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Pesquisa : G02.111.660.871.790.600.700 [Categoria DeCS]
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[PMID]:28787443
[Au] Autor:Mousas A; Ntritsos G; Chen MH; Song C; Huffman JE; Tzoulaki I; Elliott P; Psaty BM; Auer PL; Johnson AD; Evangelou E; Lettre G; Reiner AP; Blood-Cell Consortium
[Ad] Endereço:Department of Medicine, Université de Montréal, Montréal, Québec, Canada.
[Ti] Título:Rare coding variants pinpoint genes that control human hematological traits.
[So] Source:PLoS Genet;13(8):e1006925, 2017 Aug.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The identification of rare coding or splice site variants remains the most straightforward strategy to link genes with human phenotypes. Here, we analyzed the association between 137,086 rare (minor allele frequency (MAF) <1%) coding or splice site variants and 15 hematological traits in up to 308,572 participants. We found 56 such rare coding or splice site variants at P<5x10-8, including 31 that are associated with a blood-cell phenotype for the first time. All but one of these 31 new independent variants map to loci previously implicated in hematopoiesis by genome-wide association studies (GWAS). This includes a rare splice acceptor variant (rs146597587, MAF = 0.5%) in interleukin 33 (IL33) associated with reduced eosinophil count (P = 2.4x10-23), and lower risk of asthma (P = 2.6x10-7, odds ratio [95% confidence interval] = 0.56 [0.45-0.70]) and allergic rhinitis (P = 4.2x10-4, odds ratio = 0.55 [0.39-0.76]). The single new locus identified in our study is defined by a rare p.Arg172Gly missense variant (rs145535174, MAF = 0.05%) in plasminogen (PLG) associated with increased platelet count (P = 6.8x10-9), and decreased D-dimer concentration (P = 0.018) and platelet reactivity (P<0.03). Finally, our results indicate that searching for rare coding or splice site variants in very large sample sizes can help prioritize causal genes at many GWAS loci associated with complex human diseases and traits.
[Mh] Termos MeSH primário: Asma/sangue
Endometriose/sangue
Genoma Humano
Polimorfismo de Nucleotídeo Único
Rinite Alérgica/sangue
[Mh] Termos MeSH secundário: Asma/genética
Bases de Dados Genéticas
Endometriose/genética
Feminino
Produtos de Degradação da Fibrina e do Fibrinogênio/genética
Produtos de Degradação da Fibrina e do Fibrinogênio/metabolismo
Frequência do Gene
Loci Gênicos
Estudo de Associação Genômica Ampla
Seres Humanos
Interleucina-33/genética
Interleucina-33/metabolismo
Modelos Lineares
Modelos Logísticos
Masculino
Mutação de Sentido Incorreto
Fenótipo
Plasminogênio/genética
Plasminogênio/metabolismo
Contagem de Plaquetas
Análise de Componente Principal
Processamento de Proteína/genética
Rinite Alérgica/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibrin Fibrinogen Degradation Products); 0 (Interleukin-33); 0 (fibrin fragment D); 9001-91-6 (Plasminogen)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170909
[Lr] Data última revisão:
170909
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006925


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[PMID]:28649707
[Au] Autor:Ramsoomair CK; Yakely AE; Urbanski LM; Karanja K; Giaccone ZT; Siegart NM; Wang C; Gomez AV; Reitter JN; Mills KV
[Ad] Endereço:Department of Chemistry, College of the Holy Cross, Worcester, MA, USA.
[Ti] Título:Coordination of the third step of protein splicing in two cyanobacterial inteins.
[So] Source:FEBS Lett;591(14):2147-2154, 2017 Jul.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The third step of protein splicing is cyclization of Asn coupled to peptide bond cleavage. In two related cyanobacterial inteins, this step is facilitated by Asn or Gln. For a Synechococcus sp. PCC7002 intein, the isolated third step of protein splicing is more efficient with its native Asn than with substitution to Gln. For a Trichodesmium erythraeum intein, its native Gln facilitates the third step as efficiently as with Asn. Despite these differences, the yield of splicing is not affected, suggesting that the third step is influenced by mechanism-linked conformational changes. A conserved catalytic His and the penultimate residue also play roles in promoting side-chain cyclization.
[Mh] Termos MeSH primário: Inteínas/genética
Processamento de Proteína
Synechococcus/genética
Trichodesmium/genética
[Mh] Termos MeSH secundário: Mutação
[Pt] Tipo de publicação:LETTER
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12730


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[PMID]:28191958
[Au] Autor:Du K; Zhao J; Sun J; Feng W
[Ad] Endereço:Department of Biochemical Engineering, Beijing University of Chemical Technology , Beijing, 100029, China.
[Ti] Título:Specific Ligation of Two Multimeric Enzymes with Native Peptides and Immobilization with Controlled Molar Ratio.
[So] Source:Bioconjug Chem;28(4):1166-1175, 2017 Apr 19.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:d-Amino acid oxidases (DAAOs) are flavor enzymes and have been used in resolution of racemic amino acids and manufacturing of pharmaceuticals. However, the evolved H O during the catalysis has deleterious and inhibitory effects. Decomposition of the hydrogen peroxide by catalase (CAT) can eliminate the negative effects. DAAO and CAT are dimeric and tetrameric proteins, respectively. Here, the N-terminus of the DAAO subunits has been specifically ligated to the C-terminus of the CAT subunits with native peptides through intein-mediated in vivo protein splicing. The in vivo splicing has little effect on the secondary structures of the enzymes as confirmed by circular dichroism (CD) spectra, and fluorescence spectra showed that the spliced product DAAO&CAT has a higher stability than DAAO. In the spliced product DAAO&CAT, the DAAO subunits are in close proximity to the CAT subunits, facilitating immediate transfer of H O from one catalytic site to the other, enabling efficient decomposition of the generated H O . The reduced cofactors of the DAAO subunits were reoxidized by the evolved molecular oxygen around. Kinetics analysis showed that the d-alanine substrate follows Michaelis-Menten kinetics. The catalytic efficiency of DAAO&CAT is 22.4-fold that of DAAO. Furthermore, the spliced product DAAO&CAT has been encapsulated within a coordination polymer with an encapsulation efficiency of 91.3 ± 2.7%. The encapsulated DAAO&CAT has retained 98.1 ± 3.1% and 94.9 ± 2.9% of the activity of free DAAO&CAT at 30 and 40 °C, respectively.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/química
Catalase/química
Peptídeos/química
[Mh] Termos MeSH secundário: Aminoácido Oxirredutases/metabolismo
Catalase/metabolismo
Peróxido de Hidrogênio/síntese química
Peróxido de Hidrogênio/metabolismo
Cinética
Processamento de Proteína
Subunidades Proteicas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Protein Subunits); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.6 (Catalase); EC 1.4.- (Amino Acid Oxidoreductases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170214
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00043


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[PMID]:28152480
[Au] Autor:Chen YC; Chang JG; Liu TY; Jong YJ; Cheng WL; Yuo CY
[Ad] Endereço:Graduate Institute of Medicine, College of medicine, Kaohsiung Medical University, Kaohsiung 80708, Taiwan.
[Ti] Título:Securinine enhances SMN2 exon 7 inclusion in spinal muscular atrophy cells.
[So] Source:Biomed Pharmacother;88:708-714, 2017 Apr.
[Is] ISSN:1950-6007
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Spinal muscular atrophy (SMA) is an autosomal recessive disease characterized by the degeneration of motor neurons in the spinal cord, leading to muscular atrophy. SMA is caused by deletions or mutations in the survival motor neuron gene (SMN1) on chromosome 5q13. A second copy of the SMN gene (SMN2) also exists on chromosome 5, and both genes can produce functional protein. However, due to alternative splicing of the exon 7, the majority of SMN protein produced by SMN2 is truncated and unable to compensate for the loss of SMN1. Increasing full-length SMN protein production by promoting the exon 7 inclusion in SMN2 mRNA or increasing SMN2 gene transcription could be a therapeutic approach for SMA. In this study, we screened for the compounds that enhance SMN2 exon 7 inclusion by using SMN2 minigene-luciferase reporter system. We found that securinine can increase luciferase activity, indicating that securinine promoted SMN2 exon 7 inclusion. In addition, securinine increased full-length SMN2 mRNA and SMN protein expression in SMA patient-derived lymphoid cell lines. To investigate the mechanism of securinine effect on SMN2 splicing, we compared the protein levels of relevant splicing factors between securinine-treated and untreated cells. We found that securinine downregulated hnRNP A1 and Sam68 and upregulated Tra2-ß1 expression. However, securinine, unlike HDAC inhibitors, did not enhance tra2-ß1 gene transcription, indicating a post-transcriptional mechanism for Tra2-ß1 upregulation. Furthermore, we treated SMA-like mice with securinine by i.p. injection and found that securinine treatment increased SMN2 exon 7 inclusion and SMN protein expression in the brain and spinal cord. According to our results, securinine might have the potential to become a therapeutic drug for SMA disease.
[Mh] Termos MeSH primário: Azepinas/farmacologia
Estimulantes do Sistema Nervoso Central/farmacologia
Éxons/genética
Compostos Heterocíclicos de Anel em Ponte/farmacologia
Lactonas/farmacologia
Atrofia Muscular Espinal/genética
Piperidinas/farmacologia
Proteína 2 de Sobrevivência do Neurônio Motor/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Ribonucleoproteínas Nucleares Heterogêneas/biossíntese
Ribonucleoproteínas Nucleares Heterogêneas/genética
Tecido Linfoide/metabolismo
Camundongos
Atrofia Muscular Espinal/fisiopatologia
Processamento de Proteína
RNA Mensageiro/biossíntese
RNA Mensageiro/genética
Fatores de Processamento de Serina-Arginina/biossíntese
Fatores de Processamento de Serina-Arginina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azepines); 0 (Central Nervous System Stimulants); 0 (Heterocyclic Compounds, Bridged-Ring); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Lactones); 0 (Piperidines); 0 (RNA, Messenger); 0 (SMN2 protein, mouse); 0 (Survival of Motor Neuron 2 Protein); 0 (Tra2b protein, mouse); 170974-22-8 (Serine-Arginine Splicing Factors); G4VS580P5E (securinine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170313
[Lr] Data última revisão:
170313
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170203
[St] Status:MEDLINE


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[PMID]:28144031
[Au] Autor:Lewis CJ; Pan T; Kalsotra A
[Ad] Endereço:Department of Biochemistry, University of Illinois.
[Ti] Título:RNA modifications and structures cooperate to guide RNA-protein interactions.
[So] Source:Nat Rev Mol Cell Biol;18(3):202-210, 2017 Mar.
[Is] ISSN:1471-0080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An emerging body of evidence indicates that post-transcriptional gene regulation relies not only on the sequence of mRNAs but also on their folding into intricate secondary structures and on the chemical modifications of the RNA bases. These features, which are highly dynamic and interdependent, exert direct control over the transcriptome and thereby influence many aspects of cell function. Here, we consider how the coupling of RNA modifications and structures shapes RNA-protein interactions at different steps of the gene expression process.
[Mh] Termos MeSH primário: Proteínas/genética
RNA Guia/química
RNA Guia/metabolismo
[Mh] Termos MeSH secundário: Conformação de Ácido Nucleico
Biossíntese de Proteínas
Processamento de Proteína
Proteínas/metabolismo
Estabilidade de RNA
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Proteins); 0 (RNA, Guide); 0 (RNA, Messenger)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170805
[Lr] Data última revisão:
170805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170202
[St] Status:MEDLINE
[do] DOI:10.1038/nrm.2016.163


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[PMID]:27794069
[Au] Autor:Escudero-Hernández C; Martínez-Abad B; Ruipérez V; Garrote JA; Arranz E
[Ad] Endereço:1 Mucosal Immunology Laboratory, Instituto de Biología y Genética Molecular (IBGM), University of Valladolid-CSIC, Valladolid, Spain.
[Ti] Título:New IL-15 receptor-α splicing variants identified in intestinal epithelial Caco-2 cells.
[So] Source:Innate Immun;23(1):44-53, 2017 Jan.
[Is] ISSN:1753-4267
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:IL-15 is a pleiotropic cytokine related to IL-2 which acts at a broader level than its counterpart. It is presented through its specific high-affinity receptor, IL-15Rα. Both cytokine and receptor are tightly regulated at multiple levels and are widely distributed. Thus, deregulation of their expression leads to an inflammatory immune response. Variants of splicing of IL-15Rα have been described in immune and barrier cells; however, their presence has not been focused on intestinal epithelial cells. In this study, we describe five new alternative variants of splicing of IL-15Rα in Caco-2 cells. Four of them were expressed into proteins inside Caco-2 cells, but these were unable to bind IL-15 or to follow the secretory pathway. However, the expression of mRNA itself might be relevant to diseases such as celiac disease, inflammatory bowel disease or colorectal cancer.
[Mh] Termos MeSH primário: Doença Celíaca/imunologia
Neoplasias Colorretais/imunologia
Doenças Inflamatórias Intestinais/imunologia
Subunidade alfa de Receptor de Interleucina-15/metabolismo
Mucosa Intestinal/imunologia
Isoformas de Proteínas/metabolismo
[Mh] Termos MeSH secundário: Células CACO-2
Metilação de DNA
Epigênese Genética
Exocitose/genética
Seres Humanos
Interleucina-15/metabolismo
Subunidade alfa de Receptor de Interleucina-15/genética
Ligação Proteica/genética
Isoformas de Proteínas/genética
Processamento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-15); 0 (Interleukin-15 Receptor alpha Subunit); 0 (Protein Isoforms)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161030
[St] Status:MEDLINE
[do] DOI:10.1177/1753425916674263


  7 / 557 MEDLINE  
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[PMID]:27725266
[Au] Autor:Hanashima A; Hashimoto K; Ujihara Y; Honda T; Yobimoto T; Kodama A; Mohri S
[Ad] Endereço:First Department of Physiology, Kawasaki Medical School, Kurashiki 701-0192, Japan. Electronic address: hanashima@med.kawasaki-m.ac.jp.
[Ti] Título:Complete primary structure of the I-band region of connectin at which mechanical property is modulated in zebrafish heart and skeletal muscle.
[So] Source:Gene;596:19-26, 2017 Jan 05.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Connectin, also called titin, is the largest protein with a critical function as a molecular spring during contraction and relaxation of striated muscle; its mutation leads to severe myopathy and cardiomyopathy. To uncover the cause of this pathogenesis, zebrafish have recently been used as disease models because they are easier to genetically modify than mice. Although the gene structures and putative primary structures of zebrafish connectin have been determined, the actual primary structures of zebrafish connectin in heart and skeletal muscles remain unclear because of its large size and the PCR amplification-associated difficulties. In this research, using RT-PCR amplification from zebrafish heart and skeletal muscles, we determined the complete primary structures of zebrafish connectin in the I-band region at which mechanical property is modulated by alternative splicing. Our results showed that the domain structures of zebrafish connectins were largely similar to those of human connectins; however, the splicing pathways in the middle-Ig segment and the PEVK segment were highly diverse in every isoform. We also found that a set of 10 Ig domains in the middle-Ig segment of zebrafish connectin had been triplicated in human connectin. Because these triplicate regions are expressed in human leg and diaphragm, our findings may provide insight into the establishment of walking with limbs and lung respiration during tetrapod evolution.
[Mh] Termos MeSH primário: Conectina/química
Músculo Esquelético/metabolismo
Miocárdio/metabolismo
Proteínas de Peixe-Zebra/química
[Mh] Termos MeSH secundário: Processamento Alternativo
Sequência de Aminoácidos
Animais
Conectina/genética
Conectina/metabolismo
Evolução Molecular
Seres Humanos
Camundongos
Filogenia
Domínios Proteicos
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Processamento de Proteína
Sarcômeros/metabolismo
Peixe-Zebra
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connectin); 0 (Protein Isoforms); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170127
[Lr] Data última revisão:
170127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161012
[St] Status:MEDLINE


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[PMID]:27632429
[Au] Autor:Neugebauer M; Böcker JK; Matern JC; Pietrokovski S; Mootz HD
[Ti] Título:Development of a screening system for inteins active in protein splicing based on intein insertion into the LacZα-peptide.
[So] Source:Biol Chem;398(1):57-67, 2017 Jan 01.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Protein splicing by inteins has found diverse applications in biotechnology, protein chemistry and chemical biology. Inteins display a wide range of efficiencies and rates unpredictable from their amino acid sequences. Here, we identified positions T22S and S35 in the LacZα peptide as intein insertion sites that strictly require protein splicing, in contrast to cleavage side-reactions, to allow for complementation of ß-galactosidase activity. Both the cis-variant of the M86 mutant of the Ssp DnaB intein and a split form undergoing protein trans-splicing gave rise to formation of blue colonies in the ß-galactosidase read-out. Furthermore, we report the two novel, naturally split VidaL T4Lh-1 and VidaL UvsX-2 inteins whose N-terminal fragments consist of only 15 and 16 amino acids, respectively. Initial biochemical characterization with the LacZα host system of these inteins further underlines its utility. Finally, we used the LacZα host system to rapidly identify amino acid substitutions from a small randomized library at the structurally conserved intein position 2 next to the catalytic center, that are tolerated for protein splicing activity of the M86 intein. These findings demonstrate the potential of the system for initial testing and directed evolution of inteins.
[Mh] Termos MeSH primário: Biblioteca Gênica
Inteínas/genética
Óperon Lac
Peptídeos/química
Peptídeos/metabolismo
Processamento de Proteína
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Modelos Moleculares
Mutação
Peptídeos/genética
Conformação Proteica
beta-Galactosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE


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[PMID]:28031248
[Au] Autor:Lennon CW; Stanger M; Belfort M
[Ad] Endereço:Department of Biological Sciences, RNA Institute, University at Albany, Albany, New York 12222, USA.
[Ti] Título:Protein splicing of a recombinase intein induced by ssDNA and DNA damage.
[So] Source:Genes Dev;30(24):2663-2668, 2016 Dec 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inteins (or protein introns) autocatalytically excise themselves through protein splicing. We challenge the long-considered notion that inteins are merely molecular parasites and posit that some inteins evolved to regulate host protein function. Here we show substrate-induced and DNA damage-induced splicing, in which an archaeal recombinase RadA intein splices dramatically faster and more accurately when provided with ssDNA. This unprecedented example of intein splicing stimulation by the substrate of the invaded host protein provides compelling support in favor of inteins acting as pause buttons to arrest protein function until needed; then, an immediate activity switch is triggered, representing a new form of post-translational control.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Dano ao DNA/genética
DNA de Cadeia Simples/metabolismo
Proteínas de Ligação a DNA/genética
Inteínas/genética
Processamento de Proteína/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/metabolismo
Proteínas de Ligação a DNA/metabolismo
Escherichia coli/genética
Regulação da Expressão Gênica/genética
Modelos Biológicos
Mutação
Ligação Proteica
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (DNA, Single-Stranded); 0 (DNA-Binding Proteins); 0 (RadA protein, archaeal)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161230
[St] Status:MEDLINE
[do] DOI:10.1101/gad.289280.116


  10 / 557 MEDLINE  
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[PMID]:27846572
[Au] Autor:Liepe J; Marino F; Sidney J; Jeko A; Bunting DE; Sette A; Kloetzel PM; Stumpf MP; Heck AJ; Mishto M
[Ad] Endereço:Centre for Integrative Systems Biology and Bioinformatics, Department of Life Sciences, Imperial College London, London SW7 2AZ, UK. michele.mishto@charite.de j.liepe@imperial.ac.uk.
[Ti] Título:A large fraction of HLA class I ligands are proteasome-generated spliced peptides.
[So] Source:Science;354(6310):354-358, 2016 10 21.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The proteasome generates the epitopes presented on human leukocyte antigen (HLA) class I molecules that elicit CD8 T cell responses. Reports of proteasome-generated spliced epitopes exist, but they have been regarded as rare events. Here, however, we show that the proteasome-generated spliced peptide pool accounts for one-third of the entire HLA class I immunopeptidome in terms of diversity and one-fourth in terms of abundance. This pool also represents a unique set of antigens, possessing particular and distinguishing features. We validated this observation using a range of complementary experimental and bioinformatics approaches, as well as multiple cell types. The widespread appearance and abundance of proteasome-catalyzed peptide splicing events has implications for immunobiology and autoimmunity theories and may provide a previously untapped source of epitopes for use in vaccines and cancer immunotherapy.
[Mh] Termos MeSH primário: Apresentação do Antígeno
Linfócitos T CD8-Positivos/imunologia
Epitopos de Linfócito T/metabolismo
Antígenos de Histocompatibilidade Classe I/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Biologia Computacional
Seres Humanos
Ligantes
Peptídeos/imunologia
Peptídeos/metabolismo
Processamento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Epitopes, T-Lymphocyte); 0 (Histocompatibility Antigens Class I); 0 (Ligands); 0 (Peptides); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161116
[St] Status:MEDLINE



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde