubilization by depletion" mechanism of PrBP/δ differs from the extraction of prenylated proteins by the similar folded solubilization factor RhoGDI, which interacts with membrane bound cargo via an N-terminal structural element lacking in PrBP/δ.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Nucleotídeo Cíclico Fosfodiesterase do Tipo 6/metabolismo
Neopreno/metabolismo
Células Fotorreceptoras Retinianas Bastonetes/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/química
Bovinos
Cristalografia por Raios X
Nucleotídeo Cíclico Fosfodiesterase do Tipo 6/química
Modelos Moleculares
Complexos Multiproteicos/química
Complexos Multiproteicos/metabolismo
Neopreno/química
Ligação Proteica
Domínios Proteicos
Prenilação de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Inibidores da Dissociação do Nucleotídeo Guanina rho-Específico/química
Inibidores da Dissociação do Nucleotídeo Guanina rho-Específico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Multiprotein Complexes); 0 (Protein Subunits); 0 (prenyl); 0 (rho-Specific Guanine Nucleotide Dissociation Inhibitors); 9010-98-4 (Neoprene); EC 3.1.4.35 (Cyclic Nucleotide Phosphodiesterases, Type 6)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02569-y


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[PMID]:29302025
[Au] Autor:Guéant JL; Chéry C; Oussalah A; Nadaf J; Coelho D; Josse T; Flayac J; Robert A; Koscinski I; Gastin I; Filhine-Tresarrieu P; Pupavac M; Brebner A; Watkins D; Pastinen T; Montpetit A; Hariri F; Tregouët D; Raby BA; Chung WK; Morange PE; Froese DS; Baumgartner MR; Benoist JF; Ficicioglu C; Marchand V; Motorin Y; Bonnemains C; Feillet F; Majewski J; Rosenblatt DS
[Ad] Endereço:INSERM, UMR_S954 Nutrition-Genetics-Environmental Risk Exposure and Reference Centre of Inborn Metabolism Diseases, University of Lorraine and University Hospital Centre of Nancy (CHRU Nancy), 54505, Nancy, France. jean-louis.gueant@univ-lorraine.fr.
[Ti] Título:APRDX1 mutant allele causes a MMACHC secondary epimutation in cblC patients.
[So] Source:Nat Commun;9(1):67, 2018 01 04.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To date, epimutations reported in man have been somatic and erased in germlines. Here, we identify a cause of the autosomal recessive cblC class of inborn errors of vitamin B metabolism that we name "epi-cblC". The subjects are compound heterozygotes for a genetic mutation and for a promoter epimutation, detected in blood, fibroblasts, and sperm, at the MMACHC locus; 5-azacytidine restores the expression of MMACHC in fibroblasts. MMACHC is flanked by CCDC163P and PRDX1, which are in the opposite orientation. The epimutation is present in three generations and results from PRDX1 mutations that force antisense transcription of MMACHC thereby possibly generating a H3K36me3 mark. The silencing of PRDX1 transcription leads to partial hypomethylation of the epiallele and restores the expression of MMACHC. This example of epi-cblC demonstrates the need to search for compound epigenetic-genetic heterozygosity in patients with typical disease manifestation and genetic heterozygosity in disease-causing genes located in other gene trios.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
Epistasia Genética
Erros Inatos do Metabolismo/genética
Mutação
Peroxirredoxinas/genética
Vitamina B 12/metabolismo
[Mh] Termos MeSH secundário: Alelos
Azacitidina/farmacologia
Sequência de Bases
Inibidores Enzimáticos/farmacologia
Saúde da Família
Feminino
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Heterozigoto
Seres Humanos
Masculino
Erros Inatos do Metabolismo/metabolismo
Linhagem
Sequenciamento Completo do Genoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Enzyme Inhibitors); 0 (MMACHC protein, human); EC 1.11.1.15 (PRDX1 protein, human); EC 1.11.1.15 (Peroxiredoxins); M801H13NRU (Azacitidine); P6YC3EG204 (Vitamin B 12)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02306-5


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[PMID]:28463112
[Au] Autor:Edens BM; Yan J; Miller N; Deng HX; Siddique T; Ma YC
[Ad] Endereço:Department of Pediatrics, Northwestern University Feinberg School of Medicine, Ann & Robert H Lurie Children's Hospital of Chicago, Chicago, United States.
[Ti] Título:A novel ALS-associated variant in regulates motor axon morphogenesis.
[So] Source:Elife;6, 2017 05 02.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The etiological underpinnings of amyotrophic lateral sclerosis (ALS) are complex and incompletely understood, although contributions to pathogenesis by regulators of proteolytic pathways have become increasingly apparent. Here, we present a novel variant in that is associated with ALS and show that its expression compromises motor axon morphogenesis in mouse motor neurons and in zebrafish. We further demonstrate that the ALS-associated variant impairs proteasomal function, and identify the Wnt signaling pathway effector beta-catenin as a substrate. Inhibition of beta-catenin function rescues the variant-induced motor axon phenotypes. These findings provide a strong link between the regulation of axonal morphogenesis and a new ALS-associated gene variant mediated by protein degradation pathways.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/genética
Esclerose Amiotrófica Lateral/patologia
Proteínas de Transporte/genética
Morfogênese
Neurônios Motores/citologia
Proteínas Nucleares/genética
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Camundongos
Complexo de Endopeptidases do Proteassoma/metabolismo
Proteólise
Peixe-Zebra
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Nuclear Proteins); 0 (UBQLN4 protein, human); 0 (beta Catenin); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:28460455
[Au] Autor:Zhang X; Zheng Q; Wang C; Zhou H; Jiang G; Miao Y; Zhang Y; Liu Y; Li Q; Qiu X; Wang E
[Ad] Endereço:Department of Pathology, College of Basic Medical Sciences, China Medical University, Shenyang, China.
[Ti] Título:CCDC106 promotes non-small cell lung cancer cell proliferation.
[So] Source:Oncotarget;8(16):26662-26670, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Coiled-coil domain containing (CCDC) family members enhance tumor cell proliferation, and high CCDC protein levels correlate with unfavorable prognoses. Limited research demonstrated that CCDC106 may promote the degradation of p53/TP53 protein and inhibit its transactivity. The present study demonstrated that CCDC106 expression correlates with advanced TNM stage (P = 0.008), positive regional lymph node metastasis (P < 0.001), and poor overall survival (P < 0.001) in 183 non-small cell lung cancer cases. A549 and H1299 cells were selected as representative of CCDC106-low and CCDC106-high expressing cell lines, respectively. CCDC106 overexpression promoted A549 cell proliferation and xenograft tumor growth in nude mice, while siRNA-mediated CCDC106 knockdown inhibited H1299 cell proliferation. CCDC106 promoted AKT phosphorylation and upregulated the cell cycle-regulating proteins Cyclin A2 and Cyclin B1. Cell proliferation promoted by CCDC106 via Cyclin A2 and Cyclin B1 was rescued by treatment with the AKT inhibitor, LY294002. Our studies revealed that CCDC106 is associated with non-small cell lung cancer progression and unfavorable prognosis. CCDC106 enhanced Cyclin A2 and Cyclin B1 expression and promoted A549 and H1299 cell proliferation, which depended on AKT signaling. These results suggest that CCDC106 may be a novel target for lung cancer treatment.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/genética
Proteínas de Transporte/genética
Expressão Gênica
Neoplasias Pulmonares/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Biomarcadores
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Carcinoma Pulmonar de Células não Pequenas/mortalidade
Proteínas de Transporte/metabolismo
Linhagem Celular Tumoral
Proliferação Celular/genética
Ciclina A2/genética
Ciclina A2/metabolismo
Ciclina B1/genética
Ciclina B1/metabolismo
Feminino
Seres Humanos
Neoplasias Pulmonares/metabolismo
Neoplasias Pulmonares/mortalidade
Masculino
Meia-Idade
Gradação de Tumores
Metástase Neoplásica
Estadiamento de Neoplasias
Fosforilação
Prognóstico
Proteínas Proto-Oncogênicas c-akt/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (CCDC106 protein, human); 0 (Carrier Proteins); 0 (Cyclin A2); 0 (Cyclin B1); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15792


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[PMID]:29447691
[Au] Autor:Dziarski R; Gupta D
[Ad] Endereço:Indiana University School of Medicine-Northwest, Gary, IN 46408, USA. Electronic address: rdziar@iun.edu.
[Ti] Título:A Balancing Act: PGRPs Preserve and Protect.
[So] Source:Cell Host Microbe;23(2):149-151, 2018 02 14.
[Is] ISSN:1934-6069
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:How does the immune system maintain a balance between preserving a beneficial microbiome and protecting against pathogens while also inducing effective, yet not damaging, responses? In this issue of Cell Host & Microbe, Charroux et al. (2018) reveal that, in Drosophila, this task is performed by three isoforms of PGRP-LB, a peptidoglycan-hydrolyzing amidase.
[Mh] Termos MeSH primário: Proteínas de Transporte/imunologia
Drosophila/imunologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Drosophila/imunologia
Peptidoglicano
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Drosophila Proteins); 0 (Peptidoglycan)
[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:180216
[St] Status:MEDLINE



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