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Pesquisa : D08.811.277.151.486.250 [Categoria DeCS]
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[PMID]:29335468
[Au] Autor:Teater M; Dominguez PM; Redmond D; Chen Z; Ennishi D; Scott DW; Cimmino L; Ghione P; Chaudhuri J; Gascoyne RD; Aifantis I; Inghirami G; Elemento O; Melnick A; Shaknovich R
[Ad] Endereço:Department of Medicine, Division of Hematology and Medical Oncology, Weill Cornell Medicine, New York, NY, 10021, USA.
[Ti] Título:AICDA drives epigenetic heterogeneity and accelerates germinal center-derived lymphomagenesis.
[So] Source:Nat Commun;9(1):222, 2018 01 15.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Epigenetic heterogeneity is emerging as a feature of tumors. In diffuse large B-cell lymphoma (DLBCL), increased cytosine methylation heterogeneity is associated with poor clinical outcome, yet the underlying mechanisms remain unclear. Activation-induced cytidine deaminase (AICDA), an enzyme that mediates affinity maturation and facilitates DNA demethylation in germinal center (GC) B cells, is required for DLBCL pathogenesis and linked to inferior outcome. Here we show that AICDA overexpression causes more aggressive disease in BCL2-driven murine lymphomas. This phenotype is associated with increased cytosine methylation heterogeneity, but not with increased AICDA-mediated somatic mutation burden. Reciprocally, the cytosine methylation heterogeneity characteristic of normal GC B cells is lost upon AICDA depletion. These observations are relevant to human patients, since DLBCLs with high AICDA expression manifest increased methylation heterogeneity vs. AICDA-low DLBCLs. Our results identify AICDA as a driver of epigenetic heterogeneity in B-cell lymphomas with potential significance for other tumors with aberrant expression of cytidine deaminases.
[Mh] Termos MeSH primário: Citidina Desaminase/genética
Epigênese Genética
Centro Germinativo/metabolismo
Linfoma Difuso de Grandes Células B/genética
[Mh] Termos MeSH secundário: Animais
Linfócitos B/metabolismo
Linfócitos B/patologia
Citidina Desaminase/metabolismo
Perfilação da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Linfoma Difuso de Grandes Células B/enzimologia
Linfoma Difuso de Grandes Células B/metabolismo
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[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:180117
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02595-w


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[PMID]:29199976
[Au] Autor:Lee S; Wang C; Liu H; Xiong J; Jiji R; Hong X; Yan X; Chen Z; Hammel M; Wang Y; Dai S; Wang J; Jiang C; Zhang G
[Ad] Endereço:Department of Biomedical Research, National Jewish Health, Denver, CO 80206, USA.
[Ti] Título:Hydrogen bonds are a primary driving force for de novo protein folding.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 12):955-969, 2017 Dec 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The protein-folding mechanism remains a major puzzle in life science. Purified soluble activation-induced cytidine deaminase (AID) is one of the most difficult proteins to obtain. Starting from inclusion bodies containing a C-terminally truncated version of AID (residues 1-153; AID ), an optimized in vitro folding procedure was derived to obtain large amounts of AID , which led to crystals with good quality and to final structural determination. Interestingly, it was found that the final refolding yield of the protein is proline residue-dependent. The difference in the distribution of cis and trans configurations of proline residues in the protein after complete denaturation is a major determining factor of the final yield. A point mutation of one of four proline residues to an asparagine led to a near-doubling of the yield of refolded protein after complete denaturation. It was concluded that the driving force behind protein folding could not overcome the cis-to-trans proline isomerization, or vice versa, during the protein-folding process. Furthermore, it was found that successful refolding of proteins optimally occurs at high pH values, which may mimic protein folding in vivo. It was found that high pH values could induce the polarization of peptide bonds, which may trigger the formation of protein secondary structures through hydrogen bonds. It is proposed that a hydrophobic environment coupled with negative charges is essential for protein folding. Combined with our earlier discoveries on protein-unfolding mechanisms, it is proposed that hydrogen bonds are a primary driving force for de novo protein folding.
[Mh] Termos MeSH primário: Citidina Desaminase/química
Ligações de Hidrogênio
Dobramento de Proteína
[Mh] Termos MeSH secundário: Seres Humanos
Prolina/química
Conformação Proteica
Desnaturação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9DLQ4CIU6V (Proline); EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317015303


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[PMID]:29292195
[Au] Autor:Luo MT; Fan Y; Mu D; Yao YG; Zheng YT
[Ad] Endereço:Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China; Kunming College of Life Science, University of Chinese Ac
[Ti] Título:Molecular cloning and characterization of APOBEC3 family in tree shrew.
[So] Source:Gene;646:143-152, 2018 Mar 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The APOBEC3 family is a series antiviral factors that inhibit the replication of many viruses, such as HIV-1 and HBV. Tree shrews (Tupaia belangeri) possess great potential as an animal model for human diseases and therapeutic responses. However, the APOBEC3 family is unknown in tree shrews. Recent work has showed the presence of the APOBEC3 family in tree shrews. In this work, the cDNA sequences of five APOBEC3 members were identified in tree shrews, namely, tsAPOBEC3A, -3C, -3F, -3G and -3H. The results showed that their sequences encoded a zinc (Z)-coordinating-domain as a characteristic of APOBEC3 proteins. Phylogenetic analysis revealed that the tree shrew APOBEC3 (tsAPOBEC3) genes have occurred independently and that they are clustered with other mammalian APOBEC3 members. Transcript expression analysis indicated that tsAPOBEC3 genes are constitutively expressed, and high in immune-related tissues. tsAPOBEC3 gene expression was up-regulated in hepatocytes and PBMCs by IFN-α stimulation. Finally, tsAPOBEC3 proteins could edit both sides of DNA by inserting G→A and C→T hypermutations. Overall, the results suggest that the tsAPOBEC3 family could play a key role in defense immunity through distinct editing mechanisms. Our results provided insights into the genetic basis for the development of a tree shrew model for studying viral infection. Future studies will focus on deepening our understanding on the antiviral functions of these editing enzymes in tree shrew.
[Mh] Termos MeSH primário: Clonagem Molecular/métodos
Citidina Desaminase/genética
Citidina Desaminase/metabolismo
Tupaiidae/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência Conservada
Citidina Desaminase/química
Regulação Enzimológica da Expressão Gênica
Células Hep G2
Hepatócitos/metabolismo
Seres Humanos
Imunidade
Leucócitos Mononucleares/metabolismo
Família Multigênica
Filogenia
Domínios Proteicos
Distribuição Tecidual
Tupaiidae/genética
Tupaiidae/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE


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[PMID]:28461573
[Au] Autor:Ratiu JJ; Racine JJ; Hasham MG; Wang Q; Branca JA; Chapman HD; Zhu J; Donghia N; Philip V; Schott WH; Wasserfall C; Atkinson MA; Mills KD; Leeth CM; Serreze DV
[Ad] Endereço:The Jackson Laboratory, Bar Harbor, ME 04609.
[Ti] Título:Genetic and Small Molecule Disruption of the AID/RAD51 Axis Similarly Protects Nonobese Diabetic Mice from Type 1 Diabetes through Expansion of Regulatory B Lymphocytes.
[So] Source:J Immunol;198(11):4255-4267, 2017 06 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:B lymphocytes play a key role in type 1 diabetes (T1D) development by serving as a subset of APCs preferentially supporting the expansion of autoreactive pathogenic T cells. As a result of their pathogenic importance, B lymphocyte-targeted therapies have received considerable interest as potential T1D interventions. Unfortunately, the B lymphocyte-directed T1D interventions tested to date failed to halt ß cell demise. IgG autoantibodies marking humans at future risk for T1D indicate that B lymphocytes producing them have undergone the affinity-maturation processes of class switch recombination and, possibly, somatic hypermutation. This study found that CRISPR/Cas9-mediated ablation of the activation-induced cytidine deaminase gene required for class switch recombination/somatic hypermutation induction inhibits T1D development in the NOD mouse model. The activation-induced cytidine deaminase protein induces genome-wide DNA breaks that, if not repaired through RAD51-mediated homologous recombination, result in B lymphocyte death. Treatment with the RAD51 inhibitor 4,4'-diisothiocyanatostilbene-2, 2'-disulfonic acid also strongly inhibited T1D development in NOD mice. The genetic and small molecule-targeting approaches expanded CD73 B lymphocytes that exert regulatory activity suppressing diabetogenic T cell responses. Hence, an initial CRISPR/Cas9-mediated genetic modification approach has identified the AID/RAD51 axis as a target for a potentially clinically translatable pharmacological approach that can block T1D development by converting B lymphocytes to a disease-inhibitory CD73 regulatory state.
[Mh] Termos MeSH primário: Linfócitos B Reguladores/imunologia
Proteínas de Transporte/antagonistas & inibidores
Citidina Desaminase/antagonistas & inibidores
Diabetes Mellitus Tipo 1/imunologia
Diabetes Mellitus Tipo 1/prevenção & controle
Ativação Linfocitária
Proteínas Nucleares/antagonistas & inibidores
[Mh] Termos MeSH secundário: Ácido 4,4'-Di-Isotiocianoestilbeno-2,2'-Dissulfônico/farmacologia
5'-Nucleotidase/imunologia
Animais
Autoanticorpos/imunologia
Sistemas CRISPR-Cas
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Citidina Desaminase/genética
Citidina Desaminase/metabolismo
Diabetes Mellitus Experimental
Switching de Imunoglobulina
Camundongos
Camundongos Endogâmicos NOD
Proteínas Nucleares/deficiência
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Hipermutação Somática de Imunoglobulina
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Carrier Proteins); 0 (Nuclear Proteins); 0 (Rad51ap1 protein, mouse); EC 3.1.3.5 (5'-Nucleotidase); EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase); Q1O6DSW23R (4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180127
[Lr] Data última revisão:
180127
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700024


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[PMID]:29191651
[Au] Autor:Fang Y; Xiao X; Li SX; Wolfe A; Chen XS
[Ad] Endereço:Molecular and Computational Biology, Departments of Biological Sciences and Chemistry, University of Southern California, Los Angeles, CA 90089, USA; 161 Hospital of PLA, Wuhan, 430012, China; Department of Clinical Microbiology and Immunology of Southwest Hospital, Third Military Medical University
[Ti] Título:Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.
[So] Source:J Mol Biol;430(1):87-101, 2018 Jan 05.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The single-stranded DNA (ssDNA) cytidine deaminase APOBEC3F (A3F) deaminates cytosine (C) to uracil (U) and is a known restriction factor of HIV-1. Its C-terminal catalytic domain (CD2) alone is capable of binding single-stranded nucleic acids and is important for deamination. However, little is known about how the CD2 interacts with ssDNA. Here we report a crystal structure of A3F-CD2 in complex with a 10-nucleotide ssDNA composed of poly-thymine, which reveals a novel positively charged nucleic acid binding site distal to the active center that plays a key role in substrate DNA binding and catalytic activity. Lysine and tyrosine residues within this binding site interact with the ssDNA, and mutating these residues dramatically impairs both ssDNA binding and catalytic activity. This binding site is not conserved in APOBEC3G (A3G), which may explain differences in ssDNA-binding characteristics between A3F-CD2 and A3G-CD2. In addition, we observed an alternative Zn-coordination conformation around the active center. These findings reveal the structural relationships between nucleic acid interactions and catalytic activity of A3F.
[Mh] Termos MeSH primário: Citidina Desaminase/metabolismo
DNA de Cadeia Simples/metabolismo
[Mh] Termos MeSH secundário: Desaminase APOBEC-3G/metabolismo
Sequência de Aminoácidos
Sítios de Ligação/fisiologia
Domínio Catalítico/fisiologia
Citosina Desaminase/metabolismo
Desaminação/fisiologia
Escherichia coli/metabolismo
HIV-1/metabolismo
Seres Humanos
Ligação Proteica/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Single-Stranded); EC 3.5.4.1 (Cytosine Deaminase); EC 3.5.4.5 (APOBEC-3G Deaminase); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


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[PMID]:29220655
[Au] Autor:Pannunzio NR; Lieber MR
[Ad] Endereço:USC Norris Comprehensive Cancer Center, University of Southern California Keck School of Medicine, 1441 Eastlake Avenue, Rm. 5428, Los Angeles, CA 90089, USA.
[Ti] Título:AID and Reactive Oxygen Species Can Induce DNA Breaks within Human Chromosomal Translocation Fragile Zones.
[So] Source:Mol Cell;68(5):901-912.e3, 2017 Dec 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA double-strand breaks (DSBs) occurring within fragile zones of less than 200 base pairs account for the formation of the most common human chromosomal translocations in lymphoid malignancies, yet the mechanism of how breaks occur remains unknown. Here, we have transferred human fragile zones into S. cerevisiae in the context of a genetic assay to understand the mechanism leading to DSBs at these sites. Our findings indicate that a combination of factors is required to sensitize these regions. Foremost, DNA strand separation by transcription or increased torsional stress can expose these DNA regions to damage from either the expression of human AID or increased oxidative stress. This damage causes DNA lesions that, if not repaired quickly, are prone to nuclease cleavage, resulting in DSBs. Our results provide mechanistic insight into why human neoplastic translocation fragile DNA sequences are more prone to enzymes or agents that cause longer-lived DNA lesions.
[Mh] Termos MeSH primário: Cromossomos Humanos/genética
Citidina Desaminase/genética
Quebras de DNA de Cadeia Dupla
DNA Fúngico/genética
Estresse Oxidativo
Espécies Reativas de Oxigênio/metabolismo
Saccharomyces cerevisiae/genética
Translocação Genética
[Mh] Termos MeSH secundário: Cromossomos Humanos/química
Cromossomos Humanos/metabolismo
Citidina Desaminase/metabolismo
DNA Fúngico/química
DNA Fúngico/metabolismo
Endonucleases/genética
Endonucleases/metabolismo
Regulação Enzimológica da Expressão Gênica
Regulação Fúngica da Expressão Gênica
Seres Humanos
Conformação de Ácido Nucleico
Peroxidases/genética
Peroxidases/metabolismo
Saccharomyces cerevisiae/enzimologia
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Relação Estrutura-Atividade
Transcrição Genética
Uracila-DNA Glicosidase/genética
Uracila-DNA Glicosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Reactive Oxygen Species); 0 (Saccharomyces cerevisiae Proteins); EC 1.11.1.- (Peroxidases); EC 1.11.1.- (Tsa1 protein, S cerevisiae); EC 3.1.- (Endonucleases); EC 3.1.- (artemis nuclease, human); EC 3.2.2.- (Uracil-DNA Glycosidase); EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


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[PMID]:28471629
[Au] Autor:Shamriz O; Molho-Pessach V; Shaag A; Daum H; Stepensky P
[Ad] Endereço:Pediatric Division, Hadassah-Hebrew University Medical Center, Ein Kerem Campus, Jerusalem, Israel.
[Ti] Título:Coexistence of Two Rare Autosomal Recessive Disorders: Activation-Induced Cytidine Deaminase Deficiency and Sjogren-Larsson Syndrome.
[So] Source:Isr Med Assoc J;18(10):636-638, 2016 Oct.
[Is] ISSN:1565-1088
[Cp] País de publicação:Israel
[La] Idioma:eng
[Mh] Termos MeSH primário: Citidina Desaminase/genética
Síndrome de Imunodeficiência com Hiper-IgM/diagnóstico
Síndrome de Sjogren-Larsson/diagnóstico
[Mh] Termos MeSH secundário: Criança
Seres Humanos
Síndrome de Imunodeficiência com Hiper-IgM/genética
Masculino
Mutação
Irmãos
Síndrome de Sjogren-Larsson/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


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[PMID]:28972092
[Au] Autor:Chen Y; Hu F; Dong X; Zhao M; Wang J; Sun X; Kim TJ; Li Z; Liu W
[Ad] Endereço:Ministry of Education Key Laboratory of Protein Sciences, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, School of Life Sciences, Tsinghua University, Beijing 100084, China.
[Ti] Título:SHIP-1 Deficiency in AID B Cells Leads to the Impaired Function of B10 Cells with Spontaneous Autoimmunity.
[So] Source:J Immunol;199(9):3063-3073, 2017 Nov 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Unlike conventional B cells, regulatory B cells exhibit immunosuppressive functions to downregulate inflammation via IL-10 production. However, the molecular mechanism regulating the production of IL-10 is not fully understood. In this study, we report the finding that activation-induced cytidine deaminase (AID) is highly upregulated in the IL-10-competent B cell (B10) cell from Innp5d Aicda mice, whereas the 5' inositol phosphatase SHIP-1 is downregulated. Notably, SHIP-1 deficiency in AID B cells leads to a reduction in cell count and impaired IL-10 production by B10 cells. Furthermore, the Innp5d Aicda mouse model shows B cell-dependent autoimmune lupus-like phenotypes, such as elevated IgG serum Abs, formation of spontaneous germinal centers, production of anti-dsDNA and anti-nuclear Abs, and the obvious deposition of IgG immune complexes in the kidney with age. We observe that these lupus-like phenotypes can be reversed by the adoptive transfer of B10 cells from control Innp5d mice, but not from the Innp5d Aicda mice. This finding highlights the importance of defective B10 cells in Innp5d Aicda mice. Whereas p-Akt is significantly upregulated, MAPK and AP-1 activation is impaired in B10 cells from Innp5d Aicda mice, resulting in the reduced production of IL-10. These results show that SHIP-1 is required for the maintenance of B10 cells and production of IL-10, and collectively suggests that SHIP-1 could be a new potential therapeutic target for the treatment of autoimmune diseases.
[Mh] Termos MeSH primário: Subpopulações de Linfócitos B/imunologia
Citidina Desaminase/imunologia
Interleucina-10/imunologia
Lúpus Eritematoso Sistêmico/imunologia
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/deficiência
[Mh] Termos MeSH secundário: Transferência Adotiva
Animais
Subpopulações de Linfócitos B/patologia
Citidina Desaminase/genética
MAP Quinases Reguladas por Sinal Extracelular/genética
MAP Quinases Reguladas por Sinal Extracelular/imunologia
Centro Germinativo/imunologia
Centro Germinativo/patologia
Interleucina-10/genética
Lúpus Eritematoso Sistêmico/genética
Lúpus Eritematoso Sistêmico/patologia
Lúpus Eritematoso Sistêmico/terapia
Camundongos
Camundongos Transgênicos
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/imunologia
Proteínas Proto-Oncogênicas c-akt/genética
Proteínas Proto-Oncogênicas c-akt/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL10 protein, mouse); 130068-27-8 (Interleukin-10); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases); EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700138


  9 / 2836 MEDLINE  
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[PMID]:28939756
[Au] Autor:Liu J; Xiong E; Zhu H; Mori H; Yasuda S; Kinoshita K; Tsubata T; Wang JY
[Ad] Endereço:Department of Immunology, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
[Ti] Título:Efficient Induction of Ig Gene Hypermutation in Ex Vivo-Activated Primary B Cells.
[So] Source:J Immunol;199(9):3023-3030, 2017 Nov 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Activation-induced cytidine deaminase (AID) initiates both somatic hypermutation (SHM) and class switch recombination (CSR) of Ig genes. How AID is targeted to the Ig V gene and switch region to trigger SHM and CSR remains elusive. Primary B cells stimulated with CD40L plus IL-4 or LPS plus IL-4 undergo efficient CSR, but it has been difficult to induce SHM in these cells. In the current study, we used B cells from B1-8 mice carrying a prerecombined V 186.2DFL16.1J 2 Ab gene to investigate the induction of SHM under in vitro culture conditions. B1-8 splenic B cells stimulated with CD40L plus IL-4 or LPS plus IL-4 underwent robust CSR to IgG , but failed to generate SHM in the V 186.2 gene. Remarkably, ectopic expression of AID in AID-deficient, but not wild-type, B1-8 B cells induced efficient SHM at a rate close to that observed in germinal center B cells. We further established an AID-deficient CH12 B lymphoma line and found that ectopic expression of AID in the mutant line, but not in AID-sufficient CH12 cells, induced efficient point mutations and deletions in the V gene. These results demonstrate that the endogenous AID in ex vivo-activated primary B and B lymphoma cells not only cannot induce SHM but also inhibit the induction of SHM by the exogenous AID. Our results further suggest that the spatiotemporal distribution and/or posttranslational modification of AID strongly affects the induction of SHM in ex vivo-activated primary B cells.
[Mh] Termos MeSH primário: Linfócitos B/imunologia
Citidina Desaminase/imunologia
Imunoglobulina G/imunologia
Ativação Linfocitária
Hipermutação Somática de Imunoglobulina
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Citidina Desaminase/genética
Imunoglobulina G/genética
Camundongos
Camundongos Knockout
Mutação Puntual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulin G); EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170924
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700868


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[PMID]:28841445
[Au] Autor:Molan AM; Hanson HM; Chweya CM; Anderson BD; Starrett GJ; Richards CM; Harris RS
[Ad] Endereço:Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA; Institute for Molecular Virology, University of Minnesota, Minneapolis, MN 55455, USA; Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455, USA.
[Ti] Título:APOBEC3B lysine residues are dispensable for DNA cytosine deamination, HIV-1 restriction, and nuclear localization.
[So] Source:Virology;511:74-81, 2017 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The APOBEC3 DNA cytosine deaminase family comprises a fundamental arm of the innate immune response and is best known for retrovirus restriction. Several APOBEC3 enzymes restrict HIV-1 and related retroviruses by deaminating viral cDNA cytosines to uracils compromising viral genomes. Human APOBEC3B (A3B) shows strong virus restriction activities in a variety of experimental systems, and is subjected to tight post-translational regulation evidenced by cell-specific HIV-1 restriction activity and active nuclear import. Here we ask whether lysines and/or lysine post-translational modifications are required for these A3B activities. A lysine-free derivative of human A3B was constructed and shown to be indistinguishable from the wild-type enzyme in DNA cytosine deamination, HIV-1 restriction, and nuclear localization activities. However, lysine loss did render the protein resistant to degradation by SIV Vif. Taken together, we conclude that lysine side chains and modifications thereof are unlikely to be central to A3B function or regulation in human cells.
[Mh] Termos MeSH primário: Citidina Desaminase/genética
Citidina Desaminase/metabolismo
Análise Mutacional de DNA
Lisina/genética
Lisina/metabolismo
Antígenos de Histocompatibilidade Menor/genética
Antígenos de Histocompatibilidade Menor/metabolismo
Proteínas Mutantes/genética
Proteínas Mutantes/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Citosina/metabolismo
Desaminação
Células HEK293
HIV-1/imunologia
Seres Humanos
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Minor Histocompatibility Antigens); 0 (Mutant Proteins); 8J337D1HZY (Cytosine); EC 3.5.4.5 (APOBEC3B protein, human); EC 3.5.4.5 (Cytidine Deaminase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170826
[St] Status:MEDLINE



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