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[PMID]:28460454
[Au] Autor:Shan X; Zhang Y; Chen H; Dong L; Wu B; Xu T; Hu J; Liu Z; Wang W; Wu L; Feng Z; Liang G
[Ad] Endereço:Chemical Biology Research Center at School of Pharmaceutical Sciences, Wenzhou Medical University, Wenzhou, Zhejiang, China.
[Ti] Título:Inhibition of epidermal growth factor receptor attenuates LPS-induced inflammation and acute lung injury in rats.
[So] Source:Oncotarget;8(16):26648-26661, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acute lung injury (ALI) and its severe form acute respiratory distress syndrome remain the leading cause of morbidity and mortality in intensive care units. Inhibition of epidermal growth factor receptor (EGFR) has been found to be able to reduce inflammatory response. However, it is still unclear whether EGFR inhibition can prevent ALI. This study aimed to validate the EGFR's role in ALI and investigated the effects of EGFR inhibition on lipopolysaccharides (LPS)-induced ALI in rats. In vitro, both pharmacological inhibitors (AG1478 and 451) and si-RNA silencing of EGFR significantly inhibited LPS-induced EGFR signaling activation and inflammatory response in human lung epithelial cells or macrophages. Mechanistically, LPS induced EGFR activation via TLR4 and c-Src signaling. In vivo, rat model with ALI induced by intratracheal instillation of LPS was treated by oral administration of AG1478 and 451. It was observed that AG1478 and 451 blocked the activation of EGFR signaling in lung tissue and reduced the LPS-induced infiltration of inflammatory cells, inflammatory gene expression, and lung injuries. This study demonstrates that TLR4/c-Src-dependent EGFR signaling plays an important role in LPS-induced ALI, and that EGFR may be a potential target in treating ALI.
[Mh] Termos MeSH primário: Lesão Pulmonar Aguda/etiologia
Lesão Pulmonar Aguda/metabolismo
Lipopolissacarídeos/efeitos adversos
Receptor do Fator de Crescimento Epidérmico/metabolismo
[Mh] Termos MeSH secundário: Lesão Pulmonar Aguda/tratamento farmacológico
Lesão Pulmonar Aguda/patologia
Animais
Linhagem Celular
Citocinas/genética
Citocinas/metabolismo
Mediadores da Inflamação/metabolismo
Macrófagos/imunologia
Macrófagos/metabolismo
Inibidores de Proteínas Quinases/farmacologia
Quinazolinas/farmacologia
Ratos
Receptor do Fator de Crescimento Epidérmico/antagonistas & inibidores
Transdução de Sinais/efeitos dos fármacos
Receptor 4 Toll-Like/metabolismo
Tirfostinas/farmacologia
Quinases da Família src/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Inflammation Mediators); 0 (Lipopolysaccharides); 0 (Protein Kinase Inhibitors); 0 (Quinazolines); 0 (Toll-Like Receptor 4); 0 (Tyrphostins); 170449-18-0 (tyrphostin AG 1478); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 2.7.10.2 (CSK tyrosine-protein kinase); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15790


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[PMID]:29288363
[Au] Autor:Hamurcu Z; Delibasi N; Geçene S; Sener EF; Dönmez-Altuntas H; Özkul Y; Canatan H; Ozpolat B
[Ad] Endereço:Department of Medical Biology, Faculty of Medicine, Erciyes University, Kayseri, Turkey.
[Ti] Título:Targeting LC3 and Beclin-1 autophagy genes suppresses proliferation, survival, migration and invasion by inhibition of Cyclin-D1 and uPAR/Integrin ß1/ Src signaling in triple negative breast cancer cells.
[So] Source:J Cancer Res Clin Oncol;144(3):415-430, 2018 Mar.
[Is] ISSN:1432-1335
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Autophagy is a catabolic process for degrading dysfunctional proteins and organelles, and closely associated with cancer cell survival under therapeutic, metabolic stress, hypoxia, starvation and lack of growth factors, contributing to resistance to therapies. However, the role of autophagy in breast cancer cells is not well understood. In the present study, we investigated the role of autophagy in highly aggressive and metastatic triple negative breast cancer (TNBC) and non-metastatic breast cancer cells and demonstrated that the knockdown of autophagy-related genes (LC3 and Beclin-1) inhibited autophagy and significantly suppressed cell proliferation, colony formation, migration/invasion and induced apoptosis in MDA-MB-231 and BT-549 TNBC cells. Knockdown of LC3 and Beclin-1 led to inhibition of multiple proto-oncogenic signaling pathways, including cyclin D1, uPAR/integrin-ß1/Src, and PARP1. In conclusion, our study suggests that LC3 and Beclin-1 are required for cell proliferation, survival, migration and invasion, and may contribute to tumor growth and progression of highly aggressive and metastatic TNBC cells and therapeutic targeting of autophagy genes may be a potential therapeutic strategy for TNBC in breast cancer.
[Mh] Termos MeSH primário: Beclina-1/antagonistas & inibidores
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Proteínas Associadas aos Microtúbulos/antagonistas & inibidores
Terapia de Alvo Molecular/métodos
RNA Interferente Pequeno/farmacologia
Neoplasias de Mama Triplo Negativas/patologia
[Mh] Termos MeSH secundário: Autofagia/genética
Beclina-1/genética
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/genética
Ciclina D1/antagonistas & inibidores
Ciclina D1/metabolismo
Feminino
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Integrina beta1/metabolismo
Células MCF-7
Proteínas Associadas aos Microtúbulos/genética
Receptores de Ativador de Plasminogênio Tipo Uroquinase/antagonistas & inibidores
Receptores de Ativador de Plasminogênio Tipo Uroquinase/metabolismo
Transdução de Sinais/efeitos dos fármacos
Transdução de Sinais/genética
Neoplasias de Mama Triplo Negativas/genética
Quinases da Família src/antagonistas & inibidores
Quinases da Família src/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Beclin-1); 0 (CCND1 protein, human); 0 (Integrin beta1); 0 (Microtubule-Associated Proteins); 0 (RNA, Small Interfering); 0 (Receptors, Urokinase Plasminogen Activator); 0 (light chain 3, human); 136601-57-5 (Cyclin D1); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE
[do] DOI:10.1007/s00432-017-2557-5


  3 / 8777 MEDLINE  
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[PMID]:29175418
[Au] Autor:Mitchell J; Kim SJ; Seelmann A; Veit B; Shepard B; Im E; Rhee SH
[Ad] Endereço:Department of Biological Sciences, Oakland University, Rochester, MI 48309, USA.
[Ti] Título:Src family kinase tyrosine phosphorylates Toll-like receptor 4 to dissociate MyD88 and Mal/Tirap, suppressing LPS-induced inflammatory responses.
[So] Source:Biochem Pharmacol;147:119-127, 2018 01.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Src family kinases (SFKs) are a family of protein tyrosine kinases containing nine members: Src, Lyn, Fgr, Hck, Lck, Fyn, Blk, Yes, and Ylk. Although SFK activation is a major immediate signaling event in LPS/Toll-like receptor 4 (TLR4) signaling, its precise role has remained elusive due to various contradictory results obtained from a certain SFK member-deficient mice or cells. The observed inconsistencies may be due to the compensation or redundancy by other SFKs upon a SFK deficiency. The chemical rescuing approach was suggested to induce temporal and precise SFK activation in living cells, thereby limiting the chance of cellular adaption to a SFK-deficient condition. Using the rescuing approach, we demonstrate that restoring SFK activity not only induces tyrosine phosphorylation of TLR4, but also inhibits LPS-induced NFκB and JNK1/2 activation and consequently suppresses LPS-induced cytokine production. TLR4 normally recruits TIR domain-containing adaptors in response to LPS, however, temporally restored SFK activation disrupts the LPS-induced association of MyD88 and Mal/Tirap with TLR4. Additionally, using kinase-dead SFK-Lyn (Y397/508F) and constitutively active SFK-Lyn (Y508F), we found that the kinase-dead SFK inhibits TLR4 tyrosine phosphorylation with reduced binding affinity to TLR4, while the kinase-active SFK strongly binds to TLR4 and promotes TLR4 tyrosine phosphorylation, suggesting that SFK kinase activity is required for TLR4 tyrosine phosphorylation and TLR4-SFK interaction. Together, our results demonstrate that SFK activation induces TLR4 tyrosine phosphorylation, consequently dissociating MyD88 and Mal/Tirap from TLR4 and inhibiting LPS-induced inflammatory responses, suggesting a negative feedback loop regulated by SFK-induced tyrosine phosphorylation in TLR4.
[Mh] Termos MeSH primário: Mediadores da Inflamação/metabolismo
Glicoproteínas de Membrana/metabolismo
Fator 88 de Diferenciação Mieloide/metabolismo
Receptores de Interleucina-1/metabolismo
Receptor 4 Toll-Like/metabolismo
Quinases da Família src/metabolismo
[Mh] Termos MeSH secundário: Animais
Células HEK293
Seres Humanos
Inflamação/induzido quimicamente
Inflamação/metabolismo
Lipopolissacarídeos/toxicidade
Camundongos
Fosforilação/efeitos dos fármacos
Fosforilação/fisiologia
Células RAW 264.7
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Inflammation Mediators); 0 (Lipopolysaccharides); 0 (Membrane Glycoproteins); 0 (Myd88 protein, mouse); 0 (Myeloid Differentiation Factor 88); 0 (Receptors, Interleukin-1); 0 (TIRAP protein, mouse); 0 (Tlr4 protein, mouse); 0 (Toll-Like Receptor 4); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


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[PMID]:28468300
[Au] Autor:Sp N; Kang DY; Joung YH; Park JH; Kim WS; Lee HK; Song KD; Park YM; Yang YM
[Ad] Endereço:Department of Pathology, School of Medicine, Institute of Biomedical Science and Technology, Konkuk University, Seoul 05029, Korea. nipinsp@gmail.com.
[Ti] Título:Nobiletin Inhibits Angiogenesis by Regulating Src/FAK/STAT3-Mediated Signaling through PXN in ER⁺ Breast Cancer Cells.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 30.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Tumor angiogenesis is one of the major hallmarks of tumor progression. Nobiletin is a natural flavonoid isolated from citrus peel that has anti-angiogenic activity. Steroid receptor coactivator (Src) is an intracellular tyrosine kinase so that focal adhesion kinase (FAK) binds to Src to play a role in tumor angiogenesis. Signal transducer and activator of transcription 3 (STAT3) is a marker for tumor angiogenesis which interacts with Src. Paxillin (PXN) acts as a downstream target for both FAK and STAT3. The main goal of this study was to assess inhibition of tumor angiogenesis by nobiletin in estrogen receptor positive (ER⁺) breast cancer cells via Src, FAK, and STAT3-mediated signaling through PXN. Treatment with nobiletin in MCF-7 and T47D breast cancer cells inhibited angiogenesis markers, based on western blotting and RT-PCR. Validation of in vitro angiogenesis in the human umbilical vein endothelial cells (HUVEC) endothelial cell line proved the anti-angiogenic activity of nobiletin. Electrophoretic mobility shift assay and the ChIP assay showed that nobiletin inhibits STAT3/DNA binding activity and STAT3 binding to a novel binding site of the gene promoter. We also investigated the migration and invasive ability of nobiletin in ER⁺ cells. Nobiletin inhibited tumor angiogenesis by regulating Src, FAK, and STAT3 signaling through PXN in ER⁺ breast cancer cells.
[Mh] Termos MeSH primário: Inibidores da Angiogênese/farmacologia
Flavonas/farmacologia
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Paxilina/metabolismo
Receptores Estrogênicos/metabolismo
Fator de Transcrição STAT3/metabolismo
Quinases da Família src/metabolismo
[Mh] Termos MeSH secundário: Proliferação Celular
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/metabolismo
Células Endoteliais da Veia Umbilical Humana/fisiologia
Seres Humanos
Células MCF-7
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Angiogenesis Inhibitors); 0 (Flavones); 0 (Paxillin); 0 (Receptors, Estrogen); 0 (STAT3 Transcription Factor); D65ILJ7WLY (nobiletin); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  5 / 8777 MEDLINE  
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[PMID]:29324748
[Au] Autor:Shahzad MMK; Felder M; Ludwig K; Van Galder HR; Anderson ML; Kim J; Cook ME; Kapur AK; Patankar MS
[Ad] Endereço:Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin, United States of America.
[Ti] Título:Trans10,cis12 conjugated linoleic acid inhibits proliferation and migration of ovarian cancer cells by inducing ER stress, autophagy, and modulation of Src.
[So] Source:PLoS One;13(1):e0189524, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The goal of this study was to investigate the anti-cancer effects of Trans10,cis12 conjugated linoleic acid (t10,c12 CLA). MTT assays and QCM™ chemotaxis 96-wells were used to test the effect of t10,c12 CLA on the proliferation and migration and invasion of cancer cells. qPCR and Western Blotting were used to determine the expression of specific factors. RNA sequencing was conducted using the Illumina platform and apoptosis was measured using a flow cytometry assay. t10,c12 CLA (IC50, 7 µM) inhibited proliferation of ovarian cancer cell lines SKOV-3 and A2780. c9,t11 CLA did not attenuate the proliferation of these cells. Transcription of 165 genes was significantly repressed and 28 genes were elevated. Genes related to ER stress, ATF4, CHOP, and GADD34 were overexpressed whereas EDEM2 and Hsp90, genes required for proteasomal degradation of misfolded proteins, were downregulated upon treatment. While apoptosis was not detected, t10,c12 CLA treatment led to 9-fold increase in autophagolysosomes and higher levels of LC3-II. G1 cell cycle arrest in treated cells was correlated with phosphorylation of GSK3ß and loss of ß-catenin. microRNA miR184 and miR215 were upregulated. miR184 likely contributed to G1 arrest by downregulating E2F1. miR215 upregulation was correlated with increased expression of p27/Kip-1. t10,c12 CLA-mediated inhibition of invasion and migration correlated with decreased expression of PTP1b and decreased Src activation by inhibiting phosphorylation at Tyr416. Due to its ability to inhibit proliferation and migration, t10,c12 CLA should be considered for treatment of ovarian cancer.
[Mh] Termos MeSH primário: Autofagia/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Ácidos Linoleicos Conjugados/farmacologia
Neoplasias Ovarianas/patologia
Quinases da Família src/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Feminino
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Linoleic Acids, Conjugated); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189524


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[PMID]:28740133
[Au] Autor:Konitsiotis AD; Roßmannek L; Stanoev A; Schmick M; Bastiaens PIH
[Ad] Endereço:Department of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
[Ti] Título:Spatial cycles mediated by UNC119 solubilisation maintain Src family kinases plasma membrane localisation.
[So] Source:Nat Commun;8(1):114, 2017 07 24.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The peripheral membrane proto-oncogene Src family protein tyrosine kinases relay growth factor signals to the cytoplasm of mammalian cells. We unravel the spatial cycles of solubilisation, trapping on perinuclear membrane compartments and vesicular transport that counter entropic equilibration to endomembranes for maintaining the enrichment and activity of Src family protein tyrosine kinases at the plasma membrane. The solubilising factor UNC119 sequesters myristoylated Src family protein tyrosine kinases from the cytoplasm, enhancing their diffusion to effectively release Src family protein tyrosine kinases on the recycling endosome by localised Arl2/3 activity. Src is then trapped on the recycling endosome via electrostatic interactions, whereas Fyn is quickly released to be kinetically trapped on the Golgi by palmitoyl acyl-transferase activity. Vesicular trafficking from these compartments restores enrichment of the Src family protein tyrosine kinases to the plasma membrane. Interference with these spatial cycles by UNC119 knockdown disrupts Src family protein tyrosine kinase localisation and signalling activity, indicating that UNC119 could be a drug target to affect oncogenic Src family protein tyrosine kinase signalling.The peripheral membrane proto-oncogene Src family protein tyrosine kinases (SFKs) transmit growth factor signals to the cytoplasm. Here the authors show that the solubilising factor UNC119 sequesters myristoylated SFKs to maintain its enrichment at the plasma membrane to enable signal transduction.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Membrana Celular/metabolismo
Transdução de Sinais
Quinases da Família src/metabolismo
[Mh] Termos MeSH secundário: Fatores de Ribosilação do ADP/genética
Fatores de Ribosilação do ADP/metabolismo
Proteínas Adaptadoras de Transdução de Sinal/química
Proteínas Adaptadoras de Transdução de Sinal/genética
Linhagem Celular
Endossomos/metabolismo
Proteínas de Ligação ao GTP/genética
Proteínas de Ligação ao GTP/metabolismo
Complexo de Golgi/metabolismo
Células HT29
Células HeLa
Seres Humanos
Immunoblotting
Microscopia Confocal
Modelos Biológicos
Ácido Mirístico/metabolismo
Ligação Proteica
Proteínas Proto-Oncogênicas c-fyn/genética
Proteínas Proto-Oncogênicas c-fyn/metabolismo
Interferência de RNA
Solubilidade
Quinases da Família src/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (UNC119 protein, human); 0I3V7S25AW (Myristic Acid); EC 2.7.10.2 (Proto-Oncogene Proteins c-fyn); EC 2.7.10.2 (src-Family Kinases); EC 3.6.1.- (ARL2 protein, human); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.5.2 (ADP-Ribosylation Factors); EC 3.6.5.2 (ARL3 protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00116-3


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[PMID]:28671269
[Au] Autor:Urciuoli E; Coletta I; Rizzuto E; De Vito R; Petrini S; D'Oria V; Pezzullo M; Milano GM; Cozza R; Locatelli F; Peruzzi B
[Ad] Endereço:Research Laboratories, Bambino Gesù Children's Hospital, Rome, Italy.
[Ti] Título:Src nuclear localization and its prognostic relevance in human osteosarcoma.
[So] Source:J Cell Physiol;233(2):1658-1670, 2018 Feb.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Osteosarcoma is the most common malignant bone tumor in children and young adults. The identification of proteins which exhibit different subcellular localization in low- versus high-risk osteosarcoma can be instrumental to obtain prognostic information and to develop innovative therapeutic strategies. Beside the well-characterized membrane and cytoplasmic localization of Src protein, this study evaluated the prognostic relevance of its so-far unknown nuclear compartmentalization. We analyzed the subcellular distribution of total and activated (pY418) Src in a tissue microarray including 60 osteosarcoma samples. Immunohistochemical analyses revealed a variable pattern of Src expression and localization, ranging from negative to high-stained nuclei combined with a substantial cytoplasmic staining for total and activated forms. The analysis of Kaplan-Meier survival curves in relationship to the diverse permutations of cytoplasmic and nuclear staining suggested a correlation between Src subcellular localization and the overall survival (OS) of osteosarcoma patients. In order to explain this different subcellular localization, normal osteoblasts and three osteosarcoma cell lines were used to investigate the molecular mechanism. Once confirmed a variable Src localization also in these cell lines, we demonstrated a correlation between the N-myristoyltransferase enzymes expression and activity and the Src nuclear content. In conclusion, these results described a so-far unknown Src nuclear localization in osteosarcoma cells, suggesting that the combined detection of nuclear and cytoplasmic Src levels can be used as a prognostic marker for osteosarcoma patient survival. A correlation between the N-myristoyltransferase enzymes and the Src subcellular localization was described as well.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Neoplasias Ósseas/enzimologia
Núcleo Celular/enzimologia
Osteossarcoma/enzimologia
Quinases da Família src/metabolismo
[Mh] Termos MeSH secundário: Aciltransferases/metabolismo
Adolescente
Adulto
Neoplasias Ósseas/mortalidade
Neoplasias Ósseas/patologia
Neoplasias Ósseas/terapia
Linhagem Celular Tumoral
Criança
Ativação Enzimática
Feminino
Seres Humanos
Estimativa de Kaplan-Meier
Masculino
Osteossarcoma/mortalidade
Osteossarcoma/patologia
Osteossarcoma/terapia
Prognóstico
Processamento de Proteína Pós-Traducional
Fatores de Tempo
Análise Serial de Tecidos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 2.3.- (Acyltransferases); EC 2.3.1.97 (glycylpeptide N-tetradecanoyltransferase); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.26079


  8 / 8777 MEDLINE  
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[PMID]:28471594
[Au] Autor:Liossis SC; Konstantopoulou GM
[Ad] Endereço:University of Patras Medical School, Patras, Greece.
[Ti] Título:The Potential Role of Lyn Kinase in Systemic Lupus Erythematosus and Autoimmunity.
[So] Source:Isr Med Assoc J;18(9):513-515, 2016 Sep.
[Is] ISSN:1565-1088
[Cp] País de publicação:Israel
[La] Idioma:eng
[Mh] Termos MeSH primário: Autoimunidade/fisiologia
Lúpus Eritematoso Sistêmico/enzimologia
Quinases da Família src/metabolismo
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Seres Humanos
Lúpus Eritematoso Sistêmico/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.10.2 (lyn protein-tyrosine kinase); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


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[PMID]:27777385
[Au] Autor:Miwa S; Czapiewski R; Wan T; Bell A; Hill KN; von Zglinicki T; Saretzki G
[Ad] Endereço:Institute for Cell and Molecular Biosciences, Newcastle Institute for Ageing, Campus for Ageing and Vitality, Newcastle University, Newcastle upon Tyne, NE4 5PL, UK.
[Ti] Título:Decreased mTOR signalling reduces mitochondrial ROS in brain via accumulation of the telomerase protein TERT within mitochondria.
[So] Source:Aging (Albany NY);8(10):2551-2567, 2016 Oct 22.
[Is] ISSN:1945-4589
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Telomerase in its canonical function maintains telomeres in dividing cells. In addition, the telomerase protein TERT has non-telomeric functions such as shuttling to mitochondria resulting in a decreased oxidative stress, DNA damage and apoptosis. TERT protein persists in adult neurons and can co-localise to mitochondria under various stress conditions. We show here that TERT expression decreased in mouse brain during aging while release of reactive oxygen species (ROS) from the mitochondrial electron transport chain increased. Dietary restriction (DR) caused accumulation of TERT protein in mouse brain mitochondria correlating to decreased ROS release and improved learning and spatial short-term memory. Decreased mTOR signalling is a mediator of DR. Accordingly, feeding mice with rapamycin increased brain mitochondrial TERT and reduced ROS release. Importantly, the beneficial effects of rapamycin on mitochondrial function were absent in brains and fibroblasts from first generation TERT -/- mice, and when TERT shuttling was inhibited by the Src kinase inhibitor bosutinib. Taken together, our data suggests that the mTOR signalling pathway impinges on the mitochondrial localisation of TERT protein, which might in turn contribute to the protection of the brain by DR or rapamycin against age-associated mitochondrial ROS increase and cognitive decline.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Mitocôndrias/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais/fisiologia
Serina-Treonina Quinases TOR/metabolismo
Telomerase/metabolismo
[Mh] Termos MeSH secundário: Compostos de Anilina/farmacologia
Animais
Encéfalo/efeitos dos fármacos
Camundongos
Camundongos Knockout
Nitrilos/farmacologia
Estresse Oxidativo/efeitos dos fármacos
Quinolinas/farmacologia
Transdução de Sinais/efeitos dos fármacos
Sirolimo/farmacologia
Telomerase/genética
Quinases da Família src/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aniline Compounds); 0 (Nitriles); 0 (Quinolines); 0 (Reactive Oxygen Species); 5018V4AEZ0 (bosutinib); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.1.1 (mTOR protein, mouse); EC 2.7.10.2 (src-Family Kinases); EC 2.7.7.49 (Telomerase); EC 2.7.7.49 (Tert protein, mouse); W36ZG6FT64 (Sirolimus)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE
[do] DOI:10.18632/aging.101089


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[PMID]:29053950
[Au] Autor:Michnick SW
[Ad] Endereço:Département de Biochimie, Université de Montréal, C.P. 6128, Succursale Centre-ville, Montréal, QC H3C 3J7, Canada; Centre Robert-Cedergren, Bio-Informatique et Génomique, Université de Montréal, C.P. 6128, Succursale Centre-ville, Montréal, QC H3C 3J7, Canada. Electronic address: stephen.michnick@umontreal.ca.
[Ti] Título:More than One Way to Skin a Catalyst.
[So] Source:Cell Chem Biol;24(10):1196-1197, 2017 Oct 19.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this issue of Cell Chemical Biology, Diaz et al. (2017) report a strategy to achieve temporal, spatial, and stoichiometric control over the protein kinase cAbl in living cells. They achieve this by splitting cAbl into two inactive fragments that form an active kinase upon small molecule addition, potentially providing a general way to probe the wiring of signal transduction networks.
[Mh] Termos MeSH primário: Biocatálise
Engenharia de Proteínas
Proteínas Proto-Oncogênicas c-abl/metabolismo
[Mh] Termos MeSH secundário: Ativação Enzimática/efeitos dos fármacos
Células HeLa
Seres Humanos
Proteínas Proto-Oncogênicas c-abl/genética
Transdução de Sinais/efeitos dos fármacos
Quinases da Família src/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.10.2 (Proto-Oncogene Proteins c-abl); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE



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