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[PMID]:28671974
[Au] Autor:Tan TL; Goh YY
[Ad] Endereço:Department of Emergency Medicine, Faculty of Medicine, Universiti Kebangsaan Malaysia, Kuala Lumpur, Malaysia.
[Ti] Título:The role of group IIA secretory phospholipase A2 (sPLA2-IIA) as a biomarker for the diagnosis of sepsis and bacterial infection in adults-A systematic review.
[So] Source:PLoS One;12(7):e0180554, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: This paper investigates the role of Group II Secretory Phospholipase A2 (sPLA2-IIA) as a biomarker for the diagnosis of sepsis and bacterial infection in adults. Sepsis and bacterial infection are common problems encountered by patients in the hospital and often carry adverse outcomes if not managed early. METHODS: Two independent reviewers conducted a comprehensive search using Ovid MEDLINE published from years 1993 to 2016 and SCOPUS published from year 1985 to 2017 to screen for relevant studies. The main inclusion criteria included adult subjects, patients with suspected or confirmed signs of infection and relevant outcomes which looked into the role of sPLA2-IIA in detecting the presence of sepsis and bacterial infection in the subjects. RESULTS AND DISCUSSION: Four studies met the inclusion criteria. SPLA2-IIA was found to be effective in detecting the presence of sepsis and bacterial infection in adults. The levels of serum sPLA2-IIA also correlated well with the presence of sepsis and bacterial infection. CONCLUSION: This systematic review highlights the role of sPLA2-IIA as a reliable tool to diagnose sepsis and bacterial infection in adult patients. Nonetheless, further studies should be done in the future to provide more compelling evidence on its application in the clinical setting.
[Mh] Termos MeSH primário: Infecções Bacterianas/diagnóstico
Biomarcadores/sangue
Fosfolipases A2 do Grupo II/sangue
Sepse/diagnóstico
[Mh] Termos MeSH secundário: Infecções Bacterianas/enzimologia
Seres Humanos
Sepse/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biomarkers); EC 3.1.1.4 (Group II Phospholipases A2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180554


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[PMID]:28554871
[Au] Autor:Lokeshwari DM; Rekha ND; Srinivasan B; Vivek HK; Kariyappa AK
[Ad] Endereço:Department of Chemistry, Yuvaraja College, University of Mysore, Mysuru, India.
[Ti] Título:Design, synthesis of novel furan appended benzothiazepine derivatives and in vitro biological evaluation as potent VRV-PL-8a and H /K ATPase inhibitors.
[So] Source:Bioorg Med Chem Lett;27(14):3048-3054, 2017 07 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A series of new of furan derivatised [1,4] benzothiazepine analogues were synthesized starting from 1-(furan-2-yl)ethanone. 1-(Furan-2-yl)ethanone was converted into chalcones by its reaction with various aromatic aldehydes, then were reacted with 2-aminobenzenethiol in acidic conditions to obtain the title compounds in good yields. The synthesized new compounds were characterized by H NMR, C NMR, Mass spectral studies and elemental analyses. All the new compounds were evaluated for their in vitro VRV-PL-8a and H /K ATPase inhibitor properties. Preliminary studies revealed that, some molecules amongst the designed series showed promising VRV-PL-8a and H /K ATPase inhibitor properties. Further, rigid body docking studies were performed to understand possible docking sites of the molecules on the target proteins and the mode of binding. This finding presents a promising series of lead molecules that can serve as prototypes for the treatment of inflammatory related disorder that can mitigate the ulcer inducing side effect shown by other NSAIDs.
[Mh] Termos MeSH primário: Desenho de Drogas
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/farmacologia
Fosfolipases A2 do Grupo II/antagonistas & inibidores
ATPase Trocadora de Hidrogênio-Potássio/química
Tiazepinas/síntese química
Tiazepinas/farmacologia
[Mh] Termos MeSH secundário: Anti-Inflamatórios não Esteroides/síntese química
Anti-Inflamatórios não Esteroides/química
Anti-Inflamatórios não Esteroides/metabolismo
Anti-Inflamatórios não Esteroides/farmacologia
Sítios de Ligação
Chalconas/química
Ativação Enzimática/efeitos dos fármacos
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Furanos/química
Fosfolipases A2 do Grupo II/metabolismo
ATPase Trocadora de Hidrogênio-Potássio/metabolismo
Concentração Inibidora 50
Espectroscopia de Ressonância Magnética
Conformação Molecular
Simulação de Acoplamento Molecular
Estrutura Terciária de Proteína
Inibidores da Bomba de Prótons/síntese química
Inibidores da Bomba de Prótons/química
Inibidores da Bomba de Prótons/metabolismo
Inibidores da Bomba de Prótons/farmacologia
Tiazepinas/química
Tiazepinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Chalcones); 0 (Enzyme Inhibitors); 0 (Furans); 0 (Proton Pump Inhibitors); 0 (Thiazepines); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.4 (VRV-PL-VIIIa phospholipase A2, Vipera russelli); EC 3.6.3.10 (H(+)-K(+)-Exchanging ATPase); UC0XV6A8N9 (furan)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE


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[PMID]:28077172
[Au] Autor:Zhu C; Song H; Shen B; Wu L; Liu F; Liu X
[Ad] Endereço:Department of Clinical Laboratory, Renmin Hospital of Wuhan University, Wuhan, Hubei, 430060, People's Republic of China.
[Ti] Título:Promoting effect of hepatitis B virus on the expressoin of phospholipase A2 group IIA.
[So] Source:Lipids Health Dis;16(1):5, 2017 Jan 11.
[Is] ISSN:1476-511X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hepatitis B virus (HBV) infection causes acute and chronic liver disease, ultimately leading to the development of liver cirrhosis (LC) and hepatocellular carcinoma (HCC). Phospholipase A2 group IIA (PLA2G2A) plays important roles in the development and progression of many tumors. Thus far, there have been no reports on the association between HBV and PLA2G2A. The present study investigated the effect of HBV infection on PLA2G2A expression and its application in the diagnosis of HBV-related diseases. METHODS: Serum levels of PLA2G2A in 308 HBV-infected patients and 185 healthy controls were measured using an enzyme-linked immunosorbent assay (ELISA). The difference in serum levels of PLA2G2A was analyzed among chronic hepatitis B (CHB), LC, and HCC patients. PLA2G2A mRNA and protein expression in HepG2 and HepG2.2.15 cells carrying the integrated HBV genome were measured using reverse transcription polymerase chain reaction (RT-PCR) and western blot assays. The HBV infectious clone pHBV1.3, the control plasmid pBlue-ks and PLA2G2A gene promoter were transfected into HepG2 and HepG2.2.15 cells. After transfection, the luciferase activity was measured in the cells. PLA2G2A mRNA and protein expression levels were examined using RT-PCR and western blot assays. RESULTS: The serum levels of PLA2G2A were 258.3 ± 20.3ng/dl in the healthy controls and 329.0 ± 22.5ng/dl, 385.4 ± 29.3ng/dl and 459.2 ± 38.6ng/dl in the CHB, LC, and HCC patients, respectively. Statistical analyses revealed significantly higher serum levels of PLA2G2A in CHB, LC, and HCC patients than in the healthy controls (P < 0.05), and PLA2G2A levels were elevated in the order of HCC > LC > CHB group. High serum PLA2G2A levels in HCC patients were associated with a lower prevalence of lymph node metastasis and a lower TNM stage. HepG2.2.15 cells carrying the HBV genome expressed higher levels of PLA2G2A mRNA and protein than the HepG2 cells. In addition, HBV triggered PLA2G2A promoter activity and enhanced PLA2G2A mRNA and protein expression compared to the empty vector pBlue-ks. CONCLUSION: HBV can upregulate the expression of PLA2G2A, and serum levels of PLA2G2A are associated with the progression of HBV-related diseases.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/genética
Fosfolipases A2 do Grupo II/genética
Vírus da Hepatite B/patogenicidade
Hepatite B Crônica/genética
Interações Hospedeiro-Patógeno
Cirrose Hepática/genética
Neoplasias Hepáticas/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Carcinoma Hepatocelular/etiologia
Carcinoma Hepatocelular/patologia
Carcinoma Hepatocelular/virologia
Estudos de Casos e Controles
Feminino
Expressão Gênica
Genes Reporter
Fosfolipases A2 do Grupo II/sangue
Células Hep G2
Vírus da Hepatite B/crescimento & desenvolvimento
Hepatite B Crônica/complicações
Hepatite B Crônica/patologia
Hepatite B Crônica/virologia
Seres Humanos
Cirrose Hepática/etiologia
Cirrose Hepática/patologia
Cirrose Hepática/virologia
Neoplasias Hepáticas/etiologia
Neoplasias Hepáticas/patologia
Neoplasias Hepáticas/virologia
Luciferases/genética
Luciferases/metabolismo
Metástase Linfática
Masculino
Meia-Idade
Estadiamento de Neoplasias
Plasmídeos/química
Plasmídeos/metabolismo
Regiões Promotoras Genéticas
RNA Mensageiro/sangue
RNA Mensageiro/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); EC 1.13.12.- (Luciferases); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (PLA2G2A protein, human)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1186/s12944-016-0400-7


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[PMID]:28056488
[Au] Autor:Kim RR; Malde AK; Nematollahi A; Scott KF; Church WB
[Ad] Endereço:Group in Biomolecular Structure and Informatics, Faculty of Pharmacy, The University of Sydney, Sydney, NSW, 2006, Australia.
[Ti] Título:Molecular dynamics simulations reveal structural insights into inhibitor binding modes and functionality in human Group IIA phospholipase A .
[So] Source:Proteins;85(5):827-842, 2017 May.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human Group IIA phospholipase A (hGIIA) promotes inflammation in immune-mediated pathologies by regulating the arachidonic acid pathway through both catalysis-dependent and -independent mechanisms. The hGIIA crystal structure, both alone and inhibitor-bound, together with structures of closely related snake-venom-derived secreted phospholipase enzymes has been well described. However, differentiation of biological and nonbiological contacts and the relevance of structures determined from snake venom enzymes to human enzymes are not clear. We employed molecular dynamics (MD) and docking approaches to understand the binding of inhibitors that selectively or nonselectively block the catalysis-independent mechanism of hGIIA. Our results indicate that hGIIA behaves as a monomer in the solution environment rather than a dimer arrangement that is in the asymmetric unit of some crystal structures. The binding mode of a nonselective inhibitor, KH064, was validated by a combination of the experimental electron density and MD simulations. The binding mode of the selective pentapeptide inhibitor FLSYK to hGIIA was stipulated to be different to that of the snake venom phospholipases A of Daboia russelli pulchella (svPLA ). Our data suggest that the application of MD approaches to crystal structure data is beneficial in evaluating the robustness of conclusions drawn based on crystal structure data alone. Proteins 2017; 85:827-842. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Elétrons
Fosfolipases A2 do Grupo II/antagonistas & inibidores
Simulação de Dinâmica Molecular
Oligopeptídeos/química
Ácidos Pentanoicos/química
Inibidores de Fosfolipase A2/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Sítios de Ligação
Fosfolipases A2 do Grupo II/química
Seres Humanos
Simulação de Acoplamento Molecular
Fosfolipases A2/química
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Venenos de Víboras/química
Viperidae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5-(4-benzyloxyphenyl)-4S-(7-phenylheptanoylamino)pentanoic acid); 0 (Oligopeptides); 0 (Pentanoic Acids); 0 (Phospholipase A2 Inhibitors); 0 (Viper Venoms); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (PLA2G2A protein, human); EC 3.1.1.4 (Phospholipases A2)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170106
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25235


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[PMID]:28034717
[Au] Autor:Salvador GH; Dos Santos JI; Lomonte B; Fontes MR
[Ad] Endereço:Departamento de Física e Biofísica, Instituto de Biociências, UNESP - Univ. Estadual Paulista, Botucatu, SP, Brazil.
[Ti] Título:Crystal structure of a phospholipase A from Bothrops asper venom: Insights into a new putative "myotoxic cluster".
[So] Source:Biochimie;133:95-102, 2017 Feb.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Snake venoms from the Viperidae and Elapidae families often have several phospholipases A (PLA s), which may display different functions despite having a similar structural scaffold. These proteins are considered an important target for the development of drugs against local myotoxic damage because they are not efficiently neutralized by conventional serum therapy. PLA s from these venoms are generally divided into two classes: (i) catalytic PLA s (or Asp49-PLA s) and (ii) non-catalytic PLA -like toxins (or Lys49-PLA s). In many Viperidae venoms, a subset of the basic Asp49-PLA s displays some functional and structural characteristics of PLA -like proteins and group within the same phylogenetic clade, but their myotoxic mechanism is still largely unknown. In the present study, we have crystallized and solved the structure of myotoxin I (MT-I), a basic myotoxic Asp49-PLA isolated from Bothrops asper venom. The structure presents a dimeric conformation that is compatible with that of previous dimers found for basic myotoxic Asp49-PLA s and Lys49-PLA s and has been confirmed by other biophysical and bioinformatics techniques. This arrangement suggests a possible cooperative action between both monomers to exert myotoxicity via two different sites forming a putative membrane-docking site (MDoS) and a putative membrane disruption site (MDiS). This mechanism would resemble that proposed for Lys49-PLA s, but the sites involved appear to be situated in a different region. Thus, as both sites are close to one another, they form a "myotoxic cluster", which is also found in two other basic myotoxic Asp49-PLA s from Viperidae venoms. Such arrangement may represent a novel structural strategy for the mechanism of muscle damage exerted by the group of basic, Asp49-PLA s found in viperid snake venoms.
[Mh] Termos MeSH primário: Venenos de Crotalídeos/enzimologia
Fosfolipases A2 do Grupo II/química
Fosfolipases A2/química
Proteínas de Répteis/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Animais
Bothrops
Venenos de Crotalídeos/química
Venenos de Crotalídeos/toxicidade
Cristalografia por Raios X
Fosfolipases A2 do Grupo II/genética
Fosfolipases A2 do Grupo II/metabolismo
Fosfolipases A2 do Grupo II/toxicidade
Seres Humanos
Músculo Esquelético/química
Músculo Esquelético/efeitos dos fármacos
Fosfolipases A2/genética
Fosfolipases A2/toxicidade
Filogenia
Proteínas de Répteis/genética
Proteínas de Répteis/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crotalid Venoms); 0 (Reptilian Proteins); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (Phospholipases A2); EC 3.1.1.4 (myotoxin I)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161231
[St] Status:MEDLINE


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[PMID]:27928710
[Au] Autor:Kameshwar VH; R KJ; Priya BS; Swamy SN
[Ad] Endereço:Department of Biotechnology, JSS Science and Technology University, Mysuru, 570006, India.
[Ti] Título:Synthesis, characterization and bioactivity studies of novel 1,3,4-oxadiazole small molecule that targets basic phospholipase A from Vipera russelli.
[So] Source:Mol Cell Biochem;426(1-2):161-175, 2017 Feb.
[Is] ISSN:1573-4919
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Secretory phospholipase A (sPLA ) is a key enzyme participating in the inflammatory cascade followed by the action of cyclooxygenase-2 and lipoxygenases. Therefore, inhibitors of sPLA could be used as potent anti-inflammatory agents to treat the early phase of inflammation. In this study, we have prepared the fenoprofen and ibuprofen analogs containing 1,3,4-oxadiazole nucleus and tested against Vipera russelli venom's basic sPLA (VRV-PL-VIIIa). Among the tested ligands 5(a-t),2-(2-chlorophenyl)-5-(1-(4-phenoxyphenyl) ethyl)-1,3,4-oxadiazole (5m) inhibited the catalytic activity of VRV-PL-VIIIa with an IC value of 11.52 µM. Biophysical studies revealed that the 5m quenches the intrinsic fluorescence of VRV-PL-VIIIa, in a concentration dependent manner. Also, the compound 5m affected VRV-PL-VIIIa conformation, which was observed by circular dichroism spectra that recorded the prominent shift in the α-helix peak and the random coil formation of VRV-PL-VIIIa. Further, molecular docking analysis revealed that the compound 5m possess strong hydrophobic interactions at catalytic triad region of the VRV-PL-VIIIa. Evident to in vitro and in silico studies, 5m strongly inhibited the hemolysis of red blood cells. Our in vivo pharmacological studies revealed that the compound 5m inhibited the edematogenic activity of VRV-PL-VIIIa in mouse foot pad. Additionally, the 5m inhibited VRV-PL-VIIIa-induced myotoxicity and lung hemorrhage in mice. Overall, our ADMET results depicted that 5m possess better druggable property. Thus, this study explored the new fenoprofen and ibuprofen analog 5m as the lead-structure that serves as an anti-inflammatory agent.
[Mh] Termos MeSH primário: Inibidores Enzimáticos
Fenoprofeno
Fosfolipases A2 do Grupo II
Ibuprofeno
Oxidiazóis
[Mh] Termos MeSH secundário: Animais
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Fenoprofeno/análogos & derivados
Fenoprofeno/síntese química
Fenoprofeno/química
Fenoprofeno/farmacologia
Fosfolipases A2 do Grupo II/antagonistas & inibidores
Fosfolipases A2 do Grupo II/química
Fosfolipases A2 do Grupo II/toxicidade
Hemólise/efeitos dos fármacos
Ibuprofeno/análogos & derivados
Ibuprofeno/síntese química
Ibuprofeno/química
Ibuprofeno/farmacologia
Masculino
Camundongos
Simulação de Acoplamento Molecular
Oxidiazóis/síntese química
Oxidiazóis/química
Oxidiazóis/farmacologia
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Oxadiazoles); 20O2F20OUR (1,3,4-oxadiazole); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.4 (VRV-PL-VIIIa phospholipase A2, Vipera russelli); RA33EAC7KY (Fenoprofen); WK2XYI10QM (Ibuprofen)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161209
[St] Status:MEDLINE
[do] DOI:10.1007/s11010-016-2888-6


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[PMID]:27864802
[Au] Autor:Takada Y; Fujita M
[Ad] Endereço:Department of Dermatology, Biochemistry and Molecular Medicine, UC Davis School of Medicine, Research III Suite 3300, 4645 Second Avenue, Sacramento, CA, 95817, USA. ytakada@ucdavis.edu.
[Ti] Título:Secreted Phospholipase A2 Type IIA (sPLA2-IIA) Activates Integrins in an Allosteric Manner.
[So] Source:Adv Exp Med Biol;925:103-115, 2017.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secreted phospholipase A2 type IIA (sPLA2-IIA) is a well-established pro-inflammatory protein and has been a major target for drug discovery. However, the mechanism of its signaling action has not been fully understood. We previously found that sPLA2-IIA binds to integrins αvß3 and α4ß1 in human and that this interaction plays a role in sPLA2-IIA's signaling action. Our recent studies found that sPLA2-IIA activates integrins in an allosteric manner through direct binding to a newly identified binding site of integrins (site 2), which is distinct from the classical RGD-binding site (site 1). The sPLA2-IIA-induced integrin activation may be related to the signaling action of sPLA2-IIA. Since sPLA2-IIA is present in normal human tears in addition to rheumatoid synovial fluid at high concentrations the sPLA2-IIA-mediated integrin activation on leukocytes may be involved in immune responses in normal and pathological conditions.
[Mh] Termos MeSH primário: Fosfolipases A2 do Grupo II/química
Integrina alfa4beta1/química
Integrina alfaVbeta3/química
Transdução de Sinais/imunologia
[Mh] Termos MeSH secundário: Regulação Alostérica
Artrite Reumatoide/genética
Artrite Reumatoide/imunologia
Artrite Reumatoide/patologia
Sítios de Ligação
Regulação da Expressão Gênica
Fosfolipases A2 do Grupo II/genética
Fosfolipases A2 do Grupo II/imunologia
Seres Humanos
Integrina alfa4beta1/genética
Integrina alfa4beta1/imunologia
Integrina alfaVbeta3/genética
Integrina alfaVbeta3/imunologia
Simulação de Acoplamento Molecular
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Líquido Sinovial/química
Líquido Sinovial/imunologia
Lágrimas/química
Lágrimas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Integrin alpha4beta1); 0 (Integrin alphaVbeta3); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (PLA2G2A protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161120
[St] Status:MEDLINE
[do] DOI:10.1007/5584_2016_95


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[PMID]:27590117
[Au] Autor:Collaço RC; Randazzo-Moura P; Tamascia ML; da Silva IR; Rocha T; Cogo JC; Hyslop S; Sanny CG; Rodrigues-Simioni L
[Ad] Endereço:Departamento de Farmacologia, Faculdade de Ciências Médicas, Universidade Estadual de Campinas (UNICAMP), Rua Tessália Vieira de Camargo, 126, 13083-887, Campinas, SP, Brazil.
[Ti] Título:Bothrops fonsecai snake venom activities and cross-reactivity with commercial bothropic venom.
[So] Source:Comp Biochem Physiol C Toxicol Pharmacol;191:86-100, 2017 Jan.
[Is] ISSN:1532-0456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work, we examined some biochemical and biological activities of Bothrops fonsecai venom, a pitviper endemic to southeastern Brazil, and assessed their neutralization by commercial bothropic antivenom (CAv). Cross-reactivity of venom with CAv was also assessed by immunoblotting and size-exclusion high performance chromatography (SE-HPLC). Bothrops fonsecai venom had PLA , proteolytic and esterase activities that were neutralized to varying extents by venom:antivenom ratios of 5:1 and 5:2 (PLA and esterase activities) or not significantly by either venom:antivenom ratio (proteolytic activity). The minimum hemorrhagic dose (69.2µg) was totally neutralized by both ratios. Clotting time in rat citrated plasma was 33±10.5s (mean±SD; n=5) and was completely neutralized by a 5:2 ratio. Edema formation was dose-dependent (1-30µg/site) and significantly inhibited by both ratios. Venom (10-300µg/mL) caused neuromuscular blockade in extensor digitorum longus preparations; this blockade was inhibited best by a 5:2 ratio. Venom caused myonecrosis and creatine kinase release in vivo (gastrocnemius muscle) and in vitro (extensor digitorum longus) that was effectively neutralized by both venom:antivenom ratios. Immunoblotting showed that venom components of ~25-100kDa interacted with CAv. SE-HPLC profiles for venom incubated with CAv or specific anti-B. fonsecai antivenom raised in rabbits (SAv) indicated that CAv had a higher binding capacity than SAv, whereas SAv had higher affinity than CAv. These findings indicate that B. fonsecai venom contains various activities that are neutralized to different extents by CAv and suggest that CAv could be used to treat envenoming by B. fonsecai.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/imunologia
Antídotos
Antivenenos/imunologia
Bothrops/imunologia
Venenos de Crotalídeos/imunologia
Proteínas de Répteis/imunologia
Mordeduras de Serpentes/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/farmacologia
Antídotos/farmacologia
Antivenenos/farmacologia
Coagulação Sanguínea/efeitos dos fármacos
Western Blotting
Bothrops/metabolismo
Cromatografia em Gel
Cromatografia Líquida de Alta Pressão
Reações Cruzadas
Venenos de Crotalídeos/enzimologia
Venenos de Crotalídeos/toxicidade
Relação Dose-Resposta a Droga
Edema/induzido quimicamente
Edema/prevenção & controle
Eletroforese em Gel Bidimensional
Esterases/imunologia
Esterases/metabolismo
Fosfolipases A2 do Grupo II/imunologia
Fosfolipases A2 do Grupo II/metabolismo
Hemorragia/sangue
Hemorragia/induzido quimicamente
Hemorragia/prevenção & controle
Masculino
Camundongos
Junção Neuromuscular/efeitos dos fármacos
Peptídeo Hidrolases/imunologia
Peptídeo Hidrolases/metabolismo
Proteólise
Ratos Wistar
Proteínas de Répteis/metabolismo
Proteínas de Répteis/toxicidade
Mordeduras de Serpentes/tratamento farmacológico
Mordeduras de Serpentes/enzimologia
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antidotes); 0 (Antivenins); 0 (Crotalid Venoms); 0 (Reptilian Proteins); EC 3.1.- (Esterases); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170213
[Lr] Data última revisão:
170213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160904
[St] Status:MEDLINE


  9 / 813 MEDLINE  
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[PMID]:27898742
[Au] Autor:Zhu S; Wang Y; Chen W; Li W; Wang A; Wong S; Bao G; Li J; Yang H; Tracey KJ; D'Angelo J; Wang H
[Ad] Endereço:Department of Emergency Medicine, North Shore University Hospital, Manhasset, New York, United States of America.
[Ti] Título:High-Density Lipoprotein (HDL) Counter-Regulates Serum Amyloid A (SAA)-Induced sPLA2-IIE and sPLA2-V Expression in Macrophages.
[So] Source:PLoS One;11(11):e0167468, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human serum amyloid A (SAA) has been demonstrated as a chemoattractant and proinflammatory mediator of lethal systemic inflammatory diseases. In the circulation, it can be sequestered by a high-density lipoprotein, HDL, which carries cholesterol, triglycerides, phospholipids and apolipoproteins (Apo-AI). The capture of SAA by HDL results in the displacement of Apo-AI, and the consequent inhibition of SAA's chemoattractant activities. It was previously unknown whether HDL similarly inhibits SAA-induced sPLA2 expression, as well as the resultant HMGB1 release, nitric oxide (NO) production and autophagy activation. Here we provided compelling evidence that human SAA effectively upregulated the expression and secretion of both sPLA2-IIE and sPLA2-V in murine macrophages, which were attenuated by HDL in a dose-dependent fashion. Similarly, HDL dose-dependently suppressed SAA-induced HMGB1 release, NO production, and autophagy activation. In both RAW 264.7 cells and primary macrophages, HDL inhibited SAA-induced secretion of several cytokines (e.g., IL-6) and chemokines (e.g., MCP-1 and RANTES) that were likely dependent on functional TLR4 signaling. Collectively, these findings suggest that HDL counter-regulates SAA-induced upregulation and secretion of sPLA2-IIE/V in addition to other TLR4-dependent cytokines and chemokines in macrophage cultures.
[Mh] Termos MeSH primário: Lipoproteínas HDL/farmacologia
Fosfolipases A2 Secretórias/metabolismo
Proteína Amiloide A Sérica/metabolismo
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Autofagia/efeitos dos fármacos
Células Cultivadas
Quimiocinas/metabolismo
Citocinas/metabolismo
Relação Dose-Resposta a Droga
Fosfolipases A2 do Grupo II/genética
Fosfolipases A2 do Grupo II/metabolismo
Proteína HMGB1/metabolismo
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Óxido Nítrico/metabolismo
Fosfolipases A2 Secretórias/genética
Células RAW 264.7
Transdução de Sinais/efeitos dos fármacos
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokines); 0 (Cytokines); 0 (HMGB1 Protein); 0 (Lipoproteins, HDL); 0 (Serum Amyloid A Protein); 0 (Toll-Like Receptor 4); 31C4KY9ESH (Nitric Oxide); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (Phospholipases A2, Secretory)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0167468


  10 / 813 MEDLINE  
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[PMID]:27783042
[Au] Autor:Seo J; Maeng J; Kim HJ
[Ad] Endereço:College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul 120-750, Korea. hui7505@hanmail.net.
[Ti] Título:Translationally Controlled Tumor Protein Stimulates Dopamine Release from PC12 Cells via Ca -Independent Phospholipase A2 Pathways.
[So] Source:Int J Mol Sci;17(10), 2016 Oct 24.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The translationally controlled tumor protein (TCTP), initially identified as a tumor- and growth-related protein, is also known as a histamine-releasing factor (HRF). TCTP is widely distributed in the neuronal systems, but its function is largely uncharacterized. Here, we report a novel function of TCTP in the neurotransmitter release from a neurosecretory, pheochromocytoma (PC12) cells. Treatment with recombinant TCTP (rTCTP) enhanced both basal and depolarization (50 mM KCl)-evoked [³H]dopamine release in concentration- and time-dependent manners. Interestingly, even though rTCTP induced the increase in intracellular calcium levels ([Ca ] ), the rTCTP-driven effect on dopamine release was mediated by a Ca -independent pathway, as evidenced by the fact that Ca -modulating agents such as Ca chelators and a voltage-gated L-type Ca -channel blocker did not produce any changes in rTCTP-evoked dopamine release. In a study to investigate the involvement of phospholipase A2 (PLA2) in rTCTP-induced dopamine release, the inhibitor for Ca -independent PLA2 (iPLA2) produced a significant inhibitory effect on rTCTP-induced dopamine release, whereas this release was not significantly inhibited by Ca -dependent cytosolic PLA2 (cPLA2) and secretory PLA2 (sPLA2) inhibitors. We found that rTCTP-induced dopamine release from neuronal PC12 cells was modulated by a Ca -independent mechanism that involved PLA2 in the process, suggesting the regulatory role of TCTP in the neuronal functions.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Dopamina/metabolismo
Fosfolipases A2 do Grupo II/metabolismo
Neurônios/metabolismo
Fosfolipases A2 Citosólicas/metabolismo
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Células PC12
Ratos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (tumor protein, translationally-controlled 1); EC 3.1.1.4 (Group II Phospholipases A2); EC 3.1.1.4 (Phospholipases A2, Cytosolic); SY7Q814VUP (Calcium); VTD58H1Z2X (Dopamine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170328
[Lr] Data última revisão:
170328
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161027
[St] Status:MEDLINE



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