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Pesquisa : G02.111.570.820.709.275.500.440 [Categoria DeCS]
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[PMID]:28465343
[Au] Autor:Coxon CH; Geer MJ; Senis YA
[Ad] Endereço:Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Headington, United Kingdom; and.
[Ti] Título:ITIM receptors: more than just inhibitors of platelet activation.
[So] Source:Blood;129(26):3407-3418, 2017 06 29.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Since their discovery, immunoreceptor tyrosine-based inhibition motif (ITIM)-containing receptors have been shown to inhibit signaling from immunoreceptor tyrosine-based activation motif (ITAM)-containing receptors in almost all hematopoietic cells, including platelets. However, a growing body of evidence has emerged demonstrating that this is an oversimplification, and that ITIM-containing receptors are versatile regulators of platelet signal transduction, with functions beyond inhibiting ITAM-mediated platelet activation. PECAM-1 was the first ITIM-containing receptor identified in platelets and appeared to conform to the established model of ITIM-mediated attenuation of ITAM-driven activation. PECAM-1 was therefore widely accepted as a major negative regulator of platelet activation and thrombosis for many years, but more recent findings suggest a more complex role for this receptor, including the facilitation of α ß -mediated platelet functions. Since the identification of PECAM-1, several other ITIM-containing platelet receptors have been discovered. These include G6b-B, a critical regulator of platelet reactivity and production, and the noncanonical ITIM-containing receptor TREM-like transcript-1, which is localized to α-granules in resting platelets, binds fibrinogen, and acts as a positive regulator of platelet activation. Despite structural similarities and shared binding partners, including the Src homology 2 domain-containing protein-tyrosine phosphatases Shp1 and Shp2, knockout and transgenic mouse models have revealed distinct phenotypes and nonredundant functions for each ITIM-containing receptor in the context of platelet homeostasis. These roles are likely influenced by receptor density, compartmentalization, and as-yet unknown binding partners. In this review, we discuss the diverse repertoire of ITIM-containing receptors in platelets, highlighting intriguing new functions, controversies, and future areas of investigation.
[Mh] Termos MeSH primário: Motivo de Inibição do Imunorreceptor Baseado em Tirosina/fisiologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Motivo de Ativação do Imunorreceptor Baseado em Tirosina
Ativação Plaquetária
Inibidores da Agregação de Plaquetas
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Platelet Aggregation Inhibitors)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180113
[Lr] Data última revisão:
180113
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-12-720185


  2 / 32 MEDLINE  
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[PMID]:28082678
[Au] Autor:Bauer B; Wotapek T; Zöller T; Rutkowski E; Steinle A
[Ad] Endereço:From the Institute for Molecular Medicine, Goethe University, 60590 Frankfurt am Main, Germany.
[Ti] Título:The Activating C-type Lectin-like Receptor NKp65 Signals through a Hemi-immunoreceptor Tyrosine-based Activation Motif (hemITAM) and Spleen Tyrosine Kinase (Syk).
[So] Source:J Biol Chem;292(8):3213-3223, 2017 Feb 24.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NKp65 is an activating human C-type lectin-like receptor (CTLR) triggering cellular cytotoxicity and cytokine secretion upon high-affinity interaction with the cognate CTLR keratinocyte-associated C-type lectin (KACL) selectively expressed by human keratinocytes. Previously, we demonstrated that NKp65-mediated cellular cytotoxicity depends on tyrosine 7, located in a cytoplasmic sequence motif of NKp65 resembling a hemi-immunoreceptor tyrosine-based activation motif (hemITAM). HemITAMs have been reported for a few activating myeloid-specific CTLRs, including Dectin-1 and CLEC-2, and consist of a single tyrosine signaling unit preceded by a triacidic motif. Upon receptor engagement, the hemITAM undergoes phosphotyrosinylation and specifically recruits spleen tyrosine kinase (Syk), initiating cellular activation. In this study, we addressed the functionality of the putative hemITAM of NKp65. We show that NKp65 forms homodimers and is phosphorylated at the hemITAM-embedded tyrosine 7 upon engagement by antibodies or KACL homodimers. HemITAM phosphotyrosinylation initiates a signaling pathway involving and depending on Syk, leading to cellular activation and natural killer (NK) cell degranulation. However, although NKp65 utilizes Syk for NK cell activation, a physical association of Syk with the NKp65 hemITAM could not be detected, unlike shown previously for the hemITAM of myeloid CTLR. Failure of NKp65 to recruit Syk is not due to an alteration of the triacidic motif, which rather affects the efficiency of hemITAM phosphotyrosinylation. In summary, NKp65 utilizes a hemITAM-like motif for cellular activation that requires Syk, although Syk appears not to be recruited to NKp65.
[Mh] Termos MeSH primário: Motivo de Ativação do Imunorreceptor Baseado em Tirosina
Células Matadoras Naturais/imunologia
Receptores Semelhantes a Lectina de Células NK/imunologia
Quinase Syk/imunologia
[Mh] Termos MeSH secundário: Degranulação Celular
Linhagem Celular
Seres Humanos
Imunidade Inata
Células Matadoras Naturais/citologia
Multimerização Proteica
Receptores Semelhantes a Lectina de Células NK/análise
Quinase Syk/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NKp65 protein, human); 0 (Receptors, NK Cell Lectin-Like); EC 2.7.10.2 (Syk Kinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.759977


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[PMID]:27742545
[Au] Autor:Iborra S; Martínez-López M; Cueto FJ; Conde-Garrosa R; Del Fresno C; Izquierdo HM; Abram CL; Mori D; Campos-Martín Y; Reguera RM; Kemp B; Yamasaki S; Robinson MJ; Soto M; Lowell CA; Sancho D
[Ad] Endereço:Immunobiology Laboratory, Fundación Centro Nacional de Investigaciones Cardiovasculares "Carlos III" (CNIC), Melchor Fernández Almagro 3, Madrid 28029, Spain; Departamento de Biología Molecular Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Nicolás Cabrera 1, Universidad Autónoma de Madrid, M
[Ti] Título:Leishmania Uses Mincle to Target an Inhibitory ITAM Signaling Pathway in Dendritic Cells that Dampens Adaptive Immunity to Infection.
[So] Source:Immunity;45(4):788-801, 2016 Oct 18.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:C-type lectin receptors sense a diversity of endogenous and exogenous ligands that may trigger differential responses. Here, we have found that human and mouse Mincle bind to a ligand released by Leishmania, a eukaryote parasite that evades an effective immune response. Mincle-deficient mice had milder dermal pathology and a tenth of the parasite burden compared to wild-type mice after Leishmania major intradermal ear infection. Mincle deficiency enhanced adaptive immunity against the parasite, correlating with increased activation, migration, and priming by Mincle-deficient dendritic cells (DCs). Leishmania triggered a Mincle-dependent inhibitory axis characterized by SHP1 coupling to the FcRγ chain. Selective loss of SHP1 in CD11c cells phenocopies enhanced adaptive immunity to Leishmania. In conclusion, Leishmania shifts Mincle to an inhibitory ITAM (ITAMi) configuration that impairs DC activation. Thus, ITAMi can be exploited for immune evasion by a pathogen and may represent a paradigm for ITAM-coupled receptors sensing self and non-self.
[Mh] Termos MeSH primário: Imunidade Adaptativa/imunologia
Células Dendríticas/imunologia
Motivo de Ativação do Imunorreceptor Baseado em Tirosina/imunologia
Lectinas Tipo C/imunologia
Leishmania major/imunologia
Proteínas de Membrana/imunologia
Transdução de Sinais/imunologia
[Mh] Termos MeSH secundário: Animais
Antígeno CD11c/imunologia
Diferenciação Celular/imunologia
Linhagem Celular Tumoral
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Proteína Tirosina Fosfatase não Receptora Tipo 6/imunologia
Receptores Fc/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD11c Antigen); 0 (Clecsf8 protein, mouse); 0 (Lectins, C-Type); 0 (Membrane Proteins); 0 (Receptors, Fc); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161016
[St] Status:MEDLINE


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[PMID]:26806373
[Au] Autor:Baker-Groberg SM; Lattimore S; Recht M; McCarty OJ; Haley KM
[Ad] Endereço:Department of Biomedical Engineering, Portland, OR, USA.
[Ti] Título:Assessment of neonatal platelet adhesion, activation, and aggregation.
[So] Source:J Thromb Haemost;14(4):815-27, 2016 Apr.
[Is] ISSN:1538-7836
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Acquired and inherited bleeding disorders may present in the neonatal period with devastating lifelong effects. Diagnosing bleeding disorders in the neonatal population could aid in preventing and treating the associated complications. However, currently available platelet function testing is limited in neonates, owing to difficulties in obtaining an adequate blood volume, a lack of normal reference ranges, and an incomplete understanding of the neonatal platelet functional phenotype. OBJECTIVE: To develop small-volume, whole blood platelet function assays in order to quantify and compare neonatal and adult platelet function. METHODS AND RESULTS: Peripheral blood was obtained from healthy, full-term neonates at 24 h of life. Platelet activation, secretion and aggregation were measured via flow cytometry. Platelet adhesion and aggregation were assessed under static and flow conditions. As compared with adult platelets, peripheral neonatal platelet P-selectin expression and integrin glycoprotein IIbIIIa activation were significantly reduced in response to the G-protein-coupled receptor (GPCR) agonists thrombin receptor activator peptide-6 (TRAP-6), ADP, and U46619, and the immunoreceptor tyrosine-based activation motif (ITAM) signaling pathway agonists collagen-related peptide (CRP) and rhodocytin. Neonatal platelet aggregation was markedly reduced in response to TRAP-6, ADP, U46619, CRP and rhodocytin as compared with adult platelets. The extents of neonatal and adult platelet adhesion and aggregate formation under static and shear conditions on collagen and von Willebrand factor were similar. CONCLUSIONS: As compared with adult platelets, we found that neonatal platelet activation and secretion were blunted in response to GPCR or ITAM agonists, whereas the extent of neonatal platelet adhesion and aggregate formation was similar to that of adult platelets.
[Mh] Termos MeSH primário: Plaquetas/citologia
Ativação Plaquetária
Adesividade Plaquetária
Agregação Plaquetária
[Mh] Termos MeSH secundário: Ácido 15-Hidroxi-11 alfa,9 alfa-(epoximetano)prosta-5,13-dienoico/química
Difosfato de Adenosina/química
Adulto
Proteína C-Reativa/química
Separação Celular
Citometria de Fluxo
Glicoproteínas/química
Hemorragia/sangue
Seres Humanos
Motivo de Ativação do Imunorreceptor Baseado em Tirosina
Recém-Nascido
Lectinas Tipo C/química
Oligopeptídeos/química
Testes de Função Plaquetária
Complexo Glicoproteico GPIIb-IIIa de Plaquetas/química
Complexo Glicoproteico GPIb-IX de Plaquetas/química
Receptores Acoplados a Proteínas-G/agonistas
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Lectins, C-Type); 0 (Oligopeptides); 0 (Platelet Glycoprotein GPIIb-IIIa Complex); 0 (Platelet Glycoprotein GPIb-IX Complex); 0 (Receptors, G-Protein-Coupled); 0 (Ser-Phe-Phe-Leu-Arg-Asn); 0 (adhesion receptor); 61D2G4IYVH (Adenosine Diphosphate); 76898-47-0 (15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid); 9007-41-4 (C-Reactive Protein)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160126
[St] Status:MEDLINE
[do] DOI:10.1111/jth.13270


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[PMID]:26749528
[Au] Autor:Lee RH; Bergmeier W
[Ad] Endereço:McAllister Heart Institute, University of North Carolina, Chapel Hill, NC, USA.
[Ti] Título:Platelet immunoreceptor tyrosine-based activation motif (ITAM) and hemITAM signaling and vascular integrity in inflammation and development.
[So] Source:J Thromb Haemost;14(4):645-54, 2016 Apr.
[Is] ISSN:1538-7836
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Platelets are essential for maintaining hemostasis following mechanical injury to the vasculature. Besides this established function, novel roles of platelets are becoming increasingly recognized, which are critical in non-injury settings to maintain vascular barrier integrity. For example, during embryogenesis platelets act to support the proper separation of blood and lymphatic vessels. This role continues beyond birth, where platelets prevent leakage of blood into the lymphatic vessel network. During the course of inflammation, platelets are necessary to prevent local hemorrhage due to neutrophil diapedesis and disruption of endothelial cell-cell junctions. Surprisingly, platelets also work to secure tumor-associated blood vessels, inhibiting excessive vessel permeability and intra-tumor hemorrhaging. Interestingly, many of these novel platelet functions depend on immunoreceptor tyrosine-based activation motif (ITAM) signaling but not on signaling via G protein-coupled receptors, which plays a crucial role in platelet plug formation at sites of mechanical injury. Murine platelets express two ITAM-containing receptors: the Fc receptor γ-chain (FcRγ), which functionally associates with the collagen receptor GPVI, and the C-type lectin-like 2 (CLEC-2) receptor, a hemITAM receptor for the mucin-type glycoprotein podoplanin. Human platelets express an additional ITAM receptor, FcγRIIA. These receptors share common downstream effectors, including Syk, SLP-76 and PLCγ2. Here we will review the recent literature that highlights a critical role for platelet GPVI/FcRγ and CLEC-2 in vascular integrity during development and inflammation in mice and discuss the relevance to human disease.
[Mh] Termos MeSH primário: Plaquetas/citologia
Motivo de Ativação do Imunorreceptor Baseado em Tirosina
Inflamação
Transdução de Sinais
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Plaquetas/metabolismo
Desenvolvimento Embrionário
Glicoproteínas/metabolismo
Hemorragia/metabolismo
Hemorragia/fisiopatologia
Hemostasia
Seres Humanos
Lectinas Tipo C/metabolismo
Vasos Linfáticos/fisiologia
Glicoproteínas de Membrana/metabolismo
Camundongos
Mucinas/metabolismo
Neoplasias/irrigação sanguínea
Permeabilidade
Ativação Plaquetária
Glicoproteínas da Membrana de Plaquetas/metabolismo
Domínios Proteicos
Tirosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (CLEC-2 protein, mouse); 0 (CLEC2B protein, human); 0 (Glycoproteins); 0 (Lectins, C-Type); 0 (Membrane Glycoproteins); 0 (Mucins); 0 (Platelet Membrane Glycoproteins); 0 (platelet membrane glycoprotein VI); 42HK56048U (Tyrosine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170330
[Lr] Data última revisão:
170330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160111
[St] Status:MEDLINE
[do] DOI:10.1111/jth.13250


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[PMID]:26468009
[Au] Autor:Feng C; Post CB
[Ad] Endereço:Department of Medicinal Chemistry and Molecular Pharmacology, Markey Center for Structural Biology, Purdue Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, USA. cbp@purdue.edu.
[Ti] Título:Insights into the allosteric regulation of Syk association with receptor ITAM, a multi-state equilibrium.
[So] Source:Phys Chem Chem Phys;18(8):5807-18, 2016 Feb 17.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The phosphorylation of interdomain A (IA), a linker region between tandem SH2 domains of Syk tyrosine kinase, regulates the binding affinity for association of Syk with doubly-phosphorylated ITAM regions of the B cell receptor. The mechanism of this allosteric regulation has been suggested to be a switch from the high-affinity bifunctional binding, mediated through both SH2 domains binding two phosphotyrosine residues of ITAM, to a substantially lower-affinity binding of only one SH2 domain. IA phosphorylation triggers the switch by inducing disorder in IA and weakening the SH2-SH2 interaction. The postulated switch to a single-SH2-domain binding mode is examined using NMR to monitor site-specific binding to each SH2 domain of Syk variants engineered to have IA regions that differ in conformational flexibility. The combined analysis of titration curves and NMR line-shapes provides sufficient information to determine the energetics of inter-molecular binding at each SH2 site along with an intra-molecular binding or isomerization step. A less favorable isomerization equilibrium associated with the changes in the SH2-SH2 conformational ensemble and IA flexibility accounts for the inhibition of Syk association with membrane ITAM regions when IA is phosphorylated, and refutes the proposed switch to single-SH2-domain binding. Syk localizes in the cell through its SH2 interactions, and this basis for allosteric regulation of ITAM association proposes for the first time a phosphorylation-dependent model to regulate Syk binding to alternate receptors and other signaling proteins that differ either in the number of residues separating ITAM phosphotyrosines or by having only one phosphotyrosine, a half ITAM.
[Mh] Termos MeSH primário: Motivo de Ativação do Imunorreceptor Baseado em Tirosina
Modelos Moleculares
Quinase Syk/química
Quinase Syk/metabolismo
[Mh] Termos MeSH secundário: Regulação Alostérica
Sequência de Aminoácidos
Domínio Catalítico
Espectroscopia de Ressonância Magnética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.10.2 (SYK protein, human); EC 2.7.10.2 (Syk Kinase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170217
[Lr] Data última revisão:
170217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151016
[St] Status:MEDLINE
[do] DOI:10.1039/c5cp05417f


  7 / 32 MEDLINE  
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[PMID]:26459387
[Au] Autor:Zhao B
[Ad] Endereço:Arthritis and Tissue Degeneration Program and David Z. Rosensweig Genomics Research Center, Hospital for Special Surgery and Department of Medicine, Weill Cornell Medical College, New York, NY, USA.
[Ti] Título:RBP-J and ITAM crosstalk.
[So] Source:Oncotarget;6(34):35135-6, 2015 Nov 03.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Proteína de Ligação a Sequências Sinal de Recombinação J de Imunoglobina/metabolismo
Motivo de Ativação do Imunorreceptor Baseado em Tirosina/fisiologia
[Mh] Termos MeSH secundário: Animais
Sinalização do Cálcio
Seres Humanos
Camundongos
Osteoclastos/metabolismo
Fosfolipase C gama/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (Immunoglobulin J Recombination Signal Sequence-Binding Protein); 0 (RBPJ protein, human); 0 (Rbpj protein, mouse); EC 3.1.4.3 (Phospholipase C gamma)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151014
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.6034


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[PMID]:26170006
[Au] Autor:Guselnikov SV; Grayfer L; De Jesús Andino F; Rogozin IB; Robert J; Taranin AV
[Ad] Endereço:Institute of Molecular and Cellular Biology, Siberian Branch of the Russian Academy of Sciences, Lavrentiev Avenue 8/2, Novosibirsk 630090, Russia; Novosibirsk State University, Pirogov Street 2, Novosibirsk 630090, Russia. Electronic address: sguselnikov@mcb.nsc.ru.
[Ti] Título:Retention of duplicated ITAM-containing transmembrane signaling subunits in the tetraploid amphibian species Xenopus laevis.
[So] Source:Dev Comp Immunol;53(1):158-68, 2015 Nov.
[Is] ISSN:1879-0089
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ITAM-bearing transmembrane signaling subunits (TSS) are indispensable components of activating leukocyte receptor complexes. The TSS-encoding genes map to paralogous chromosomal regions, which are thought to arise from ancient genome tetraploidization(s). To assess a possible role of tetraploidization in the TSS evolution, we studied TSS and other functionally linked genes in the amphibian species Xenopus laevis whose genome was duplicated about 40 MYR ago. We found that X. laevis has retained a duplicated set of sixteen TSS genes, all except one being transcribed. Furthermore, duplicated TCRα loci and genes encoding TSS-coupling protein kinases have also been retained. No clear evidence for functional divergence of the TSS paralogs was obtained from gene expression and sequence analyses. We suggest that the main factor of maintenance of duplicated TSS genes in X. laevis was a protein dosage effect and that this effect might have facilitated the TSS set expansion in early vertebrates.
[Mh] Termos MeSH primário: Motivo de Ativação do Imunorreceptor Baseado em Tirosina/genética
Receptores de Antígenos de Linfócitos T alfa-beta/genética
Receptores de IgG/genética
Transdução de Sinais/imunologia
Tetraploidia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Linhagem Celular
Evolução Molecular
Células HEK293
Seres Humanos
Dados de Sequência Molecular
Receptores de Antígenos de Linfócitos T alfa-beta/imunologia
Receptores de IgG/imunologia
Alinhamento de Sequência
Transdução de Sinais/genética
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Receptors, Antigen, T-Cell, alpha-beta); 0 (Receptors, IgG)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150715
[St] Status:MEDLINE


  9 / 32 MEDLINE  
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[PMID]:25959494
[Au] Autor:Hwang S; Palin AC; Li L; Song KD; Lee J; Herz J; Tubo N; Chu H; Pepper M; Lesourne R; Zvezdova E; Pinkhasov J; Jenkins MK; McGavern D; Love PE
[Ad] Endereço:Program in Genomics of Differentiation, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Room 2B-210, Building 6B, Bethesda, Maryland 20892, USA.
[Ti] Título:TCR ITAM multiplicity is required for the generation of follicular helper T-cells.
[So] Source:Nat Commun;6:6982, 2015 May 11.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The T-cell antigen receptor (TCR) complex contains 10 copies of a di-tyrosine Immunoreceptor-Tyrosine-based-Activation-Motif (ITAM) that initiates TCR signalling by recruiting protein tyrosine kinases. ITAM multiplicity amplifies TCR signals, but the importance of this capability for T-cell responses remains undefined. Most TCR ITAMs (6 of 10) are contributed by the CD3ζ subunits. We generated 'knock-in' mice that express non-signalling CD3ζ chains in lieu of wild-type CD3ζ. Here we demonstrate that ITAM multiplicity is important for the development of innate-like T-cells and follicular helper T-cells, events that are known to require strong/sustained TCR-ligand interactions, but is not essential for 'general' T-cell responses including proliferation and cytokine production or for the generation of a diverse antigen-reactive TCR repertoire.
[Mh] Termos MeSH primário: Motivo de Ativação do Imunorreceptor Baseado em Tirosina
Receptores de Antígenos de Linfócitos T/química
Receptores de Antígenos de Linfócitos T/metabolismo
Linfócitos T Auxiliares-Indutores/citologia
[Mh] Termos MeSH secundário: Animais
Antígenos/imunologia
Proliferação Celular
Células Clonais
Feminino
Memória Imunológica
Masculino
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Células T Matadoras Naturais/citologia
Células T Matadoras Naturais/imunologia
Receptores de Antígenos de Linfócitos T alfa-beta/química
Receptores de Antígenos de Linfócitos T alfa-beta/metabolismo
Receptores de Antígenos de Linfócitos T gama-delta/química
Receptores de Antígenos de Linfócitos T gama-delta/metabolismo
Transdução de Sinais
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Antigens); 0 (Receptors, Antigen, T-Cell); 0 (Receptors, Antigen, T-Cell, alpha-beta); 0 (Receptors, Antigen, T-Cell, gamma-delta)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161203
[Lr] Data última revisão:
161203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150512
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms7982


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[PMID]:25527332
[Au] Autor:Loren CP; Aslan JE; Rigg RA; Nowak MS; Healy LD; Gruber A; Druker BJ; McCarty OJ
[Ad] Endereço:Department of Biomedical Engineering; Department of Cell & Developmental Biology. Electronic address: cassandraloren@gmail.com.
[Ti] Título:The BCR-ABL inhibitor ponatinib inhibits platelet immunoreceptor tyrosine-based activation motif (ITAM) signaling, platelet activation and aggregate formation under shear.
[So] Source:Thromb Res;135(1):155-60, 2015 Jan.
[Is] ISSN:1879-2472
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Treatment of chronic myelogenous leukemia (CML) with the BCR-ABL tyrosine kinase inhibitor (TKI) imatinib significantly improves patient outcomes. As some patients are unresponsive to imatinib, next generation BCR-ABL inhibitors such as nilotinib have been developed to treat patients with imatinib-resistant CML. The use of some BCR-ABL inhibitors has been associated with bleeding diathesis, and these inhibitors have been shown to inhibit platelet functions, which may explain the hemostasis impairment. Surprisingly, a new TKI, ponatinib, has been associated with a high incidence of severe acute ischemic cardiovascular events. The mechanism of this unexpected adverse effect remains undefined. OBJECTIVE AND METHODS: This study used biochemical and functional assays to evaluate whether ponatinib was different from the other BCR-ABL inhibitors with respect to platelet activation, spreading, and aggregation. RESULTS AND CONCLUSIONS: Our results show that ponatinib, similar to other TKIs, acts as a platelet antagonist. Ponatinib inhibited platelet activation, spreading, granule secretion, and aggregation, likely through broad spectrum inhibition of platelet tyrosine kinase signaling, and also inhibited platelet aggregate formation in whole blood under shear. As our results indicate that pobatinib inhibits platelet function, the adverse cardiovascular events observed in patients taking ponatinib may be the result of the effect of ponatinib on other organs or cell types, or disease-specific processes, such as BCR-ABL+cells undergoing apoptosis in response to chemotherapy, or drug-induced adverse effects on the integrity of the vascular endothelium in ponatinib-treated patients.
[Mh] Termos MeSH primário: Plaquetas/efeitos dos fármacos
Proteínas de Fusão bcr-abl/antagonistas & inibidores
Imidazóis/antagonistas & inibidores
Motivo de Ativação do Imunorreceptor Baseado em Tirosina
Piridazinas/antagonistas & inibidores
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Apoptose
Plaquetas/citologia
Colágeno/química
Células Endoteliais/citologia
Fibrinogênio/química
Seres Humanos
Leucemia Mielogênica Crônica BCR-ABL Positiva/tratamento farmacológico
Leucemia Mielogênica Crônica BCR-ABL Positiva/metabolismo
Selectina-P/química
Fosfatidilserinas/química
Fosforilação
Ativação Plaquetária
Agregação Plaquetária
Resistência ao Cisalhamento
Transdução de Sinais
Tirosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Imidazoles); 0 (P-Selectin); 0 (Phosphatidylserines); 0 (Pyridazines); 42HK56048U (Tyrosine); 4340891KFS (ponatinib); 9001-32-5 (Fibrinogen); 9007-34-5 (Collagen); EC 2.7.10.2 (Fusion Proteins, bcr-abl)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:170729
[Lr] Data última revisão:
170729
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141221
[St] Status:MEDLINE



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