Base de dados : MEDLINE
Pesquisa : E05.481.500.311 [Categoria DeCS]
Referências encontradas : 570 [refinar]
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[PMID]:28456379
[Au] Autor:Rivière I; Sadelain M
[Ad] Endereço:Center for Cell Engineering, Molecular Pharmacology and Immunology Programs, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
[Ti] Título:Chimeric Antigen Receptors: A Cell and Gene Therapy Perspective.
[So] Source:Mol Ther;25(5):1117-1124, 2017 May 03.
[Is] ISSN:1525-0024
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chimeric antigen receptors (CARs) are synthetic receptors that reprogram T lymphocytes to target chosen antigens. The targeting of CD19, a cell surface molecule expressed in the vast majority of leukemias and lymphomas, has been successfully translated in the clinic, earning CAR therapy a special distinction in the selection of "cancer immunotherapy" by Science as the breakthrough of the year in 2013. CD19 CAR therapy is predicated on advances in genetic engineering, T cell biology, tumor immunology, synthetic biology, target identification, cell manufacturing sciences, and regulatory compliance-the central tenets of CAR therapy. Here, we review two of these foundations: the genetic engineering approaches and cell types to engineer.
[Mh] Termos MeSH primário: Antígenos CD19/genética
Terapia Baseada em Transplante de Células e Tecidos/métodos
Leucemia/terapia
Linfoma/terapia
Proteínas Mutantes Quiméricas/genética
Receptores de Antígenos de Linfócitos T/genética
Linfócitos T/imunologia
[Mh] Termos MeSH secundário: Antígenos CD19/imunologia
Engenharia Celular/métodos
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/imunologia
Seres Humanos
Imunoterapia/métodos
Lentivirus/genética
Lentivirus/imunologia
Leucemia/genética
Leucemia/imunologia
Leucemia/patologia
Linfoma/genética
Linfoma/imunologia
Linfoma/patologia
Proteínas Mutantes Quiméricas/imunologia
Engenharia de Proteínas/métodos
Receptores de Antígenos de Linfócitos T/imunologia
Retroviridae/genética
Retroviridae/imunologia
Linfócitos T/classificação
Linfócitos T/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antigens, CD19); 0 (CD19 molecule, human); 0 (Mutant Chimeric Proteins); 0 (Receptors, Antigen, T-Cell)
[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:170501
[St] Status:MEDLINE


  2 / 570 MEDLINE  
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[PMID]:28465209
[Au] Autor:Lalonde ME; Durocher Y
[Ad] Endereço:Département de biochimie et médecine moléculaire, Faculté de médecine, Université de Montréal, Qc, H3C 3J7, Canada.
[Ti] Título:Therapeutic glycoprotein production in mammalian cells.
[So] Source:J Biotechnol;251:128-140, 2017 Jun 10.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Over the last years, the biopharmaceutical industry has significantly turned its biologics production towards mammalian cell expression systems. The presence of glycosylation machineries within these systems, and the fact that monoclonal antibodies represent today the vast majority of new therapeutic candidates, has largely influenced this new direction. Recombinant glycoproteins, including monoclonal antibodies, have shown different biological properties based on their glycan profiles. Thus, the industry has developed cell engineering strategies not only to improve cell's specific productivity, but also to adapt their glycosylation profiles for increased therapeutic activity. Additionally, the advance of "omics" technologies has recently given rise to new possibilities in improving these expression platforms and will significantly help developing new strategies, in particular for CHO (Chinese Hamster Ovary) cells.
[Mh] Termos MeSH primário: Glicoproteínas/biossíntese
[Mh] Termos MeSH secundário: Animais
Engenharia Celular
Linhagem Celular
Genômica
Seres Humanos
Proteínas Recombinantes/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  3 / 570 MEDLINE  
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[PMID]:28452462
[Au] Autor:Yang Q; An Y; Zhu S; Zhang R; Loke CM; Cipollo JF; Wang LX
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Maryland , College Park, Maryland 20742, United States.
[Ti] Título:Glycan Remodeling of Human Erythropoietin (EPO) Through Combined Mammalian Cell Engineering and Chemoenzymatic Transglycosylation.
[So] Source:ACS Chem Biol;12(6):1665-1673, 2017 06 16.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The tremendous structural heterogeneity of N-glycosylation of glycoproteins poses a great challenge for deciphering the biological functions of specific glycoforms and for developing protein-based therapeutics. We have previously reported a chemoenzymatic glycan remodeling method for producing homogeneous glycoforms of N-glycoproteins including intact antibodies, which consist of endoglycosidase-catalyzed deglycosylation and novel glycosynthase-catalyzed transglycosylation, but its application to complex glycoproteins carrying multiple N-glycans remains to be examined. We report here site-selective chemoenzymatic glycosylation remodeling of recombinant human erythropoietin (EPO) that contains three N-glycans. We found that the generation of a HEK293S GnT I knockout FUT8 overexpressing cell line enabled the production of an unusual Man GlcNAc Fuc glycoform, which could be converted to the core-fucosylated GlcNAc-EPO intermediate acceptor for enzymatic transglycosylation. With this acceptor, homogeneous sialylated glycoform or azide-tagged glycoform were produced using the glycosynthase (EndoF3-D165A) catalyzed transglycosylation. Interestingly, a remarkable site-selectivity was observed in the transglycosylation reactions, leading to the introduction of two N-glycans selectively at the Asn-38 and Asn-83 sites, which was confirmed by a detailed MS/MS analysis of the transglycosylation product. Finally, a different N-glycan was attached at the third (Asn-24) site by pushing the enzymatic transglycosylation with a distinct glycan oxazoline, achieving the site-selective glycosylation modification of the protein. This study represents the first example of site-selective chemoenzymatic glycan engineering of complex glycoproteins carrying multiple N-glycans.
[Mh] Termos MeSH primário: Engenharia Celular/métodos
Eritropoetina/metabolismo
Polissacarídeos/metabolismo
Engenharia de Proteínas/métodos
[Mh] Termos MeSH secundário: Asparagina/metabolismo
Glicosilação
Células HEK293
Seres Humanos
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Polysaccharides); 11096-26-7 (Erythropoietin); 7006-34-0 (Asparagine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00282


  4 / 570 MEDLINE  
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[PMID]:28748939
[Au] Autor:Perkel JM
[Ad] Endereço:Nature.
[Ti] Título:Cell engineering: How to hack the genome.
[So] Source:Nature;547(7664):477-479, 2017 07 26.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Engenharia Celular
Engenharia Genética
Genoma/genética
Biologia Sintética/tendências
[Mh] Termos MeSH secundário: Animais
Cromatina/genética
Cromatina/metabolismo
Cromossomos Artificiais de Levedura/genética
DNA/biossíntese
DNA/genética
DNA/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Redes Reguladoras de Genes/genética
Seres Humanos
Mycoplasma mycoides/genética
Saccharomyces cerevisiae/genética
Salmonella typhimurium/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 9007-49-2 (DNA)
[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:170728
[St] Status:MEDLINE
[do] DOI:10.1038/547477a


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[PMID]:28858290
[Au] Autor:Nolbrant S; Heuer A; Parmar M; Kirkeby A
[Ad] Endereço:Wallenberg Neuroscience Center, Department of Experimental Medical Sciences, Lund University, Lund, Sweden.
[Ti] Título:Generation of high-purity human ventral midbrain dopaminergic progenitors for in vitro maturation and intracerebral transplantation.
[So] Source:Nat Protoc;12(9):1962-1979, 2017 Sep.
[Is] ISSN:1750-2799
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Generation of precisely patterned neural cells from human pluripotent stem cells (hPSCs) is instrumental in developing disease models and stem cell therapies. Here, we provide a detailed 16-d protocol for obtaining high-purity ventral midbrain (VM) dopamine (DA) progenitors for intracerebral transplantation into animal models and for in vitro maturation into neurons. We have successfully transplanted such cells into the rat; however, in principle, the cells can be used for transplantation into any animal model, and the protocol is designed to also be compatible with clinical transplantation into humans. We show how to precisely set the balance of patterning factors to obtain specifically the caudal VM progenitors that give rise to DA-rich grafts. By specifying how to perform quality control (QC), troubleshooting and adaptation of the procedure, this protocol will facilitate implementation in different laboratories and with a variety of hPSC lines. To facilitate reproducibility of experiments and enable shipping of cells between centers, we present a method for cryopreservation of the progenitors for subsequent direct transplantation or terminal differentiation into DA neurons. This protocol is free of xeno-derived products and can be performed under good manufacturing practice (GMP) conditions.
[Mh] Termos MeSH primário: Neurônios Dopaminérgicos
Células-Tronco Embrionárias/citologia
Mesencéfalo/cirurgia
Transplante de Células-Tronco
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Engenharia Celular
Linhagem Celular
Neurônios Dopaminérgicos/química
Neurônios Dopaminérgicos/citologia
Neurônios Dopaminérgicos/transplante
Perfilação da Expressão Gênica
Seres Humanos
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1038/nprot.2017.078


  6 / 570 MEDLINE  
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[PMID]:28845660
[Au] Autor:Ehrenworth AM; Claiborne T; Peralta-Yahya P
[Ad] Endereço:School of Chemistry and Biochemistry, Georgia Institute of Technology , Atlanta, Georgia 30332, United States.
[Ti] Título:Medium-Throughput Screen of Microbially Produced Serotonin via a G-Protein-Coupled Receptor-Based Sensor.
[So] Source:Biochemistry;56(41):5471-5475, 2017 Oct 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chemical biosensors, for which chemical detection triggers a fluorescent signal, have the potential to accelerate the screening of noncolorimetric chemicals produced by microbes, enabling the high-throughput engineering of enzymes and metabolic pathways. Here, we engineer a G-protein-coupled receptor (GPCR)-based sensor to detect serotonin produced by a producer microbe in the producer microbe's supernatant. Detecting a chemical in the producer microbe's supernatant is nontrivial because of the number of other metabolites and proteins present that could interfere with sensor performance. We validate the two-cell screening system for medium-throughput applications, opening the door to the rapid engineering of microbes for the increased production of serotonin. We focus on serotonin detection as serotonin levels limit the microbial production of hydroxystrictosidine, a modified alkaloid that could accelerate the semisynthesis of camptothecin-derived anticancer pharmaceuticals. This work shows the ease of generating GPCR-based chemical sensors and their ability to detect specific chemicals in complex aqueous solutions, such as microbial spent medium. In addition, this work sets the stage for the rapid engineering of serotonin-producing microbes.
[Mh] Termos MeSH primário: Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/metabolismo
Receptores 5-HT4 de Serotonina/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Serotonina/análise
[Mh] Termos MeSH secundário: Engenharia Celular
Meios de Cultivo Condicionados/química
Proteínas Inibidoras de Quinase Dependente de Ciclina/genética
Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/genética
Proteínas Ativadoras de GTPase/genética
Galactose/metabolismo
Deleção de Genes
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Seres Humanos
Cinética
Isoformas de Proteínas/agonistas
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Receptores de Fator de Acasalamento/genética
Receptores 5-HT4 de Serotonina/química
Receptores 5-HT4 de Serotonina/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Reprodutibilidade dos Testes
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/agonistas
Proteínas de Saccharomyces cerevisiae/genética
Serotonina/metabolismo
Serotonina/secreção
Espectrometria de Fluorescência
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Culture Media, Conditioned); 0 (Cyclin-Dependent Kinase Inhibitor Proteins); 0 (FAR1 protein, S cerevisiae); 0 (GTPase-Activating Proteins); 0 (Protein Isoforms); 0 (Receptors, Mating Factor); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (SST2 protein, S cerevisiae); 0 (STE2 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 147336-22-9 (Green Fluorescent Proteins); 158165-40-3 (Receptors, Serotonin, 5-HT4); 333DO1RDJY (Serotonin); EC 3.6.5.1 (GPA1 protein, S cerevisiae); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gq-G11); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00605


  7 / 570 MEDLINE  
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[PMID]:28817124
[Au] Autor:Bao X; Lian X; Qian T; Bhute VJ; Han T; Palecek SP
[Ad] Endereço:Department of Chemical &Biological Engineering, University of Wisconsin-Madison, Madison, Wisconsin, USA.
[Ti] Título:Directed differentiation and long-term maintenance of epicardial cells derived from human pluripotent stem cells under fully defined conditions.
[So] Source:Nat Protoc;12(9):1890-1900, 2017 Sep.
[Is] ISSN:1750-2799
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Here, we describe how to efficiently direct human pluripotent stem cells (hPSCs) differentiation into self-renewing epicardial cells in a completely defined, xeno-free system by temporal modulation of regulators of canonical Wnt signaling. Appropriate differentiation-stage-specific application of Gsk3 inhibitor, Wnt inhibitor, and Gsk3 inhibitor (GiWiGi) is sufficient to produce cells expressing epicardial markers and exhibiting epicardial phenotypes with a high yield and purity from multiple hPSC lines in 16 d. Characterization of differentiated cells is performed via flow cytometry and immunostaining to assess quantitative expression and localization of epicardial cell-specific proteins. In vitro differentiation into fibroblasts and smooth muscle cells (SMCs) is also described. In addition, culture in the presence of transforming growth factor (TGF)-ß inhibitors allows long-term expansion of hPSC-derived epicardial cells (for at least 25 population doublings). Functional human epicardial cells differentiated via this protocol may constitute a potential cell source for heart disease modeling, drug screening, and cell-based therapeutic applications.
[Mh] Termos MeSH primário: Diferenciação Celular/fisiologia
Engenharia Celular/métodos
Pericárdio/citologia
Células-Tronco Pluripotentes/citologia
[Mh] Termos MeSH secundário: Técnicas de Cultura de Células
Seres Humanos
Via de Sinalização Wnt/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE
[do] DOI:10.1038/nprot.2017.080


  8 / 570 MEDLINE  
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[PMID]:28704435
[Au] Autor:Klose D; Woitok M; Niesen J; Beerli RR; Grawunder U; Fischer R; Barth S; Fendel R; Nachreiner T
[Ad] Endereço:Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Aachen, Germany.
[Ti] Título:Generation of an artificial human B cell line test system using Transpo-mAbTM technology to evaluate the therapeutic efficacy of novel antigen-specific fusion proteins.
[So] Source:PLoS One;12(7):e0180305, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The antigen-specific targeting of autoreactive B cells via their unique B cell receptors (BCRs) is a novel and promising alternative to the systemic suppression of humoral immunity. We generated and characterized cytolytic fusion proteins based on an existing immunotoxin comprising tetanus toxoid fragment C (TTC) as the targeting component and the modified Pseudomonas aeruginosa exotoxin A (ETA') as the cytotoxic component. The immunotoxin was reconfigured to replace ETA' with either the granzyme B mutant R201K or MAPTau as human effector domains. The novel cytolytic fusion proteins were characterized with a recombinant human lymphocytic cell line developed using Transpo-mAb™ technology. Genes encoding a chimeric TTC-reactive immunoglobulin G were successfully integrated into the genome of the precursor B cell line REH so that the cells could present TTC-reactive BCRs on their surface. These cells were used to investigate the specific cytotoxicity of GrB(R201K)-TTC and TTC-MAPTau, revealing that the serpin proteinase inhibitor 9-resistant granzyme B R201K mutant induced apoptosis specifically in the lymphocytic cell line. Our data confirm that antigen-based fusion proteins containing granzyme B (R201K) are suitable candidates for the depletion of autoreactive B cells.
[Mh] Termos MeSH primário: Linfócitos B/citologia
Engenharia Celular/métodos
Granzimas/genética
Toxoide Tetânico/imunologia
[Mh] Termos MeSH secundário: Linfócitos B/metabolismo
Linhagem Celular Tumoral
Granzimas/metabolismo
Seres Humanos
Imunotoxinas/metabolismo
Receptores de Antígenos de Linfócitos B/imunologia
Proteínas Recombinantes de Fusão/imunologia
Proteínas Recombinantes de Fusão/metabolismo
Anticorpos de Cadeia Única/metabolismo
Toxoide Tetânico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunotoxins); 0 (Receptors, Antigen, B-Cell); 0 (Recombinant Fusion Proteins); 0 (Single-Chain Antibodies); 0 (Tetanus Toxoid); EC 3.4.21.- (GZMB protein, human); EC 3.4.21.- (Granzymes)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180305


  9 / 570 MEDLINE  
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[PMID]:28651073
[Au] Autor:Parvathaneni K; Abdeladhim M; Pratt KP; Scott DW
[Ad] Endereço:Department of Medicine, Uniformed Services University of Health Sciences, Bethesda, Md.
[Ti] Título:Hemophilia A inhibitor treatment: the promise of engineered T-cell therapy.
[So] Source:Transl Res;187:44-52, 2017 Sep.
[Is] ISSN:1878-1810
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hemophilia A is a bleeding disorder caused by mutations in the gene encoding factor VIII (FVIII), a cofactor protein that is essential for normal blood clotting. Approximately, 1 in 3 patients with severe hemophilia A produce neutralizing antibodies (inhibitors) that block its biologic function in the clotting cascade. Current efforts to eliminate inhibitors consist of repeated FVIII injections under what is termed an "ITI" protocol (Immune Tolerance Induction). However, this method is extremely costly and approximately 30% of patients undergoing ITI do not achieve peripheral tolerance. Human T regulatory cells (Tregs) have been proposed as a new strategy to treat this antidrug antibody response, as well as other diseases. Polyclonal Tregs are nonspecific and could potentially cause general immunosuppression. Novel approaches to induce tolerance to FVIII include the use of engineered human and mouse antigen-specific Tregs, or alternatively antigen-specific cytotoxic cells, to delete, anergize, or kill FVIII-specific lymphocytes. In this review, we discuss the current state of engineered T-cell therapies, and we describe the recent progress in applying these therapies to induce FVIII-specific tolerance.
[Mh] Termos MeSH primário: Engenharia Celular/métodos
Fator VIII/uso terapêutico
Hemofilia A/terapia
Imunoterapia Adotiva/métodos
Linfócitos T/fisiologia
[Mh] Termos MeSH secundário: Fator VIII/genética
Fator VIII/metabolismo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
9001-27-8 (Factor VIII)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE


  10 / 570 MEDLINE  
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[PMID]:28541315
[Au] Autor:Sadelain M; Rivière I; Riddell S
[Ad] Endereço:Memorial Sloan Kettering Cancer Center, New York, New York 10065, USA.
[Ti] Título:Therapeutic T cell engineering.
[So] Source:Nature;545(7655):423-431, 2017 05 24.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Genetically engineered T cells are powerful new medicines, offering hope for curative responses in patients with cancer. Chimaeric antigen receptors (CARs) are a class of synthetic receptors that reprogram lymphocyte specificity and function. CARs targeting CD19 have demonstrated remarkable potency in B cell malignancies. Engineered T cells are applicable in principle to many cancers, pending further progress to identify suitable target antigens, overcome immunosuppressive tumour microenvironments, reduce toxicities, and prevent antigen escape. Advances in the selection of optimal T cells, genetic engineering, and cell manufacturing are poised to broaden T-cell-based therapies and foster new applications in infectious diseases and autoimmunity.
[Mh] Termos MeSH primário: Engenharia Celular/métodos
Neoplasias/imunologia
Neoplasias/terapia
Linfócitos T/metabolismo
Linfócitos T/transplante
[Mh] Termos MeSH secundário: Animais
Antígenos CD19/imunologia
Antígenos CD19/metabolismo
Doenças Autoimunes/imunologia
Doenças Autoimunes/patologia
Doenças Autoimunes/terapia
Seres Humanos
Infecção/imunologia
Infecção/patologia
Infecção/terapia
Neoplasias/patologia
Receptores de Antígenos de Linfócitos T/imunologia
Receptores de Antígenos de Linfócitos T/metabolismo
Proteínas Recombinantes de Fusão/imunologia
Proteínas Recombinantes de Fusão/metabolismo
Linfócitos T/imunologia
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Antigens, CD19); 0 (Receptors, Antigen, T-Cell); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1038/nature22395



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