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  1 / 6819 MEDLINE  
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[PMID]:29395079
[Au] Autor:Münzer P; Mittelstädt S; Geue S; Manke MC; Walker-Allgaier B; Lang F; Gawaz M; Borst O
[Ad] Endereço:Department of Cardiology and Cardiovascular Medicine, University of Tübingen, Germany.
[Ti] Título:Ceramidase critically affects GPVI-dependent platelet activation and thrombus formation.
[So] Source:Biochem Biophys Res Commun;496(3):792-798, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Platelet aggregation, dense granule secretion and thrombus formation are dependent on sphingolipids like ceramide and sphingosine as well as sphingosine-1 phosphate. Sphingosine/ceramide metabolism involves ceramide synthases and ceramidases. However, the role of ceramide synthase and ceramidase in the regulation of platelet function remained ill-defined. The present study determined transmission light aggregometry, employed luciferase based ATP release measurements and studied in vitro thrombus formation under high arterial shear rates in order to define the impact of pharmacological inhibition of serine palmitoyltransferase, ceramide synthase and ceramidase on platelet function. As a result, inhibition of ceramidase significantly blunted collagen related peptide (CRP) induced glyocoprotein VI (GPVI)-dependent platelet aggregation, ATP release and thrombus formation on a collagen-coated surface under shear rates of 1700 . Defective platelet aggregation after ceramidase inhibition could partially be overcome by exogenous sphingosine treatment reflecting a pivotal role of ceramidase-derived sphingosine in platelet function. Inhibition of serine palmitoyltransferase and ceramide synthase did not significantly modify GPVI-dependent platelet activation. In conclusion, the present study unraveled ceramidase as a crucial player in sphingosine-induced platelet activation following GPVI-dependent signaling.
[Mh] Termos MeSH primário: Plaquetas/enzimologia
Ceramidases/metabolismo
Agregação Plaquetária
Glicoproteínas da Membrana de Plaquetas/metabolismo
Trombose/enzimologia
Trombose/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Feminino
Masculino
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Platelet Membrane Glycoproteins); 0 (platelet membrane glycoprotein VI); EC 3.5.1.23 (Ceramidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180204
[St] Status:MEDLINE


  2 / 6819 MEDLINE  
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[PMID]:29278700
[Au] Autor:Wang EW; Han YY; Jia XS
[Ad] Endereço:Department of Cardiac Surgery, Linyi People's Hospital, Linyi 276000, China.
[Ti] Título:PAFR-deficiency alleviates myocardial ischemia/reperfusion injury in mice via suppressing inflammation, oxidative stress and apoptosis.
[So] Source:Biochem Biophys Res Commun;495(4):2475-2481, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myocardial ischemia/reperfusion (I/R) still have high morbidity and mortality worldwide. Platelet activating factor (PAF) is a potent phospholipid regulator of inflammation. PAF acts on a single receptor (PAFR), which is expressed on cellular and nuclear membranes of various cell types. The study is aimed to explore if PAFR could modulate myocardial I/R injury in mice. PAFR expressions began to up-regulate at 1 h, and reached peak at 24 h. PAFR deletion markedly attenuated myocardial I/R injury, evidenced by the reduced infarct size and the improved cardiac function. Furthermore, PAFR-knockout inhibited inflammatory response, as demonstrated by down-regulated pro-inflammatory cytokines and chemokine, as well as the inactivation of nuclear factor κB (NF-κB). Additionally, PAFR-absence ameliorated oxidative stress induced by myocardial I/R, associated with the up-regulation of superoxide dismutase (SOD) and nuclear respiratory factor 2 (Nrf-2) activity. Finally, PAFR-deficiency impeded apoptosis, which was proved by the decreasing in terminal deoxynucleotidyl transferase (TdT)-mediated dNTP nick end labeling (TUNEL)-positive myocytes, and Caspase-3 cleavage. And the activation of Janus kinase 1-signal transducer and activator of transcription 1 (JAK1/STAT1) pathway was also suppressed by PAFR-knockout. The findings above were confirmed in lipopolysaccharide (LPS)-incubated cardiomyocytes with or without PAFR expressions in vitro. In summary, we supposed that inhibiting PAFR reduced inflammation, oxidative stress and apoptosis, and thus might be a promising therapeutic strategy to alleviate myocardial I/R injury.
[Mh] Termos MeSH primário: Apoptose/imunologia
Traumatismo por Reperfusão Miocárdica/imunologia
Miocardite/imunologia
Estresse Oxidativo/imunologia
[Mh] Termos MeSH secundário: Animais
Citocinas/imunologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Traumatismo por Reperfusão Miocárdica/patologia
Miocardite/patologia
Glicoproteínas da Membrana de Plaquetas/genética
Glicoproteínas da Membrana de Plaquetas/imunologia
Receptores Acoplados a Proteínas-G/genética
Receptores Acoplados a Proteínas-G/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Platelet Membrane Glycoproteins); 0 (Receptors, G-Protein-Coupled); 0 (platelet activating factor receptor)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


  3 / 6819 MEDLINE  
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[PMID]:28855423
[Au] Autor:Yao Y; Chen Y; Adili R; McKeown T; Chen P; Zhu G; Li D; Ling W; Ni H; Yang Y
[Ad] Endereço:Department of Nutrition, School of Public Health, Sun Yat-Sen University, Guangzhou, People's Republic of China.
[Ti] Título:Plant-based Food Cyanidin-3-Glucoside Modulates Human Platelet Glycoprotein VI Signaling and Inhibits Platelet Activation and Thrombus Formation.
[So] Source:J Nutr;147(10):1917-1925, 2017 Oct.
[Is] ISSN:1541-6100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Platelets play an important role in hemostasis, thrombosis, and atherosclerosis. Glycoprotein VI (GPVI) is a major platelet receptor that interacts with exposed collagen on injured vessel walls. Our previous studies have shown that anthocyanins (a type of natural plant pigment) attenuate platelet function; however, whether anthocyanins affect collagen-induced GPVI signaling remains unknown. The objective of this study was to explore the effects of cyanidin-3-glucoside (Cy-3-g, one of the major bioactive compounds in anthocyanins) on platelet activation and thrombosis and the GPVI signaling pathway. Platelets from healthy men and women were isolated and incubated with different concentrations (0, 0.5, 5, and 50 µM) of Cy-3-g. The expression of activated integrin αIIbß3, P-selectin, CD63, and CD40L, fibrinogen binding to platelets, and platelet aggregation were evaluated in vitro. Platelet adhesion and aggregation in whole blood under flow conditions were assessed in collagen-coated perfusion chambers. Thrombosis and hemostasis were assessed in 3-4-wk-old male C57BL/6J mice through FeCl -induced intravital microscopy and tail bleeding time. The effect of Cy-3-g on collagen-induced human platelet GPVI signaling was explored with Western blot. Cy-3-g attenuated platelet function in a dose-dependent manner. The 0.5-µM dose of Cy-3-g inhibited ( < 0.05) human platelet adhesion and aggregation to collagen at both venous (-54.02%) and arterial (-22.90%) shear stresses. The 5-µM dose inhibited ( < 0.05) collagen-induced human platelet activation (PAC-1: -48.21%, P-selectin: -50.63%), secretion (CD63: -73.89%, CD40L: -43.70%), fibrinogen binding (-56.79%), and aggregation (-17.81%). The 5-µM dose attenuated ( < 0.01) thrombus growth (-66.67%) without prolonging bleeding time in mice. The 50-µM dose downregulated ( < 0.05) collagen-induced GPVI signaling in human platelets and significantly decreased phosphorylation of Syk-linker for activation of T cells (LAT)-SLP76 (Syk: -39.08%, LAT: -32.25%, SLP76: -40.00%) and the expression of Lyn (-31.89%), Fyn (-36.27%), and phospholipase C-γ2 (-39.08%). Cy-3-g inhibits human platelet activation, aggregation, secretion, and thrombus formation, and downregulates the collagen-GPVI signaling pathway. Supplementation of Cy-3-g may have protective effects against atherothrombosis.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Fitoterapia
Extratos Vegetais/farmacologia
Plantas Comestíveis/química
Agregação Plaquetária/efeitos dos fármacos
Glicoproteínas da Membrana de Plaquetas/metabolismo
Trombose/prevenção & controle
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/sangue
Adulto
Idoso
Animais
Antocianinas/farmacologia
Antocianinas/uso terapêutico
Antígenos CD/sangue
Aterosclerose/sangue
Aterosclerose/dietoterapia
Aterosclerose/etiologia
Colágeno/sangue
Feminino
Glucosídeos/farmacologia
Glucosídeos/uso terapêutico
Hemostasia/efeitos dos fármacos
Seres Humanos
Masculino
Camundongos Endogâmicos C57BL
Meia-Idade
Selectina-P/sangue
Fosfoproteínas/sangue
Extratos Vegetais/uso terapêutico
Ativação Plaquetária/efeitos dos fármacos
Transdução de Sinais
Trombose/sangue
Trombose/etiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Anthocyanins); 0 (Antigens, CD); 0 (Glucosides); 0 (P-Selectin); 0 (Phosphoproteins); 0 (Plant Extracts); 0 (Platelet Membrane Glycoproteins); 0 (SELP protein, human); 0 (SLP-76 signal Transducing adaptor proteins); 0 (platelet membrane glycoprotein VI); 7084-24-4 (cyanidin 3-O-glucoside); 9007-34-5 (Collagen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.3945/jn.116.245944


  4 / 6819 MEDLINE  
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[PMID]:28760822
[Au] Autor:Holdfeldt A; Dahlstrand Rudin A; Gabl M; Rajabkhani Z; König GM; Kostenis E; Dahlgren C; Forsman H
[Ad] Endereço:Department of Rheumatology and Inflammation Research, University of Gothenburg, Gothenburg, Sweden.
[Ti] Título:Reactivation of Gαi-coupled formyl peptide receptors is inhibited by Gαq-selective inhibitors when induced by signals generated by the platelet-activating factor receptor.
[So] Source:J Leukoc Biol;102(3):871-880, 2017 Sep.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Formyl peptide receptor (FPR)-desensitized neutrophils display increased production/release of superoxide (O ) when activated by platelet-activating factor (PAF), a priming of the response achieved through a unique receptor crosstalk mechanism. The aim of this study was to determine the effect of an inhibitor selective for small, heterotrimeric G proteins belonging to the Gαq subclass on that receptor crosstalk. We show that signals generated by FPRs and the PAF receptor (PAFR) induce activation of the neutrophil O , producing NADPH-oxidase, and that response was sensitive to Gαq inhibition in cells activated by PAF, but no inhibition was obtained in cells activated by FPR agonists. Signaling in naive neutrophils is terminated fairly rapidly, and the receptors become homologously desensitized. The downstream sensitivity to Gαq inhibition in desensitized cells displaying increased production/release of O through the PAFR receptor crosstalk mechanism also comprised the reactivation of the FPRs, and the activation signals were redirected from the PAFR to the desensitized/reactivated FPRs. The Gαq-dependent activation signals generated by the PAFRs activate the Gαi-coupled FPRs, a receptor crosstalk that represents a novel pathway by which G protein-coupled receptors can be regulated and signaling can be turned on and off.
[Mh] Termos MeSH primário: Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/imunologia
Neutrófilos/imunologia
Glicoproteínas da Membrana de Plaquetas/imunologia
Receptores de Formil Peptídeo/imunologia
Receptores Acoplados a Proteínas-G/imunologia
Transdução de Sinais/imunologia
[Mh] Termos MeSH secundário: Seres Humanos
NADPH Oxidases/imunologia
Fator de Ativação de Plaquetas/imunologia
Superóxidos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Platelet Activating Factor); 0 (Platelet Membrane Glycoproteins); 0 (Receptors, Formyl Peptide); 0 (Receptors, G-Protein-Coupled); 0 (platelet activating factor receptor); 11062-77-4 (Superoxides); EC 1.6.3.- (NADPH Oxidases); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gq-G11)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.2A0317-086RR


  5 / 6819 MEDLINE  
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[PMID]:28704418
[Au] Autor:Parkin JD; San Antonio JD; Persikov AV; Dagher H; Dalgleish R; Jensen ST; Jeunemaitre X; Savige J
[Ad] Endereço:From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.
[Ti] Título:The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.
[So] Source:PLoS One;12(7):e0175582, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2ß1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.
[Mh] Termos MeSH primário: Colágeno Tipo III/química
Colágeno Tipo III/metabolismo
Hemostasia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Colágeno Tipo III/genética
Seres Humanos
Integrina alfa2beta1/metabolismo
Glicoproteínas da Membrana de Plaquetas/metabolismo
Ligação Proteica
Mapas de Interação de Proteínas
Estabilidade Proteica
Fator de von Willebrand/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type III); 0 (Integrin alpha2beta1); 0 (Platelet Membrane Glycoproteins); 0 (platelet membrane glycoprotein VI); 0 (von Willebrand Factor)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175582


  6 / 6819 MEDLINE  
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[PMID]:28686728
[Au] Autor:Hamel-Côté G; Gendron D; Rola-Pleszczynski M; Stankova J
[Ad] Endereço:Immunology Division, Department of Pediatrics, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, QC, Canada.
[Ti] Título:Regulation of platelet-activating factor-mediated protein tyrosine phosphatase 1B activation by a Janus kinase 2/calpain pathway.
[So] Source:PLoS One;12(7):e0180336, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Atherosclerosis is a pro-inflammatory condition underlying many cardiovascular diseases. Platelet-activating factor (PAF) and interleukin 6 (IL-6) are actively involved in the onset and progression of atherosclerotic plaques. The involvement of monocyte-derived macrophages is well characterized in the installation of inflammatory conditions in the plaque, but less is known about the contribution of monocyte-derived dendritic cells (Mo-DCs). In the same way, the involvement of calcium, phospholipase C and A2 in PAF-induced IL-6 production, in different cells types, has been shown; however, the importance of the Jak/STAT pathway and its regulation by protein-tyrosine phosphatases in this response have not been addressed. In this study, we report that PAF stimulates PTP1B activity via Jak2, thereby modulating PAF-induced IL-6 production. Using HEK 293 cells stably transfected with the PAF receptor in order to discriminate the pathway components, our results suggest that Jak2 modulates PAF-induced IL-6 production via both positive and negative pathways. Jak2 kinase activity was necessary for maximal transactivation of the IL-6 promoter, as seen by luciferase assays, whereas the same kinase also downregulated this promoter transactivation through the activation of a calcium/calpain/PTP1B pathway. The same pathways were operational in monocyte-derived dendritic cells, since PAF-induced PTP1B activation negatively regulated PAF-induced IL-6 mRNA production and, in addition, Jak2 activated calpain, one of the components involved in PAF-induced PTP1B activation. Results obtained in this study indicate that Jak2 activation is important for maximal IL-6 promoter transactivation by PAF and that PTP1B is involved in the negative regulation of this transactivation. However, PTP1B does not directly regulate Jak2 activation, but rather Jak2 regulates PAF-induced PTP1B activation.
[Mh] Termos MeSH primário: Calpaína/genética
Células Dendríticas/metabolismo
Janus Quinase 2/genética
Glicoproteínas da Membrana de Plaquetas/genética
Proteína Tirosina Fosfatase não Receptora Tipo 1/genética
Receptores Acoplados a Proteínas-G/genética
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Calpaína/metabolismo
Células Dendríticas/citologia
Regulação da Expressão Gênica
Genes Reporter
Células HEK293
Seres Humanos
Interleucina-6/genética
Interleucina-6/metabolismo
Janus Quinase 2/metabolismo
Luciferases/genética
Luciferases/metabolismo
Macrófagos/citologia
Macrófagos/metabolismo
Glicoproteínas da Membrana de Plaquetas/metabolismo
Cultura Primária de Células
Regiões Promotoras Genéticas
Proteína Tirosina Fosfatase não Receptora Tipo 1/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL6 protein, human); 0 (Interleukin-6); 0 (Platelet Membrane Glycoproteins); 0 (Receptors, G-Protein-Coupled); 0 (platelet activating factor receptor); EC 1.13.12.- (Luciferases); EC 2.7.10.2 (JAK2 protein, human); EC 2.7.10.2 (Janus Kinase 2); EC 3.1.3.48 (PTPN1 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 1); EC 3.4.22.- (Calpain); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180336


  7 / 6819 MEDLINE  
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[PMID]:28667161
[Au] Autor:Patel PS; Kearney JF
[Ad] Endereço:Department of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294.
[Ti] Título:CD36 and Platelet-Activating Factor Receptor Promote House Dust Mite Allergy Development.
[So] Source:J Immunol;199(3):1184-1195, 2017 Aug 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Over 89% of asthmatic children in underdeveloped countries demonstrate sensitivity to house dust mites (HDMs). The allergic response to HDMs is partially mediated by epithelial cell-derived cytokines that activate group 2 innate lymphoid cells, induce migration and activation of dendritic cells, and promote effector differentiation of HDM-specific TH2 cells. However, the contribution of innate receptor engagement on epithelial or dendritic cells by HDMs that ultimately mediates said innate and adaptive allergic responses is poorly understood. We and other investigators have demonstrated that HDMs express phosphorylcholine (PC) moieties. The major PC receptors involved in immune responses include CD36 and platelet-activating factor receptor (PAFR). Because CD36 and PAFR are expressed by epithelial cells and dendritic cells, and expression of these receptors is higher in human asthmatics, we determined whether engagement of CD36 or PAFR on epithelial or dendritic cells contributes to HDM allergy development. Testing bone marrow chimeric mice revealed that CD36 engagement on radioresistant cells and PAFR engagement on radioresistant and radiosensitive cells in the lung promote allergic responses to HDMs. Additionally, passive anti-PC IgM Abs administered intratracheally with HDMs decreased allergen uptake by epithelial cells and APCs in the lungs of C57BL/6 mice but not CD36 or PAFR mice. These results show that CD36 and PAFR are important mediators of HDM allergy development and that inhibiting HDM engagement with PC receptors in the lung protects against allergic airway disease.
[Mh] Termos MeSH primário: Antígenos CD36/imunologia
Antígenos CD36/metabolismo
Glicoproteínas da Membrana de Plaquetas/imunologia
Glicoproteínas da Membrana de Plaquetas/metabolismo
Pyroglyphidae/imunologia
Receptores Acoplados a Proteínas-G/imunologia
Receptores Acoplados a Proteínas-G/metabolismo
[Mh] Termos MeSH secundário: Alérgenos/imunologia
Animais
Antígenos de Dermatophagoides/imunologia
Asma/imunologia
Asma/prevenção & controle
Antígenos CD36/deficiência
Antígenos CD36/genética
Células Dendríticas/imunologia
Células Epiteliais/imunologia
Hipersensibilidade/imunologia
Hipersensibilidade/prevenção & controle
Imunidade Inata
Imunoglobulina M/administração & dosagem
Pulmão/imunologia
Camundongos
Camundongos Endogâmicos C57BL
Fosforilcolina/química
Fosforilcolina/imunologia
Pyroglyphidae/química
Hipersensibilidade Respiratória/imunologia
Hipersensibilidade Respiratória/prevenção & controle
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Antigens, Dermatophagoides); 0 (CD36 Antigens); 0 (Immunoglobulin M); 0 (Platelet Membrane Glycoproteins); 0 (Receptors, G-Protein-Coupled); 0 (platelet activating factor receptor); 107-73-3 (Phosphorylcholine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700034


  8 / 6819 MEDLINE  
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[PMID]:28618256
[Au] Autor:Kispert S; Schwartz T; McHowat J
[Ad] Endereço:Department of Pathology, Saint Louis University School of Medicine, St. Louis, Missouri.
[Ti] Título:Cigarette Smoke Regulates Calcium-Independent Phospholipase A Metabolic Pathways in Breast Cancer.
[So] Source:Am J Pathol;187(8):1855-1866, 2017 Aug.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phospholipase A (PLA )-dependent pathways are important in the regulation of cell proliferation, differentiation, motility, and immune responses, and can be dysregulated during tumor development and progression. We show herein, for the first time, that cigarette smoking leads to an increase in platelet-activating factor (PAF) content and PAF receptor expression in human breast cancer cells and tissue. PAF production could be abrogated in triple-negative breast cancer cells by inhibition of calcium-independent PLA (iPLA ). We also demonstrate that cigarette smoke induces the expression of cyclooxygenase-2 and microsomal prostaglandin E synthase-1 and reduces 15-hydroxyprostaglandin dehydrogenase, resulting in prostaglandin E release in human breast cancer. Increased cyclooxygenase-2 expression and prostaglandin E release could be abrogated in metastatic breast cancer cells by inhibition of iPLA . These studies indicate that iPLA -dependent metabolic pathways play an important role in tumor initiation or progression in smokers, representing novel therapeutic targets for breast cancer patients who smoke.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Fosfolipases A2 Independentes de Cálcio/metabolismo
Fator de Ativação de Plaquetas/metabolismo
Glicoproteínas da Membrana de Plaquetas/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
Fumaça
Fumar/metabolismo
Neoplasias de Mama Triplo Negativas/metabolismo
[Mh] Termos MeSH secundário: Mama/metabolismo
Mama/patologia
Neoplasias da Mama/patologia
Linhagem Celular Tumoral
Ciclo-Oxigenase 2/metabolismo
Feminino
Seres Humanos
Prostaglandina-E Sintases/metabolismo
Fumar/patologia
Neoplasias de Mama Triplo Negativas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Platelet Activating Factor); 0 (Platelet Membrane Glycoproteins); 0 (Receptors, G-Protein-Coupled); 0 (Smoke); 0 (platelet activating factor receptor); EC 1.14.99.1 (Cyclooxygenase 2); EC 3.1.1.4 (Phospholipases A2, Calcium-Independent); EC 5.3.99.3 (PTGES protein, human); EC 5.3.99.3 (Prostaglandin-E Synthases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE


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[PMID]:28596377
[Au] Autor:Chang CH; Chung CH; Tu YS; Tsai CC; Hsu CC; Peng HC; Tseng YJ; Huang TF
[Ad] Endereço:From the Graduate Institute of Pharmacology, College of Medicine (C.-H.C., C.-C.H., H.-C.P., T.-F.H.), Graduate Institute of Biomedical Electronics and Bioinformatics (Y.-S.T., C.-C.T., Y.J.T.), and Department of Computational Science and Information Engineering (Y.J.T.), National Taiwan University,
[Ti] Título:Trowaglerix Venom Polypeptides As a Novel Antithrombotic Agent by Targeting Immunoglobulin-Like Domains of Glycoprotein VI in Platelet.
[So] Source:Arterioscler Thromb Vasc Biol;37(7):1307-1314, 2017 Jul.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Currently prescribed antiplatelet drugs have 1 common side effect-an increased risk of hemorrhage and thrombocytopenia. On the contrary, bleeding defects associated with glycoprotein VI (GPVI) expression deficiency are usually slightly prolonged bleeding times. However, GPVI antagonists are lacking in clinic. APPROACH AND RESULTS: Using reverse-phase high-performance liquid chromatography and sequencing, we revealed the partial sequence of trowaglerix α subunit, a potent specific GPVI-targeting snaclec (snake venom C-type lectin protein). Hexapeptide (Troα6 [trowaglerix a chain hexapeptide, CKWMNV]) and decapeptide (Troα10) derived from trowaglerix specifically inhibited collagen-induced platelet aggregation through blocking platelet GPVI receptor. Computational peptide design helped to design a series of Troα6/Troα10 peptides. Protein docking studies on these decapeptides and GPVI suggest that Troα10 was bound at the lower surface of D1 domain and outer surface of D2 domain, which was at the different place of the collagen-binding site and the scFv (single-chain variable fragment) D2-binding site. The newly discovered site was confirmed by inhibitory effects of polyclonal antibodies on collagen-induced platelet aggregation. This indicates that D2 domain of GPVI is a novel and important binding epitope on GPVI-mediated platelet aggregation. Troα6/Troα10 displayed prominent inhibitory effect of thrombus formation in fluorescein sodium-induced platelet thrombus formation of mesenteric venules and ferric chloride-induced carotid artery injury thrombosis model without prolonging the in vivo bleeding time. CONCLUSIONS: We develop a novel antithrombotic peptides derived from trowaglerix that acts through GPVI antagonism with greater safety-no severe bleeding. The binding epitope of polypeptides on GPVI is novel and important. These hexa/decapeptides have therapeutic potential for developing ideal small-mass GPVI antagonists for arterial thrombogenic diseases.
[Mh] Termos MeSH primário: Plaquetas/efeitos dos fármacos
Lesões das Artérias Carótidas/tratamento farmacológico
Venenos de Crotalídeos/farmacologia
Fibrinolíticos/farmacologia
Fragmentos de Peptídeos/farmacologia
Inibidores da Agregação de Plaquetas/farmacologia
Agregação Plaquetária/efeitos dos fármacos
Glicoproteínas da Membrana de Plaquetas/antagonistas & inibidores
Trombose/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Plaquetas/metabolismo
Lesões das Artérias Carótidas/sangue
Lesões das Artérias Carótidas/induzido quimicamente
Cloretos
Projeto Auxiliado por Computador
Venenos de Crotalídeos/metabolismo
Venenos de Crotalídeos/toxicidade
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Desenho de Drogas
Compostos Férricos
Fibrinolíticos/metabolismo
Fibrinolíticos/toxicidade
Fluoresceína
Hemorragia/induzido quimicamente
Seres Humanos
Lectinas Tipo C/metabolismo
Masculino
Camundongos Endogâmicos ICR
Simulação de Acoplamento Molecular
Fragmentos de Peptídeos/metabolismo
Fragmentos de Peptídeos/toxicidade
Inibidores da Agregação de Plaquetas/metabolismo
Inibidores da Agregação de Plaquetas/toxicidade
Glicoproteínas da Membrana de Plaquetas/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Transdução de Sinais/efeitos dos fármacos
Trombose/sangue
Trombose/induzido quimicamente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chlorides); 0 (Crotalid Venoms); 0 (Ferric Compounds); 0 (Fibrinolytic Agents); 0 (Lectins, C-Type); 0 (Peptide Fragments); 0 (Platelet Aggregation Inhibitors); 0 (Platelet Membrane Glycoproteins); 0 (platelet membrane glycoprotein VI); 0 (trowaglerix protein, Tropidolaemus wagleri); TPY09G7XIR (Fluorescein); U38V3ZVV3V (ferric chloride)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.116.308604


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[PMID]:28441661
[Au] Autor:Gowert NS; Klier M; Reich M; Reusswig F; Donner L; Keitel V; Häussinger D; Elvers M
[Ad] Endereço:Department of Clinical and Experimental Hemostasis, Hemotherapy and Transfusion Medicine, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
[Ti] Título:Defective Platelet Activation and Bleeding Complications upon Cholestasis in Mice.
[So] Source:Cell Physiol Biochem;41(6):2133-2149, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Platelets are essential mediators of hemostasis to avoid excessive blood loss. Cirrhosis and chronic liver diseases are characterized by alterations in hemostasis. Alterations in the secondary hemostasis have been well studied, while defects in primary hemostasis, especially the consequences of cholestatic liver disease on platelet function are not well defined. METHODS: After bile duct ligation (BDL) platelet activation and thrombus formation were analyzed in mice. RESULTS: BDL in mice had a moderate effect on platelet counts; however, intrinsic platelet activation was strongly reduced upon activation of the collagen receptor GPVI at early time points. 7 days after bile duct ligation, platelets displayed an almost complete loss of activation with reduced agonist-triggered release of alpha and dense granules and expression of integrin αIIbß3 on the platelet surface. This activation defects resulted in strongly reduced thrombus formation under flow, reduced platelet adhesion to fibrinogen and bleeding complications in BDL mice as measured by tail bleeding experiments. Mechanistically, elevated nitric oxide and prostacyclin levels induced phosphorylation of Vasodilator-stimulated phosphoprotein (VASP), an established inhibitor of platelet activation. Furthermore increased tissue plasminogen activator in plasma of BDL mice led to enhanced plasmin levels that might be responsible for reduced glycoprotein expression of BDL platelets. Besides, high amounts of bile acids contribute to defective signal transduction as shown in platelets from mice fed with a cholic acid diet. CONCLUSIONS: Cholestatic liver disease induces multiple platelet activation defects and impairs thrombus formation responsible for bleeding complications at least in mice.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Colestase/patologia
[Mh] Termos MeSH secundário: Animais
Plaquetas/citologia
Moléculas de Adesão Celular
Colestase/metabolismo
Modelos Animais de Doenças
Ensaio de Imunoadsorção Enzimática
Epoprostenol/análise
Hemorragia/etiologia
Fígado/patologia
Camundongos
Camundongos Endogâmicos C57BL
Proteínas dos Microfilamentos
Óxido Nítrico/metabolismo
Fosfoproteínas
Fosforilação
Ativação Plaquetária
Contagem de Plaquetas
Complexo Glicoproteico GPIIb-IIIa de Plaquetas/metabolismo
Glicoproteínas da Membrana de Plaquetas/metabolismo
Baço/patologia
Trombose/metabolismo
Trombose/patologia
Ativador de Plasminogênio Tecidual/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Microfilament Proteins); 0 (Phosphoproteins); 0 (Platelet Glycoprotein GPIIb-IIIa Complex); 0 (Platelet Membrane Glycoproteins); 0 (platelet membrane glycoprotein VI); 0 (vasodilator-stimulated phosphoprotein); 31C4KY9ESH (Nitric Oxide); DCR9Z582X0 (Epoprostenol); EC 3.4.21.68 (Tissue Plasminogen Activator)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170426
[St] Status:MEDLINE
[do] DOI:10.1159/000475566



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