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  1 / 1013 MEDLINE  
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[PMID]:28453927
[Au] Autor:Gentle IE; McHenry KT; Weber A; Metz A; Kretz O; Porter D; Häcker G
[Ad] Endereço:Faculty of Medicine, Institute for Medical Microbiology and Hygiene, Medical Center - University of Freiburg, University of Freiburg, Germany.
[Ti] Título:TIR-domain-containing adapter-inducing interferon-ß (TRIF) forms filamentous structures, whose pro-apoptotic signalling is terminated by autophagy.
[So] Source:FEBS J;284(13):1987-2003, 2017 07.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The formation of amyloid-like protein structures has recently emerged as a feature in signal transduction, particularly in innate immunity. These structures appear to depend on defined domains for their formation but likely also require dedicated ways to terminate signalling. We, here, define the innate immunity protein/Toll-like receptor adaptor TIR-domain-containing adapter-inducing interferon-ß (TRIF) as a novel platform of fibril formation and probe signal initiation through TRIF as well as its termination in Toll-like receptor 3 (TLR3)-stimulated melanoma cells. A main signalling pathway triggered by TLR3 caused apoptosis, which was controlled by inhibitor of apoptosis proteins and was dependent on RIPK1 and independent of TNF. Using correlative electron/fluorescence microscopy, we visualised fibrillar structures formed through both Toll/interleukin-1 receptor and RIP homotypic interacting motif regions of TRIF. We provide evidence that these fibrillary structures are active signalling platforms whose activity is terminated by autophagy. TRIF-signalling enhanced autophagy, and fibrillary structures were partly contained within autophagosomes. Inhibition of autophagy increased levels of pro-apoptotic TRIF complexes, leading to the accumulation of active caspase-8 and enhanced apoptosis while stimulation of autophagy reduced TRIF-dependent death. We conclude that pro-death signals through TRIF are regulated by autophagy and propose that pro-apoptotic signalling through TRIF/RIPK1/caspase-8 occurs in fibrillary platforms.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Apoptose/fisiologia
Autofagia/fisiologia
Transdução de Sinais
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Adaptadoras de Transporte Vesicular/genética
Animais
Apoptose/efeitos dos fármacos
Autofagia/efeitos dos fármacos
Western Blotting
Caspase 8/genética
Caspase 8/metabolismo
Linhagem Celular Tumoral
Células Cultivadas
Células HEK293
Células HeLa
Seres Humanos
Camundongos Knockout
Microscopia Eletrônica de Transmissão
Microscopia de Fluorescência
Oligopeptídeos/farmacologia
Poli I-C/farmacologia
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Receptor 3 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (LBW242); 0 (Oligopeptides); 0 (TICAM1 protein, human); 0 (Toll-Like Receptor 3); EC 2.7.11.1 (RIPK1 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 3.4.22.- (Caspase 8); O84C90HH2L (Poly I-C)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14091


  2 / 1013 MEDLINE  
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[PMID]:28462531
[Au] Autor:Kondylis V; Kumari S; Vlantis K; Pasparakis M
[Ad] Endereço:Institute for Genetics, University of Cologne, Cologne, Germany.
[Ti] Título:The interplay of IKK, NF-κB and RIPK1 signaling in the regulation of cell death, tissue homeostasis and inflammation.
[So] Source:Immunol Rev;277(1):113-127, 2017 05.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Regulated cell death pathways have important functions in host defense and tissue homeostasis. Studies in genetic mouse models provided evidence that cell death could cause inflammation in different tissues. Inhibition of RIPK3-MLKL-dependent necroptosis by FADD and caspase-8 was identified as a key mechanism preventing inflammation in epithelial barriers. Moreover, the interplay between IKK/NF-κB and RIPK1 signaling was recognized as a critical determinant of tissue homeostasis and inflammation. NEMO was shown to regulate RIPK1 kinase activity-mediated apoptosis by NF-κB-dependent and -independent functions, which are critical for averting chronic tissue injury and inflammation in the intestine and the liver. In addition, RIPK1 was shown to exhibit kinase activity-independent functions that are essential for preventing cell death, maintaining tissue architecture and inhibiting inflammation. In the intestine, RIPK1 acts as a scaffold to prevent epithelial cell apoptosis and preserve tissue integrity. In the skin, RIPK1 functions via its RHIM to counteract ZBP1/DAI-dependent activation of RIPK3-MLKL-dependent necroptosis and inflammation. Collectively, these studies provided evidence that the regulation of cell death signaling plays an important role in the maintenance of tissue homeostasis, and suggested that cell death could be causally involved in the pathogenesis of inflammatory diseases.
[Mh] Termos MeSH primário: Quinase I-kappa B/metabolismo
NF-kappa B/metabolismo
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
[Mh] Termos MeSH secundário: Animais
Morte Celular
Homeostase
Seres Humanos
Inflamação
Transdução de Sinais
Cicatrização
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NF-kappa B); EC 2.7.11.1 (RIPK1 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 2.7.11.10 (I-kappa B Kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12550


  3 / 1013 MEDLINE  
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[PMID]:28462528
[Au] Autor:Tonnus W; Linkermann A
[Ad] Endereço:Division of Nephrology, Department of Internal Medicine III, University Hospital Carl Gustav Carus at the Technische Universität Dresden, Dresden, Germany.
[Ti] Título:The in vivo evidence for regulated necrosis.
[So] Source:Immunol Rev;277(1):128-149, 2017 05.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Necrosis is a hallmark of several widespread diseases or their direct complications. In the past decade, we learned that necrosis can be a regulated process that is potentially druggable. RIPK3- and MLKL-mediated necroptosis represents by far the best studied pathway of regulated necrosis. During necroptosis, the release of damage-associated molecular patterns (DAMPs) drives a phenomenon referred to as necroinflammation, a common consequence of necrosis. However, most studies of regulated necrosis investigated cell lines in vitro in a cell autonomous manner, which represents a non-physiological situation. Conclusions based on such work might not necessarily be transferrable to disease states in which synchronized, non-cell autonomous effects occur. Here, we summarize the current knowledge of the pathophysiological relevance of necroptosis in vivo, and in light of this understanding, we reassess the morphological classification of necrosis that is generally used by pathologists. Along these lines, we discuss the paucity of data implicating necroptosis in human disease. Finally, the in vivo relevance of non-necroptotic forms of necrosis, such as ferroptosis, is addressed.
[Mh] Termos MeSH primário: Inflamação
Ferro/metabolismo
Necrose
[Mh] Termos MeSH secundário: Animais
Microambiente Celular
Colágeno
Seres Humanos
Proteínas Quinases/metabolismo
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Receptores de Reconhecimento de Padrão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Receptors, Pattern Recognition); 9007-34-5 (Collagen); E1UOL152H7 (Iron); EC 2.7.- (MLKL protein, human); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (RIPK3 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12551


  4 / 1013 MEDLINE  
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[PMID]:28462521
[Au] Autor:Orozco S; Oberst A
[Ad] Endereço:Department of Immunology, University of Washington, Seattle, WA, USA.
[Ti] Título:RIPK3 in cell death and inflammation: the good, the bad, and the ugly.
[So] Source:Immunol Rev;277(1):102-112, 2017 05.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Necroptosis is a form of cell death that can be observed downstream of death receptor or pattern recognition receptor signaling under certain cellular contexts, or in response to some viral and bacterial infections. The receptor interacting protein kinases-1 (RIPK1) and RIPK3 are at the core of necroptotic signaling, among other proteins. Because this pathway is normally halted by the pro-apoptotic protease caspase-8 and the IAP ubiquitin ligases, how and when necroptosis is triggered in physiological settings are ongoing questions. Interestingly, accumulating evidence suggests that RIPK3 has functions beyond the induction of necroptotic cell death, especially in the areas of tissue injury and sterile inflammation. Here, we will discuss the role of RIPK3 in a variety of physiological conditions, including necroptotic and non-necroptotic cell death, in the context of viral and bacterial infections, tissue damage, and inflammation.
[Mh] Termos MeSH primário: Infecções Bacterianas/imunologia
Inflamação/imunologia
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Viroses/imunologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Degradação Necrótica do DNA
Seres Humanos
Necrose
Receptores de Morte Celular/metabolismo
Receptores de Reconhecimento de Padrão/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Receptors, Death Domain); 0 (Receptors, Pattern Recognition); EC 2.7.11.1 (RIPK3 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12536


  5 / 1013 MEDLINE  
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[PMID]:28462524
[Au] Autor:Upton JW; Shubina M; Balachandran S
[Ad] Endereço:Department of Molecular Biosciences, LaMontagne Center for Infectious Disease, University of Texas, Austin, TX, USA.
[Ti] Título:RIPK3-driven cell death during virus infections.
[So] Source:Immunol Rev;277(1):90-101, 2017 05.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The programmed self-destruction of infected cells is a powerful antimicrobial strategy in metazoans. For decades, apoptosis represented the dominant mechanism by which the virus-infected cell was thought to undergo programmed cell death. More recently, however, new mechanisms of cell death have been described that are also key to host defense. One such mechanism in vertebrates is programmed necrosis, or "necroptosis", driven by receptor-interacting protein kinase 3 (RIPK3). Once activated by innate immune stimuli, including virus infections, RIPK3 phosphorylates the mixed lineage kinase domain-like protein (MLKL), which then disrupts cellular membranes to effect necroptosis. Emerging evidence demonstrates that RIPK3 can also mediate apoptosis and regulate inflammasomes. Here, we review studies on the mechanisms by which viruses activate RIPK3 and the pathways engaged by RIPK3 that drive cell death.
[Mh] Termos MeSH primário: Inflamassomos/metabolismo
Proteínas Quinases/metabolismo
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Viroses/imunologia
Vírus/imunologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Seres Humanos
Imunidade Inata
Necrose
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Inflammasomes); EC 2.7.- (MLKL protein, human); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (RIPK3 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12539


  6 / 1013 MEDLINE  
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[PMID]:29330116
[Au] Autor:Wen SH; Lin LN; Wu HJ; Yu L; Lin L; Zhu LL; Li HY; Zhang HL; Li CC
[Ad] Endereço:Department of Pediatric Pulmonology, The Second Affiliated Hospital & Yuying Children's Hospital, Wenzhou Medical University, Wenzhou 325027, PR China.
[Ti] Título:TNF-α increases Staphylococcus aureus-induced death of human alveolar epithelial cell line A549 associated with RIP3-mediated necroptosis.
[So] Source:Life Sci;195:81-86, 2018 Feb 15.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIM: To explore the role of tumor necrosis factor-alpha (TNF-α) on Staphylococcus aureus-induced necroptosis in alveolar epithelial cells. MAIN METHODS: The A549 alveolar epithelial cell line was pretreated with small interfering RNA (siRNA) against receptor interacting protein-3 (RIP3) and then stimulated by S. aureus, where some cells were pretreated with TNF-α or TNF-α with anti-TNF-α antibody simultaneously. A549 cell death was assessed using lactate dehydrogenase (LDH) leakage and flow cytometry analyses. The protein expressions of RIP1, RIP3, cleaved caspase-1, and cleaved caspase-8 were analyzed by western blot. KEY FINDINGS: S. aureus-induced LDH release was increased significantly by TNF-α. In addition, flow cytometry showed that TNF-α increased A549 cell apoptosis and necrosis in S. aureus-infected cell cultures. Levels of RIP3 and cleaved caspase-1 protein in A549 cells infected with S. aureus increased at 12 h post-infection, as shown by western blot. Significant additional increases in RIP3 expression were observed following the addition of TNF-α. Decreasing RIP3 levels by siRNA significantly suppressed the release of LDH induced by TNF-α and S. aureus. RIP3 siRNA also significantly suppressed A549 cell necrosis induced by S. aureus and TNF-α at 6 and 12 h post-infection as shown by flow cytometry analysis. SIGNIFICANCE: TNF-α enhances the damage of S. aureus on lung epithelial cells, and its mechanism is associated with RIP3 mediated necroptosis.
[Mh] Termos MeSH primário: Morte Celular/efeitos dos fármacos
Proteína Serina-Treonina Quinases de Interação com Receptores/fisiologia
Staphylococcus aureus/efeitos dos fármacos
Fator de Necrose Tumoral alfa/farmacologia
[Mh] Termos MeSH secundário: Células A549
Células Epiteliais Alveolares
Caspase 8/genética
Caspase 8/metabolismo
Seres Humanos
L-Lactato Desidrogenase/metabolismo
Necrose/induzido quimicamente
Necrose/patologia
Complexo de Proteínas Formadoras de Poros Nucleares/efeitos dos fármacos
Complexo de Proteínas Formadoras de Poros Nucleares/fisiologia
Proteínas de Ligação a RNA/efeitos dos fármacos
Proteínas de Ligação a RNA/fisiologia
Proteína Serina-Treonina Quinases de Interação com Receptores/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AGFG1 protein, human); 0 (Nuclear Pore Complex Proteins); 0 (RNA-Binding Proteins); 0 (Tumor Necrosis Factor-alpha); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.7.11.1 (RIPK3 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 3.4.22.- (CASP8 protein, human); EC 3.4.22.- (Caspase 8)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180114
[St] Status:MEDLINE


  7 / 1013 MEDLINE  
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[PMID]:28461567
[Au] Autor:Saleh D; Najjar M; Zelic M; Shah S; Nogusa S; Polykratis A; Paczosa MK; Gough PJ; Bertin J; Whalen M; Fitzgerald KA; Slavov N; Pasparakis M; Balachandran S; Kelliher M; Mecsas J; Degterev A
[Ad] Endereço:Medical Scientist Training Program, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, MA 02111.
[Ti] Título:Kinase Activities of RIPK1 and RIPK3 Can Direct IFN-ß Synthesis Induced by Lipopolysaccharide.
[So] Source:J Immunol;198(11):4435-4447, 2017 06 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The innate immune response is a central element of the initial defense against bacterial and viral pathogens. Macrophages are key innate immune cells that upon encountering pathogen-associated molecular patterns respond by producing cytokines, including IFN-ß. In this study, we identify a novel role for RIPK1 and RIPK3, a pair of homologous serine/threonine kinases previously implicated in the regulation of necroptosis and pathologic tissue injury, in directing IFN-ß production in macrophages. Using genetic and pharmacologic tools, we show that catalytic activity of RIPK1 directs IFN-ß synthesis induced by LPS in mice. Additionally, we report that RIPK1 kinase-dependent IFN-ß production may be elicited in an analogous fashion using LPS in bone marrow-derived macrophages upon inhibition of caspases. Notably, this regulation requires kinase activities of both RIPK1 and RIPK3, but not the necroptosis effector protein, MLKL. Mechanistically, we provide evidence that necrosome-like RIPK1 and RIPK3 aggregates facilitate canonical TRIF-dependent IFN-ß production downstream of the LPS receptor TLR4. Intriguingly, we also show that RIPK1 and RIPK3 kinase-dependent synthesis of IFN-ß is markedly induced by avirulent strains of Gram-negative bacteria, and , and less so by their wild-type counterparts. Overall, these observations identify unexpected roles for RIPK1 and RIPK3 kinases in the production of IFN-ß during the host inflammatory responses to bacterial infection and suggest that the axis in which these kinases operate may represent a target for bacterial virulence factors.
[Mh] Termos MeSH primário: Interferon beta/biossíntese
Lipopolissacarídeos/imunologia
Macrófagos/imunologia
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/imunologia
Bactérias Gram-Negativas/imunologia
Interferon beta/imunologia
Klebsiella/imunologia
Macrófagos/microbiologia
Camundongos
Necrose/imunologia
Fosforilação
Receptor 4 Toll-Like/imunologia
Yersinia/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Lipopolysaccharides); 0 (Tlr4 protein, mouse); 0 (Toll-Like Receptor 4); 77238-31-4 (Interferon-beta); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 2.7.11.1 (Ripk1 protein, mouse); EC 2.7.11.1 (Ripk3 protein, mouse)
[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.1601717


  8 / 1013 MEDLINE  
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[PMID]:29045898
[Au] Autor:Kleino A; Ramia NF; Bozkurt G; Shen Y; Nailwal H; Huang J; Napetschnig J; Gangloff M; Chan FK; Wu H; Li J; Silverman N
[Ad] Endereço:Division of Infectious Diseases and Immunology, Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
[Ti] Título:Peptidoglycan-Sensing Receptors Trigger the Formation of Functional Amyloids of the Adaptor Protein Imd to Initiate Drosophila NF-κB Signaling.
[So] Source:Immunity;47(4):635-647.e6, 2017 Oct 17.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the Drosophila immune response, bacterial derived diaminopimelic acid-type peptidoglycan binds the receptors PGRP-LC and PGRP-LE, which through interaction with the adaptor protein Imd leads to activation of the NF-κB homolog Relish and robust antimicrobial peptide gene expression. PGRP-LC, PGRP-LE, and Imd each contain a motif with some resemblance to the RIP Homotypic Interaction Motif (RHIM), a domain found in mammalian RIPK proteins forming functional amyloids during necroptosis. Here we found that despite sequence divergence, these Drosophila cryptic RHIMs formed amyloid fibrils in vitro and in cells. Amyloid formation was required for signaling downstream of Imd, and in contrast to the mammalian RHIMs, was not associated with cell death. Furthermore, amyloid formation constituted a regulatable step and could be inhibited by Pirk, an endogenous feedback regulator of this pathway. Thus, diverse sequence motifs are capable of forming amyloidal signaling platforms, and the formation of these platforms may present a regulatory point in multiple biological processes.
[Mh] Termos MeSH primário: Amiloide/imunologia
Proteínas de Transporte/imunologia
Proteínas de Drosophila/imunologia
NF-kappa B/imunologia
Receptores de Superfície Celular/imunologia
Transdução de Sinais/imunologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos/genética
Motivos de Aminoácidos/imunologia
Sequência de Aminoácidos
Amiloide/metabolismo
Animais
Sítios de Ligação/genética
Sítios de Ligação/imunologia
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Linhagem Celular
Proteínas de Drosophila/genética
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/genética
Drosophila melanogaster/imunologia
Feminino
Expressão Gênica/imunologia
Masculino
Microscopia Confocal
Modelos Imunológicos
Mutação
NF-kappa B/metabolismo
Proteína Serina-Treonina Quinases de Interação com Receptores/genética
Proteína Serina-Treonina Quinases de Interação com Receptores/imunologia
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Receptores de Superfície Celular/genética
Receptores de Superfície Celular/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid); 0 (Carrier Proteins); 0 (Drosophila Proteins); 0 (NF-kappa B); 0 (Receptors, Cell Surface); 0 (immune deficiency protein, Drosophila); 0 (peptidoglycan receptor); 0 (peptidoglycan recognition protein); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE


  9 / 1013 MEDLINE  
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[PMID]:28957350
[Au] Autor:Saeed WK; Jun DW; Jang K; Chae YJ; Lee JS; Kang HT
[Ad] Endereço:Department of Internal Medicine, Hanyang University School of Medicine, Seoul, South Korea.
[Ti] Título:Does necroptosis have a crucial role in hepatic ischemia-reperfusion injury?
[So] Source:PLoS One;12(9):e0184752, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Previous studies have demonstrated protective effects of anti-receptor interacting protein kinase 1 (RIP1), a key necroptosis molecule. However, it is uncertain whether necroptosis has a crucial role in hepatic IR injury. Therefore, we evaluated the role of necroptosis in hepatic IR injury. METHOD: The IR mice underwent 70% segmental IR injury induced by the clamping of the hepatic artery and portal vein for 1 hr followed by reperfusion for 4 hr. The key necroptosis molecules (RIP1, RIP3, and MLKL) and other key molecules of regulated necrosis (PGAM5 and caspase-1) were evaluated in the warm IR injury model. A RIP1 inhibitor (necrostain-1s) and/or an anti-mitochondrial permeability transition (MPT)-mediated necrosis mediator (cyclosporine A, CyA) were administered before clamping. Necrotic injury was quantified using Suzuki's scoring system. qRT-PCR and western blot were performed to evaluate RIP1, RIP3, MLKL and PGAM5 expressions. RESULTS: RIP1, RIP3, MLKL and PGAM5 expression did not change in the hepatic IR injury model. Moreover, Nec1s pretreatment did not improve histology or biochemical markers. The overall Suzuki score (cytoplasmic vacuolization, sinusoidal congestion and hepatocytes necrosis) was increased in the RIP3(-/-) mice compared to the IR group (3.5 vs. 5, p = 0.026). CyA pretreatment and/or RIP3(-/-) mice decreased Bax/Bcl2 expression; however, it did lead to an overall change in the levels of AST, ALT and LDH or necrotic injury. The Bax/Bcl2 ratio and the expression of caspase-1 and caspase-3 did not increase in our hepatic IR injury model. CONCLUSION: Key necroptosis molecules did not increase in the necrosis-dominant hepatic IR injury model. Anti-necroptosis and/or cyclosporine-A treatment did not have an overall protective effect on necrosis-dominant hepatic IR injury.
[Mh] Termos MeSH primário: Apoptose
Fígado/irrigação sanguínea
Fígado/patologia
Traumatismo por Reperfusão/patologia
[Mh] Termos MeSH secundário: Animais
Caspase 3/metabolismo
Ciclosporina/administração & dosagem
Ciclosporina/farmacologia
Modelos Animais de Doenças
Proteínas Ativadoras de GTPase/metabolismo
Fígado/metabolismo
Masculino
Camundongos Endogâmicos C57BL
Necrose
Proteína Serina-Treonina Quinases de Interação com Receptores/deficiência
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Traumatismo por Reperfusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTPase-Activating Proteins); 0 (Ralbp1 protein, mouse); 83HN0GTJ6D (Cyclosporine); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 2.7.11.1 (Ripk3 protein, mouse); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184752


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[PMID]:28920954
[Au] Autor:Menon MB; Gropengießer J; Fischer J; Novikova L; Deuretzbacher A; Lafera J; Schimmeck H; Czymmeck N; Ronkina N; Kotlyarov A; Aepfelbacher M; Gaestel M; Ruckdeschel K
[Ad] Endereço:Institute of Cell Biochemistry, Hannover Medical School, Hannover 30625, Germany.
[Ti] Título:p38 /MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection.
[So] Source:Nat Cell Biol;19(10):1248-1259, 2017 Oct.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Receptor-interacting protein kinase-1 (RIPK1), a master regulator of cell fate decisions, was identified as a direct substrate of MAPKAP kinase-2 (MK2) by phosphoproteomic screens using LPS-treated macrophages and stress-stimulated embryonic fibroblasts. p38 /MK2 interact with RIPK1 in a cytoplasmic complex and MK2 phosphorylates mouse RIPK1 at Ser321/336 in response to pro-inflammatory stimuli, such as TNF and LPS, and infection with the pathogen Yersinia enterocolitica. MK2 phosphorylation inhibits RIPK1 autophosphorylation, curtails RIPK1 integration into cytoplasmic cytotoxic complexes, and suppresses RIPK1-dependent apoptosis and necroptosis. In Yersinia-infected macrophages, RIPK1 phosphorylation by MK2 protects against infection-induced apoptosis, a process targeted by Yersinia outer protein P (YopP). YopP suppresses p38 /MK2 activation to increase Yersinia-driven apoptosis. Hence, MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.
[Mh] Termos MeSH primário: Apoptose
Inflamação/enzimologia
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Macrófagos/enzimologia
Proteínas Serina-Treonina Quinases/metabolismo
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Yersiniose/enzimologia
Yersinia enterocolitica/patogenicidade
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Proteínas de Bactérias/metabolismo
Citosol/enzimologia
Citosol/microbiologia
Feminino
Genótipo
Células HEK293
Interações Hospedeiro-Patógeno
Seres Humanos
Quinase I-kappa B/metabolismo
Inflamação/patologia
Peptídeos e Proteínas de Sinalização Intracelular/deficiência
Peptídeos e Proteínas de Sinalização Intracelular/genética
MAP Quinase Quinase Quinases/metabolismo
Macrófagos/efeitos dos fármacos
Macrófagos/microbiologia
Macrófagos/patologia
Masculino
Proteínas de Membrana/metabolismo
Camundongos Knockout
Necrose
Fenótipo
Fosforilação
Proteínas Serina-Treonina Quinases/deficiência
Proteínas Serina-Treonina Quinases/genética
Proteína Serina-Treonina Quinases de Interação com Receptores/genética
Receptores Tipo I de Fatores de Necrose Tumoral/genética
Receptores Tipo I de Fatores de Necrose Tumoral/metabolismo
Serina
Transdução de Sinais
Fatores de Tempo
Transfecção
Fator de Necrose Tumoral alfa/toxicidade
Yersiniose/microbiologia
Yersiniose/patologia
Yersinia enterocolitica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (Receptors, Tumor Necrosis Factor, Type I); 0 (Tnfrsf1a protein, mouse); 0 (Tumor Necrosis Factor-alpha); 0 (Yop proteins translocation protein P, Yersinia); 452VLY9402 (Serine); EC 2.7.1.- (MAP-kinase-activated kinase 2); EC 2.7.1.- (MAP-kinase-activated kinase 3); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 2.7.11.1 (Ripk1 protein, mouse); EC 2.7.11.10 (I-kappa B Kinase); EC 2.7.11.10 (Ikbkb protein, mouse); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 2.7.11.25 (MAP Kinase Kinase Kinases); EC 2.7.11.25 (MAP kinase kinase kinase 7)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3614



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