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Pesquisa : D12.776.543.750.695.200.575 [Categoria DeCS]
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[PMID]:29305860
[Au] Autor:Zhong X; Lee HN; Surh YJ
[Ad] Endereço:Tumor Microenvironment Global Core Research Center, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea.
[Ti] Título:RvD1 inhibits TNFα-induced c-Myc expression in normal intestinal epithelial cells and destabilizes hyper-expressed c-Myc in colon cancer cells.
[So] Source:Biochem Biophys Res Commun;496(2):316-323, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inflammatory bowel diseases, including ulcerative colitis and Crohn's disease, are persistent disorders that lead to development of colitis-associated cancer (CAC). Facilitated resolution of colitis has been addressed as a novel therapeutic strategy to control development of CAC. Resolvin D1 (RvD1) is an endogenous lipid mediator that is generated from docosahexaenoic acid during the resolution of inflammation. Although the pro-resolving effects of RvDs have been extensively investigated and well defined, the role for RvD1 in CAC remains largely unknown. In this study, we found that RvD1 inhibited the expression of c-Myc in normal colon cells stimulated with tumor necrosis factor-α (TNFα) and also in colon cancer cells. The suppression of TNFα-induced upregulation of c-Myc in normal cells was mediated through attenuation of NF-κB signaling. Notably, RvD1 destabilized the constitutively overexpressed c-Myc protein in HCT 116 human colon cancer cells by stimulating its ubiquitination and subsequent proteasomal degradation. Further, we revealed that RvD1 stimulated c-Myc degradation through direct interaction with the ALX/FPR2 receptor. This interaction resulted in inhibition of activation of extracellular signal-regulated kinase, thereby attenuating phosphorylation-dependent stabilization of c-Myc.
[Mh] Termos MeSH primário: Anti-Inflamatórios/farmacologia
Antineoplásicos/farmacologia
Neoplasias do Colo/prevenção & controle
Proteínas de Ligação a DNA/genética
Ácidos Docosa-Hexaenoicos/farmacologia
Regulação Neoplásica da Expressão Gênica
Fatores de Transcrição/genética
Fator de Necrose Tumoral alfa/antagonistas & inibidores
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Animais
Azoximetano
Carcinógenos
Neoplasias do Colo/induzido quimicamente
Neoplasias do Colo/genética
Neoplasias do Colo/patologia
Proteínas de Ligação a DNA/antagonistas & inibidores
Proteínas de Ligação a DNA/metabolismo
Células HCT116
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
NF-kappa B/genética
NF-kappa B/metabolismo
Fosforilação/efeitos dos fármacos
Complexo de Endopeptidases do Proteassoma/efeitos dos fármacos
Complexo de Endopeptidases do Proteassoma/metabolismo
Proteólise/efeitos dos fármacos
Receptores de Formil Peptídeo/genética
Receptores de Formil Peptídeo/metabolismo
Receptores de Lipoxinas/genética
Receptores de Lipoxinas/metabolismo
Transdução de Sinais
Fatores de Transcrição/antagonistas & inibidores
Fatores de Transcrição/metabolismo
Fator de Necrose Tumoral alfa/farmacologia
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Anti-Inflammatory Agents); 0 (Antineoplastic Agents); 0 (Carcinogens); 0 (DNA-Binding Proteins); 0 (FPR2 protein, human); 0 (HSH2D protein, human); 0 (MYCBP protein, human); 0 (NF-kappa B); 0 (Receptors, Formyl Peptide); 0 (Receptors, Lipoxin); 0 (Transcription Factors); 0 (Tumor Necrosis Factor-alpha); 0 (resolvin D1); 25167-62-8 (Docosahexaenoic Acids); EC 3.4.25.1 (Proteasome Endopeptidase Complex); MO0N1J0SEN (Azoxymethane)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180107
[St] Status:MEDLINE


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[PMID]:28934373
[Au] Autor:Winther M; Holdfeldt A; Sundqvist M; Rajabkhani Z; Gabl M; Bylund J; Dahlgren C; Forsman H
[Ad] Endereço:Department of Rheumatology and Inflammation Research, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
[Ti] Título:Formyl peptide derived lipopeptides disclose differences between the receptors in mouse and men and call the pepducin concept in question.
[So] Source:PLoS One;12(9):e0185132, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A pepducin is a lipopeptide containing a peptide sequence that is identical to one of the intracellular domains of the G-protein coupled receptor (GPCR) assumed to be the target. Neutrophils express two closely related formyl peptide receptors belonging to the family of GPCRs; FPR1 and FPR2 in human and their respective orthologue Fpr1 and Fpr2 in mouse. By applying the pepducin concept, we have earlier identified FPR2 activating pepducins generated from the third intracellular loop of FPR2. The third intracellular loop of FPR2 differs in two amino acids from that of FPR1, seven from Fpr2 and three from Fpr1. Despite this, we found that pepducins generated from FPR1, FPR2, Fpr1 and Fpr2 all targeted FPR2 in human neutrophils and Fpr2 in mouse, but with different modulating outcomes. Whereas the FPR1/Fpr1 derived pepducins inhibited the FPR2 function in human neutrophils, they activated Fpr2 in mouse. The FPR2 derived pepducin activated FPR2/Fpr2, whereas the pepducin generated from Fpr2 inhibited both FPR2 and Fpr2. In summary, our data demonstrate that pepducins generated from the third intracellular loop of human FPR1/2 and mouse Fpr1/2, all targeted FPR2 in human and Fpr2 in mouse. With respect to the modulating outcomes, pepducin inhibitors identified for FPR2 are in fact activators for Fpr2 in mouse neutrophils. Our data thus questions the validity of pepducin concept regarding their receptor selectivity but supports the notion that FPR2/Fpr2 may recognize a lipopeptide molecular pattern, and highlight the differences in ligand recognition profile between FPR2 and its mouse orthologue Fpr2.
[Mh] Termos MeSH primário: Lipopeptídeos/metabolismo
Receptores de Formil Peptídeo/metabolismo
Receptores de Lipoxinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Leucócitos/metabolismo
Lipopeptídeos/administração & dosagem
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Modelos Moleculares
NADPH Oxidases/metabolismo
Ligação Proteica
Receptores de Formil Peptídeo/genética
Especificidade da Espécie
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (FPR1 protein, human); 0 (FPR2 protein, human); 0 (Fpr1 protein, mouse); 0 (Lipopeptides); 0 (Receptors, Formyl Peptide); 0 (Receptors, Lipoxin); 0 (formyl peptide receptor 2, mouse); EC 1.6.3.- (NADPH Oxidases)
[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:170922
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185132


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[PMID]:28892824
[Au] Autor:Lippestad M; Hodges RR; Utheim TP; Serhan CN; Dartt DA
[Ad] Endereço:Schepens Eye Research Institute, Massachusetts Eye and Ear Infirmary, Department of Ophthalmology, Harvard Medical School, Boston, Massachusetts, United States.
[Ti] Título:Resolvin D1 Increases Mucin Secretion in Cultured Rat Conjunctival Goblet Cells via Multiple Signaling Pathways.
[So] Source:Invest Ophthalmol Vis Sci;58(11):4530-4544, 2017 Sep 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: Goblet cells in the conjunctiva secrete mucin into the tear film protecting the ocular surface. The proresolution mediator resolvin D1 (RvD1) regulates mucin secretion to maintain homeostasis during physiological conditions and in addition, actively terminates inflammation. We determined the signaling mechanisms used by RvD1 in cultured rat conjunctival goblet cells to increase intracellular [Ca2+] ([Ca2+]i) and induce glycoconjugate secretion. Methods: Increase in [Ca2+]i were measured using fura 2/AM and glycoconjugate secretion determined using an enzyme-linked lectin assay with the lectin Ulex Europaeus Agglutinin 1. Signaling pathways activated by RvD1 were studied after goblet cells were pretreated with signaling pathway inhibitors before stimulation with RvD1. The results were compared with results when goblet cells were stimulated with RvD1 alone and percent inhibition calculated. Results: The increase in [Ca2+]i stimulated by RvD1 was blocked by inhibitors to phospholipases (PL-) -D, -C, -A2, protein kinase C (PKC), extracellular signal-regulated kinases (ERK)1/2 and Ca2+/calmodulin-dependent kinase (Ca2+/CamK). Glycoconjugate secretion was significantly inhibited by PLD, -C, -A2, ERK1/2 and Ca2+/CamK, but not PKC. Conclusions: We conclude that RvD1 increases glycoconjugate secretion from goblet cells via multiple signaling pathways including PLC, PLD, and PLA2, as well as their signaling components ERK1/2 and Ca2+/CamK to preserve the mucous layer and maintain homeostasis by protecting the eye from desiccating stress, allergens, and pathogens.
[Mh] Termos MeSH primário: Túnica Conjuntiva/efeitos dos fármacos
Ácidos Docosa-Hexaenoicos/farmacologia
Células Caliciformes/efeitos dos fármacos
Mucinas/secreção
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Células Cultivadas
Túnica Conjuntiva/metabolismo
Ensaio de Imunoadsorção Enzimática
Fura-2/análogos & derivados
Fura-2/metabolismo
Células Caliciformes/metabolismo
Receptores de Inositol 1,4,5-Trifosfato/metabolismo
Sistema de Sinalização das MAP Quinases/fisiologia
Masculino
Fosfolipase D/metabolismo
Fosfolipases A2/metabolismo
Ratos
Ratos Sprague-Dawley
Receptores de Lipoxinas/metabolismo
Fosfolipases Tipo C/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Inositol 1,4,5-Trisphosphate Receptors); 0 (Mucins); 0 (Receptors, Lipoxin); 0 (lipoxin A(4) receptor, rat); 0 (resolvin D1); 105344-37-4 (fura-2-am); 25167-62-8 (Docosahexaenoic Acids); EC 3.1.1.4 (Phospholipases A2); EC 3.1.4.- (Type C Phospholipases); EC 3.1.4.4 (Phospholipase D); SY7Q814VUP (Calcium); TSN3DL106G (Fura-2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-21914


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[PMID]:28700225
[Au] Autor:Skovbakke SL; Holdfeldt A; Nielsen C; Hansen AM; Perez-Gassol I; Dahlgren C; Forsman H; Franzyk H
[Ad] Endereço:Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen , Jagtvej 162, 2100 Copenhagen East, Denmark.
[Ti] Título:Combining Elements from Two Antagonists of Formyl Peptide Receptor 2 Generates More Potent Peptidomimetic Antagonists.
[So] Source:J Med Chem;60(16):6991-6997, 2017 Aug 24.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Structural optimization of a peptidomimetic antagonist of formyl peptide receptor 2 (FPR2) was explored by an approach involving combination of elements from the two most potent FPR2 antagonists described: a Rhodamine B-conjugated 10-residue gelsonin-derived peptide (i.e., PBP , RhB-QRLFQVKGRR-OH) and the palmitoylated α-peptide/ß-peptoid hybrid Pam-(Lys-ßNspe) -NH . This generated an array of hybrid compounds from which a new subclass of receptor-selective antagonists was identified. The most potent representatives displayed activity in the low nanomolar range. The resulting stable and potent FPR2-selective antagonists (i.e., RhB-(Lys-ßNphe) -NH ; n = 4-6) are expected to become valuable tools in further elucidation of the physiological role of FPR2 in health and disease.
[Mh] Termos MeSH primário: Gelsolina/farmacologia
Fragmentos de Peptídeos/farmacologia
Peptídeos/farmacologia
Peptidomiméticos/farmacologia
Receptores de Formil Peptídeo/antagonistas & inibidores
Receptores de Lipoxinas/antagonistas & inibidores
[Mh] Termos MeSH secundário: Ativadores de Enzimas/farmacologia
Gelsolina/síntese química
Seres Humanos
Estrutura Molecular
N-Formilmetionina Leucil-Fenilalanina/farmacologia
NADPH Oxidases/metabolismo
Neutrófilos/metabolismo
Oligopeptídeos/farmacologia
Fragmentos de Peptídeos/síntese química
Peptídeos/síntese química
Peptídeos/química
Peptidomiméticos/síntese química
Peptidomiméticos/química
Transdução de Sinais/efeitos dos fármacos
Relação Estrutura-Atividade
Superóxidos/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Activators); 0 (FPR2 protein, human); 0 (Gelsolin); 0 (Oligopeptides); 0 (Pam-(Lys-beta-Nspe)6-NH2); 0 (Peptide Fragments); 0 (Peptides); 0 (Peptidomimetics); 0 (Receptors, Formyl Peptide); 0 (Receptors, Lipoxin); 0 (Trp-Lys-Tyr-Met-Val-Met); 0 (gelsolin (160-169)); 11062-77-4 (Superoxides); 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine); EC 1.6.3.- (NADPH Oxidases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.7b00489


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[PMID]:28442547
[Au] Autor:Chatterjee A; Komshian S; Sansbury BE; Wu B; Mottola G; Chen M; Spite M; Conte MS
[Ad] Endereço:Cardiovascular Research Institute, University of California San Francisco, San Francisco, California, USA.
[Ti] Título:Biosynthesis of proresolving lipid mediators by vascular cells and tissues.
[So] Source:FASEB J;31(8):3393-3402, 2017 Aug.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent evidence suggests that specialized proresolving lipid mediators (SPMs) generated from docosahexaenoic acid (DHA) can modulate the vascular injury response. However, cellular sources for these autacoids within the vessel wall remain unclear. Here, we investigated whether isolated vascular cells and tissues can produce SPMs and assessed expression and subcellular localization of the key SPM biosynthetic enzyme 5-lipoxygenase (LOX) in vascular cells. Intact human arteries incubated with DHA produced 17-hydroxy DHA (17-HDHA) and D-series resolvins, as assessed by liquid chromatography-tandem mass spectrometry. Addition of 17-HDHA to human arteries similarly increased resolvin production. Primary cultures of human saphenous vein endothelial cells (ECs) and vascular smooth muscle cells (VSMCs) converted 17-HDHA to SPMs, including resolvin D1 (RvD1) and other D-series resolvins and protectins. This was accompanied by a rapid translocation of 5-LOX from nucleus to cytoplasm in both ECs and VSMCs, potentially facilitating SPM biosynthesis. Conditioned medium from cells exposed to 17-HDHA inhibited monocyte adhesion to TNF-α-stimulated EC monolayers. These downstream effects were partially reversed by antibodies against the RvD1 receptors ALX/FPR2 and GPR32. These results suggest that autocrine and/or paracrine signaling locally generated SPMs in the vasculature may represent a novel homeostatic mechanism of relevance to vascular health and disease.-Chatterjee, A., Komshian, S., Sansbury, B. E., Wu, B., Mottola, G., Chen, M., Spite, M., Conte, M. S. Biosynthesis of proresolving lipid mediators by vascular cells and tissues.
[Mh] Termos MeSH primário: Ácidos Docosa-Hexaenoicos/farmacologia
Células Endoteliais/metabolismo
Metabolismo dos Lipídeos/fisiologia
Miócitos de Músculo Liso/metabolismo
[Mh] Termos MeSH secundário: Anticorpos
Araquidonato 5-Lipoxigenase/genética
Araquidonato 5-Lipoxigenase/metabolismo
Células Cultivadas
Citocinas/metabolismo
Ácidos Docosa-Hexaenoicos/genética
Ácidos Docosa-Hexaenoicos/metabolismo
Regulação da Expressão Gênica/fisiologia
Seres Humanos
Inflamação/metabolismo
Leucócitos/fisiologia
Estrutura Molecular
Transporte Proteico/fisiologia
Receptores de Formil Peptídeo/genética
Receptores de Formil Peptídeo/metabolismo
Receptores Acoplados a Proteínas-G/genética
Receptores Acoplados a Proteínas-G/metabolismo
Receptores de Lipoxinas/genética
Receptores de Lipoxinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Cytokines); 0 (FPR2 protein, human); 0 (GPR32 protein, human); 0 (Receptors, Formyl Peptide); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Lipoxin); 0 (resolvin D1); 25167-62-8 (Docosahexaenoic Acids); EC 1.13.11.34 (Arachidonate 5-Lipoxygenase); EC 1.3.11.34 (ALOX5 protein, human)
[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:170427
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201700082R


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[PMID]:28218740
[Au] Autor:Zhang JL; Zhuo XJ; Lin J; Luo LC; Ying WY; Xie X; Zhang HW; Yang JX; Li D; Gao Smith F; Jin SW
[Ad] Endereço:Department of Anesthesia and Critical Care, Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University, Zhejiang, China.
[Ti] Título:Maresin1 stimulates alveolar fluid clearance through the alveolar epithelial sodium channel Na,K-ATPase via the ALX/PI3K/Nedd4-2 pathway.
[So] Source:Lab Invest;97(5):543-554, 2017 May.
[Is] ISSN:1530-0307
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Maresin1 (MaR1) is a new docosahexaenoic acid-derived pro-resolving agent that promotes the resolution of inflammation. In this study, we sought to investigate the effect and underlining mechanisms of MaR1 in modulating alveolar fluid clearance (AFC) on LPS-induced acute lung injury. MaR1 was injected intravenously or administered by instillation (200 ng/kg) 8 h after LPS (14 mg/kg) administration and AFC was measured in live rats. In primary rat alveolar type II epithelial cells, MaR1 (100 nM) was added to the culture medium with lipopolysaccharide for 6 h. MaR1 markedly stimulated AFC in LPS-induced lung injury, with the outcome of decreased pulmonary edema and lung injury. In addition, rat lung tissue protein was isolated after intervention, and we found MaR1 improved epithelial sodium channel (ENaC), Na,K-adenosine triphosphatase (ATPase) protein expression and Na,K-ATPase activity. MaR1 down-regulated Nedd4-2 protein expression though PI3k/Akt but not though PI3k/SGK1 pathway in vivo. In primary rat alveolar type II epithelial cells stimulated with LPS, MaR1-upregulated ENaC and Na,K-ATPase protein abundance in the plasma membrane. Finally, the lipoxin A4 Receptor inhibitor (BOC-2) and PI3K inhibitor (LY294002) not only blocked MaR1's effects on cAMP/cGMP, the expression of phosphorylated Akt and Nedd4-2, but also inhibited the effect of MaR1 on AFC in vivo. In conclusion, MaR1 stimulates AFC through a mechanism partly dependent on alveolar epithelial ENaC and Na,K-ATPase activation via the ALX/PI3K/Nedd4-2 signaling pathway. Our findings reveal a novel mechanism for pulmonary edema fluid reabsorption and MaR1 may provide a new therapy for the resolution of ALI/ARDS.
[Mh] Termos MeSH primário: Lesão Pulmonar Aguda/metabolismo
Ácidos Docosa-Hexaenoicos/farmacologia
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Canais Epiteliais de Sódio/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Receptores de Lipoxinas/metabolismo
Transdução de Sinais/efeitos dos fármacos
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Animais
Lipopolissacarídeos
Pulmão/química
Pulmão/efeitos dos fármacos
Pulmão/metabolismo
Masculino
Ubiquitina-Proteína Ligases Nedd4
Alvéolos Pulmonares/metabolismo
Ratos
Ratos Sprague-Dawley
ATPase Trocadora de Sódio-Potássio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (7,14-dihydroxydocosa-4,8,10,12,16,19-hexaenoic acid); 0 (Endosomal Sorting Complexes Required for Transport); 0 (Epithelial Sodium Channels); 0 (Lipopolysaccharides); 0 (Receptors, Lipoxin); 0 (lipoxin A(4) receptor, rat); 25167-62-8 (Docosahexaenoic Acids); EC 2.3.2.26 (NEDD4L protein, rat); EC 2.3.2.26 (Nedd4 Ubiquitin Protein Ligases); EC 2.3.2.26 (Nedd4 protein, rat); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE
[do] DOI:10.1038/labinvest.2016.150


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[PMID]:28089662
[Au] Autor:Zhu XL; Chen X; Wang W; Li X; Huo J; Wang Y; Min YY; Su BX; Pei JM
[Ad] Endereço:Department of Physiology, Fourth Military Medical University, Xi'an 710032, China; Department of Anesthesiology, Xijing Hospital, Fourth Military Medical University, Xi'an 710032, China.
[Ti] Título:Electroacupuncture pretreatment attenuates spinal cord ischemia-reperfusion injury via inhibition of high-mobility group box 1 production in a LXA receptor-dependent manner.
[So] Source:Brain Res;1659:113-120, 2017 Mar 15.
[Is] ISSN:1872-6240
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Paraplegia caused by spinal cord ischemia is a severe complication following surgeries in the thoracic aneurysm. HMGB1 has been recognized as a key mediator in spinal inflammatory response after spinal cord injury. Electroacupuncture (EA) pretreatment could provide neuroprotection against cerebral ischemic injury through inhibition of HMGB1 release. Therefore, the present study aims to test the hypothesis that EA pretreatment protects against spinal cord ischemia-reperfusion (I/R) injury via inhibition of HMGB1 release. Animals were pre-treated with EA stimulations 30min daily for 4 successive days, followed by 20-min spinal cord ischemia induced by using a balloon catheter placed into the aorta. We found that spinal I/R significantly increased mRNA and cytosolic protein levels of HMGB1 after reperfusion in the spinal cord. The EA-pretreated animals displayed better motor performance after reperfusion along with the decrease of apoptosis, HMGB1, TNF-α and IL-1ß expressions in the spinal cord, whereas these effects by EA pretreatment was reversed by rHMGB1 administration. Furthermore, EA pretreatment attenuated the down-regulation of LXA receptor (ALX) expression induced by I/R injury, while the decrease of HMGB1 release in EA-pretreated rats was reversed by the combined BOC-2 (an inhibitor of LXA receptor) treatment. In conclusion, EA pretreatment may promote spinal I/R injury through the inhibition of HMGB1 release in a LXA receptor-dependent manner. Our data may represent a new therapeutic technique for treating spinal cord ischemia-reperfusion injury.
[Mh] Termos MeSH primário: Eletroacupuntura
Proteína HMGB1/metabolismo
Receptores de Lipoxinas/metabolismo
Traumatismo por Reperfusão/terapia
Isquemia do Cordão Espinal/terapia
Medula Espinal/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Apoptose/fisiologia
Modelos Animais de Doenças
Interleucina-1beta/metabolismo
Masculino
Neurotransmissores/farmacologia
Oligopeptídeos/farmacologia
RNA Mensageiro/metabolismo
Ratos Sprague-Dawley
Receptores de Lipoxinas/antagonistas & inibidores
Recuperação de Função Fisiológica/fisiologia
Traumatismo por Reperfusão/metabolismo
Traumatismo por Reperfusão/patologia
Medula Espinal/efeitos dos fármacos
Medula Espinal/patologia
Isquemia do Cordão Espinal/metabolismo
Isquemia do Cordão Espinal/patologia
Fatores de Tempo
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HMGB1 Protein); 0 (Hbp1 protein, rat); 0 (IL1B protein, rat); 0 (Interleukin-1beta); 0 (Neurotransmitter Agents); 0 (Oligopeptides); 0 (RNA, Messenger); 0 (Receptors, Lipoxin); 0 (Tumor Necrosis Factor-alpha); 66556-73-8 (butyloxycarbonyl-phenylalanyl-leucyl-phenylalanyl-leucyl-phenylalanine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE


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[PMID]:28060522
[Au] Autor:Abd-Elghafour BA; El-Sayed NM; Ahmed AA; Zaitone SA; Moustafa YM
[Ad] Endereço:a Ismailia General Hospital, Ismailia, Egypt.
[Ti] Título:Aspirin and (or) omega-3 polyunsaturated fatty acids protect against corticohippocampal neurodegeneration and downregulate lipoxin A production and formyl peptide receptor-like 1 expression in pentylenetetrazole-kindled rats.
[So] Source:Can J Physiol Pharmacol;95(4):340-348, 2017 Apr.
[Is] ISSN:1205-7541
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:There is evidence for a relationship between inflammation and seizures because epilepsy can be caused by or result in inflammation. This study aimed to investigate the effect of aspirin and (or) omega-3 polyunsaturated fatty acids (PUFAs) on seizure activity and neurodegeneration in pentylenetetrazole (PTZ)-kindled rats focusing on their effect on corticohippocampal production of lipoxin A (LXA ) and expression of formyl peptide receptor-like 1 (FPRL1) receptors. Male rats were injected with PTZ (35 mg/kg, i.p.) 3 times per week for a total of 15 doses. Rats were treated daily with aspirin (20 mg/kg, i.p.), omega-3 PUFAs (85 mg/kg, p.o.), or a combination of them for 35 days. Both LXA level and expression of FPRL1 receptor in the cortices and hippocampi of rats' brains were greater in PTZ-kindled rats compared to a saline control group. Cotreatment with aspirin and (or) omega-3 PUFAs reduced convulsive behaviour; reduced levels of LXA , interleukin-1ß, and nuclear factor-κB; and showed a lower percentage of corticohippocampal degenerative cells compared to PTZ-kindled rats. The combination of the 2 therapeutic agents did not provide significant improvement in comparison with the monotherapies. These findings suggest the use of aspirin or omega-3 PUFAs may delay the development of seizures and provide neuroprotection in a clinical setting.
[Mh] Termos MeSH primário: Aspirina/uso terapêutico
Epilepsia/prevenção & controle
Ácidos Graxos Ômega-3/uso terapêutico
Lipoxinas/metabolismo
Degeneração Neural/prevenção & controle
Fármacos Neuroprotetores/uso terapêutico
Receptores de Lipoxinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Córtex Cerebral/efeitos dos fármacos
Córtex Cerebral/metabolismo
Córtex Cerebral/patologia
Modelos Animais de Doenças
Regulação para Baixo
Quimioterapia Combinada
Epilepsia/induzido quimicamente
Epilepsia/tratamento farmacológico
Hipocampo/efeitos dos fármacos
Hipocampo/metabolismo
Hipocampo/patologia
Interleucina-1beta/metabolismo
Masculino
NF-kappa B/metabolismo
Pentilenotetrazol/toxicidade
Ratos
Receptores de Formil Peptídeo/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids, Omega-3); 0 (Interleukin-1beta); 0 (Lipoxins); 0 (NF-kappa B); 0 (Neuroprotective Agents); 0 (Receptors, Formyl Peptide); 0 (Receptors, Lipoxin); 0 (lipoxin A(4) receptor, rat); 0 (lipoxin A4); R16CO5Y76E (Aspirin); WM5Z385K7T (Pentylenetetrazole)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE
[do] DOI:10.1139/cjpp-2016-0060


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[PMID]:27860453
[Au] Autor:Huang J; Burston JJ; Li L; Ashraf S; Mapp PI; Bennett AJ; Ravipati S; Pousinis P; Barrett DA; Scammell BE; Chapman V
[Ad] Endereço:University of Nottingham, Nottingham, UK.
[Ti] Título:Targeting the D Series Resolvin Receptor System for the Treatment of Osteoarthritis Pain.
[So] Source:Arthritis Rheumatol;69(5):996-1008, 2017 May.
[Is] ISSN:2326-5205
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Pain is a major symptom of osteoarthritis (OA); currently available analgesics either do not provide adequate pain relief or are associated with serious side effects. The aim of this study was to investigate the therapeutic potential of targeting the resolvin receptor system to modify OA pain and pathology. METHODS: Gene expression of 2 resolvin receptors (ALX and ChemR23) was quantified in synovium and medial tibial plateau specimens obtained from patients with OA at the time of joint replacement surgery. Two models of OA joint pain were used for the mechanistic studies. Gene expression in the joint and central nervous system was quantified. The effects of exogenous administration of the D series resolvin precursor 17(R)-hydroxy-docosahexaenoic acid (17[R]-HDoHE) on pain behavior, joint pathology, spinal microglia, and astroglyosis were quantified. Plasma levels of relevant lipids, resolvin D2, 17(R)-HDoHE, and arachidonic acid, were determined in rats, using liquid chromatography tandem mass spectrometry. RESULTS: There was a positive correlation between resolvin receptor and interleukin-6 (IL-6) expression in human OA synovial and medial tibial plateau tissue. In rats, synovial expression of ALX was positively correlated with expression of IL-1ß, tumor necrosis factor, and cyclooxygenase 2. Treatment with 17(R)-HDoHE reversed established pain behavior (but not joint pathology) in 2 models of OA pain. This was associated with a significant elevation in the plasma levels of resolvin D2 and a significant reduction in astrogliosis in the spinal cord in the monosodium iodoacetate-induced OA rat model. CONCLUSION: Our preclinical data demonstrate the robust analgesic effects of activation of the D series resolvin pathways in 2 different animal models of OA. Our data support a predominant central mechanism of action in clinically relevant models of OA pain.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Comportamento Animal/efeitos dos fármacos
Ácidos Docosa-Hexaenoicos/farmacologia
Osteoartrite do Joelho/genética
Receptores de Quimiocinas/genética
[Mh] Termos MeSH secundário: Animais
Artralgia/induzido quimicamente
Cartilagem Articular/patologia
Modelos Animais de Doenças
Inibidores Enzimáticos/toxicidade
Expressão Gênica
Seres Humanos
Ácido Iodoacético/toxicidade
Meniscos Tibiais/cirurgia
Neuroglia/citologia
Neuroglia/metabolismo
Osteoartrite do Joelho/metabolismo
Osteoartrite do Joelho/patologia
RNA Mensageiro/metabolismo
Ratos
Reação em Cadeia da Polimerase em Tempo Real
Receptores de Quimiocinas/efeitos dos fármacos
Receptores de Lipoxinas/efeitos dos fármacos
Receptores de Lipoxinas/genética
Medula Espinal/citologia
Medula Espinal/metabolismo
Membrana Sinovial/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (CMKLR1 protein, human); 0 (Cmklr1 protein, rat); 0 (Enzyme Inhibitors); 0 (HSH2D protein, human); 0 (RNA, Messenger); 0 (Receptors, Chemokine); 0 (Receptors, Lipoxin); 0 (lipoxin A(4) receptor, rat); 25167-62-8 (Docosahexaenoic Acids); 90780-52-2 (17-hydroxy-4,7,10,13,15,19-docosahexaenoic acid); WF5188V710 (Iodoacetic Acid)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1002/art.40001


  10 / 379 MEDLINE  
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[PMID]:27633771
[Au] Autor:Park JC; Baik SH; Han SH; Cho HJ; Choi H; Kim HJ; Choi H; Lee W; Kim DK; Mook-Jung I
[Ad] Endereço:Department of Biochemistry and Biomedical Sciences, College of Medicine, Seoul National University, Seoul, 110-799, Korea.
[Ti] Título:Annexin A1 restores Aß -induced blood-brain barrier disruption through the inhibition of RhoA-ROCK signaling pathway.
[So] Source:Aging Cell;16(1):149-161, 2017 Feb.
[Is] ISSN:1474-9726
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The blood-brain barrier (BBB) is composed of brain capillary endothelial cells and has an important role in maintaining homeostasis of the brain separating the blood from the parenchyma of the central nervous system (CNS). It is widely known that disruption of the BBB occurs in various neurodegenerative diseases, including Alzheimer's disease (AD). Annexin A1 (ANXA1), an anti-inflammatory messenger, is expressed in brain endothelial cells and regulates the BBB integrity. However, its role and mechanism for protecting BBB in AD have not been identified. We found that ß-Amyloid 1-42 (Aß42)-induced BBB disruption was rescued by human recombinant ANXA1 (hrANXA1) in the murine brain endothelial cell line bEnd.3. Also, ANXA1 was decreased in the bEnd.3 cells, the capillaries of 5XFAD mice, and the human serum of patients with AD. To find out the mechanism by which ANXA1 recovers the BBB integrity in AD, the RhoA-ROCK signaling pathway was examined in both Aß42-treated bEnd.3 cells and the capillaries of 5XFAD mice as RhoA was activated in both cases. RhoA inhibitors alleviated Aß42-induced BBB disruption and constitutively overexpressed RhoA-GTP (active form of RhoA) attenuated the protective effect of ANXA1. When pericytes were cocultured with bEnd.3 cells, Aß42-induced RhoA activation of bEnd.3 cells was inhibited by the secretion of ANXA1 from pericytes. Taken together, our results suggest that ANXA1 restores Aß42-induced BBB disruption through inhibition of RhoA-ROCK signaling pathway and we propose ANXA1 as a therapeutic reagent, protecting against the breakdown of the BBB in AD.
[Mh] Termos MeSH primário: Peptídeos beta-Amiloides/toxicidade
Anexina A1/metabolismo
Barreira Hematoencefálica/patologia
Fragmentos de Peptídeos/toxicidade
Transdução de Sinais/efeitos dos fármacos
Quinases Associadas a rho/antagonistas & inibidores
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Idoso
Doença de Alzheimer/sangue
Doença de Alzheimer/patologia
Animais
Anexina A1/sangue
Barreira Hematoencefálica/efeitos dos fármacos
Barreira Hematoencefálica/metabolismo
Capilares/efeitos dos fármacos
Capilares/metabolismo
Feminino
Seres Humanos
Masculino
Camundongos Transgênicos
Pericitos/efeitos dos fármacos
Pericitos/metabolismo
Receptores de Formil Peptídeo/sangue
Receptores de Lipoxinas/sangue
Proteínas Recombinantes/farmacologia
Junções Íntimas/efeitos dos fármacos
Junções Íntimas/metabolismo
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Peptides); 0 (Annexin A1); 0 (FPR2 protein, human); 0 (Peptide Fragments); 0 (Receptors, Formyl Peptide); 0 (Receptors, Lipoxin); 0 (Recombinant Proteins); 0 (amyloid beta-protein (1-42)); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160917
[St] Status:MEDLINE
[do] DOI:10.1111/acel.12530



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