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[PMID]:29016670
[Au] Autor:Kanno T; Yasutake K; Tanaka K; Hadano S; Ikeda JE
[Ad] Endereço:NGP Biomedical Research Institute, Neugen Pharma Inc., Meguro, Tokyo, Japan.
[Ti] Título:A novel function of N-linked glycoproteins, alpha-2-HS-glycoprotein and hemopexin: Implications for small molecule compound-mediated neuroprotection.
[So] Source:PLoS One;12(10):e0186227, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Therapeutic agents to the central nervous system (CNS) need to be efficiently delivered to the target site of action at appropriate therapeutic levels. However, a limited number of effective drugs for the treatment of neurological diseases has been developed thus far. Further, the pharmacological mechanisms by which such therapeutic agents can protect neurons from cell death have not been fully understood. We have previously reported the novel small-molecule compound, 2-[mesityl(methyl)amino]-N-[4-(pyridin-2-yl)-1H-imidazol-2-yl] acetamide trihydrochloride (WN1316), as a unique neuroprotectant against oxidative injury and a highly promising remedy for the treatment of amyotrophic lateral sclerosis (ALS). One of the remarkable characteristics of WN1316 is that its efficacious doses in ALS mouse models are much less than those against oxidative injury in cultured human neuronal cells. It is also noted that the WN1316 cytoprotective activity observed in cultured cells is totally dependent upon the addition of fetal bovine serum in culture medium. These findings led us to postulate some serum factors being tightly linked to the WN1316 efficacy. In this study, we sieved through fetal bovine serum proteins and identified two N-linked glycoproteins, alpha-2-HS-glycoprotein (AHSG) and hemopexin (HPX), requisites to exert the WN1316 cytoprotective activity against oxidative injury in neuronal cells in vitro. Notably, the removal of glycan chains from these molecules did not affect the WN1316 cytoprotective activity. Thus, two glycoproteins, AHSG and HPX, represent a pivotal glycoprotein of the cytoprotective activity for WN1316, showing a concrete evidence for the novel glycan-independent function of serum glycoproteins in neuroprotective drug efficacy.
[Mh] Termos MeSH primário: Acetamidas/administração & dosagem
Sistema Nervoso Central/efeitos dos fármacos
Meios de Cultura/química
Hemopexina/metabolismo
Imidazóis/administração & dosagem
Bibliotecas de Moléculas Pequenas/administração & dosagem
alfa-2-Glicoproteína-HS/metabolismo
[Mh] Termos MeSH secundário: Animais
Bovinos
Morte Celular/efeitos dos fármacos
Sistema Nervoso Central/patologia
Hemopexina/química
Seres Humanos
Camundongos
Neurônios/efeitos dos fármacos
Neurônios/patologia
Fármacos Neuroprotetores/administração & dosagem
Fármacos Neuroprotetores/química
Estresse Oxidativo/efeitos dos fármacos
Bibliotecas de Moléculas Pequenas/química
alfa-2-Glicoproteína-HS/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetamides); 0 (Culture Media); 0 (Imidazoles); 0 (Neuroprotective Agents); 0 (Small Molecule Libraries); 0 (WN1316); 0 (alpha-2-HS-Glycoprotein); 7GBN705NH1 (imidazole); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186227


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[PMID]:28596380
[Au] Autor:Hahl P; Hunt R; Bjes ES; Skaff A; Keightley A; Smith A
[Ad] Endereço:From the Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2239.
[Ti] Título:Identification of oxidative modifications of hemopexin and their predicted physiological relevance.
[So] Source:J Biol Chem;292(33):13658-13671, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hemopexin protects against heme toxicity in hemolytic diseases and conditions, sepsis, and sickle cell disease. This protection is sustained by heme-hemopexin complexes in biological fluids that resist oxidative damage during heme-driven inflammation. However, apo-hemopexin is vulnerable to inactivation by reactive nitrogen (RNS) and oxygen species (ROS) that covalently modify amino acids. The resultant nitration of amino acids is considered a specific effect reflecting biological events. Using LC-MS, we discovered low endogenous levels of tyrosine nitration in the peptide YYCFQGNQFLR in the heme-binding site of human hemopexin, which was similarly nitrated in rabbit and rat hemopexins. Immunoblotting and selective reaction monitoring were used to quantify tyrosine nitration of samples and when hemopexin was incubated with nitrating nitrite/myeloperoxidase/glucose oxidase. Significantly, heme binding by hemopexin declined as tyrosine nitration proceeded Three nitrated tyrosines reside in the heme-binding site of hemopexin, and we found that one, Tyr-199, interacts directly with the heme ring D propionate. Investigating the oxidative modifications of amino acids after incubation with -butyl hydroperoxide and hypochlorous acid , we identified additional covalent oxidative modifications on four tyrosine residues and one tryptophan residue of hemopexin. Importantly, three of the four modified tyrosines, some of which have more than one modification, cluster in the heme-binding site, supporting a hierarchy of vulnerable amino acids. We propose that during inflammation, apo-hemopexin is nitrated and oxidated in niches of the body containing activated RNS- and ROS-generating immune and endothelial cells, potentially impairing hemopexin's protective extracellular antioxidant function.
[Mh] Termos MeSH primário: Hemopexina/metabolismo
Modelos Moleculares
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Apoproteínas/química
Apoproteínas/isolamento & purificação
Apoproteínas/metabolismo
Sítios de Ligação
Cromatografia Líquida de Alta Pressão
Sequência Conservada
Heme/química
Heme/metabolismo
Hemopexina/química
Hemopexina/isolamento & purificação
Seres Humanos
Cinética
Ligantes
Estrutura Molecular
Oxirredução
Conformação Proteica
Coelhos
Ratos
Espécies Reativas de Oxigênio/química
Espécies Reativas de Oxigênio/metabolismo
Especificidade da Espécie
Espectrometria de Massas em Tandem
Triptofano/química
Tirosina/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoproteins); 0 (Ligands); 0 (Reactive Oxygen Species); 42HK56048U (Tyrosine); 42VZT0U6YR (Heme); 8DUH1N11BX (Tryptophan); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.783951


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[PMID]:28550901
[Au] Autor:Jung JY; Kwak YH; Chang I; Kwon WY; Suh GJ; Choi D
[Ad] Endereço:Department of Emergency Medicine, Seoul National University Bundang Hospital, Seong-nam, Korea.
[Ti] Título:Protective effect of hemopexin on systemic inflammation and acute lung injury in an endotoxemia model.
[So] Source:J Surg Res;212:15-21, 2017 May 15.
[Is] ISSN:1095-8673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hemopexin (HPX) has been identified as an anti-inflammatory agent, but its role in endotoxemia is unclear. The purpose of this study was to determine whether HPX suppresses systemic and lung inflammation in a mouse model of endotoxemia. MATERIALS AND METHODS: At 30 min of intraperitoneal administration of lipopolysaccharide (LPS; 10 mg/kg), either distilled water (LPS-only treated animals) or HPX (5 mg/kg) was injected into mice via the tail vein, and the survival rates were analyzed after 36 h. Furthermore, the serum levels of tumor necrosis factor-α, interleukin-6 (IL-6), and HPX were determined at 0, 3, and 6 h, and the expression levels and DNA binding activities of phosphorylated cytoplasmic inhibitor κB-α, nuclear factor-κB (NF-κB), and the p65 subunit of NF-κB were evaluated and compared with the rates of histologic lung injury after 6 h. RESULTS: Serum tumor necrosis factor-α and interleukin-6 levels were decreased in HPX-treated animals at 3 and 6 h (P < 0.05). HPX suppressed the NF-κB pathway (P < 0.05) and reduced acute lung injury at 6 h, and 36 h after initial treatment, the survival rate was higher in HPX-treated animals than that in LPS-treated animals (P < 0.05). CONCLUSIONS: HPX downregulated proinflammatory cytokine production and acute lung injury as well as improved survival rates in a mouse model of endotoxemia. These effects were associated with HPX-mediated suppression of the NF-κB pathway.
[Mh] Termos MeSH primário: Lesão Pulmonar Aguda/prevenção & controle
Anti-Inflamatórios/uso terapêutico
Endotoxemia/tratamento farmacológico
Hemopexina/uso terapêutico
Lipopolissacarídeos/administração & dosagem
[Mh] Termos MeSH secundário: Lesão Pulmonar Aguda/sangue
Lesão Pulmonar Aguda/microbiologia
Lesão Pulmonar Aguda/mortalidade
Animais
Biomarcadores/sangue
Western Blotting
Endotoxemia/sangue
Endotoxemia/complicações
Endotoxemia/mortalidade
Ensaio de Imunoadsorção Enzimática
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Taxa de Sobrevida
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Biomarkers); 0 (Lipopolysaccharides); 0 (lipopolysaccharide, Escherichia coli O111 B4); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


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[PMID]:28314763
[Au] Autor:Graw JA; Yu B; Rezoagli E; Warren HS; Buys ES; Bloch DB; Zapol WM
[Ad] Endereço:Anesthesia Center for Critical Care Research, Department of Anesthesia, Critical Care, and Pain Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts.
[Ti] Título:Endothelial dysfunction inhibits the ability of haptoglobin to prevent hemoglobin-induced hypertension.
[So] Source:Am J Physiol Heart Circ Physiol;312(6):H1120-H1127, 2017 Jun 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intravascular hemolysis produces injury in a variety of human diseases including hemoglobinopathies, malaria, and sepsis. The adverse effects of increased plasma hemoglobin are partly mediated by depletion of nitric oxide (NO) and result in vasoconstriction. Circulating plasma proteins haptoglobin and hemopexin scavenge extracellular hemoglobin and cell-free heme, respectively. The ability of human haptoglobin or hemopexin to inhibit the adverse effects of NO scavenging by circulating murine hemoglobin was tested in C57Bl/6 mice. In healthy awake mice, the systemic hemodynamic effects of intravenous coinfusion of cell-free hemoglobin and exogenous haptoglobin or of cell-free hemoglobin and hemopexin were compared with the hemodynamic effects of infusion of cell-free hemoglobin or control protein (albumin) alone. We also studied the hemodynamic effects of infusing hemoglobin and haptoglobin as well as injecting either hemoglobin or albumin alone in mice fed a high-fat diet (HFD) and in diabetic ( / ) mice. Coinfusion of a 1:1 weight ratio of haptoglobin but not hemopexin with cell-free hemoglobin prevented hemoglobin-induced systemic hypertension in healthy awake mice. In mice fed a HFD and in diabetic mice, coinfusion of haptoglobin mixed with an equal mass of cell-free hemoglobin did not reverse hemoglobin-induced hypertension. Haptoglobin retained cell-free hemoglobin in plasma, but neither haptoglobin nor hemopexin affected the ability of hemoglobin to scavenge NO ex vivo. In conclusion, in healthy C57Bl/6 mice with normal endothelium, coadministration of haptoglobin but not hemopexin with cell-free hemoglobin prevents acute hemoglobin-induced systemic hypertension by compartmentalizing cell-free hemoglobin in plasma. In murine diseases associated with endothelial dysfunction, haptoglobin therapy appears to be insufficient to prevent hemoglobin-induced vasoconstriction. Coadministraton of haptoglobin but not hemopexin with cell-free hemoglobin prevents hemoglobin-induced systemic hypertension in mice with a normal endothelium. In contrast, treatment with the same amount of haptoglobin is unable to prevent hemoglobin-induced vasoconstriction in mice with hyperlipidemia or diabetes mellitus, disorders that are associated with endothelial dysfunction.
[Mh] Termos MeSH primário: Anti-Hipertensivos/farmacologia
Endotélio Vascular/efeitos dos fármacos
Haptoglobinas/farmacologia
Hemoglobinas
Hemopexina/farmacologia
Hipertensão/prevenção & controle
Vasoconstrição/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Anti-Hipertensivos/administração & dosagem
Diabetes Mellitus/fisiopatologia
Dieta Hiperlipídica
Endotélio Vascular/metabolismo
Endotélio Vascular/fisiopatologia
Haptoglobinas/administração & dosagem
Hemopexina/administração & dosagem
Hipertensão/induzido quimicamente
Hipertensão/metabolismo
Hipertensão/fisiopatologia
Infusões Intravenosas
Rim/metabolismo
Rim/fisiopatologia
Masculino
Camundongos Endogâmicos C57BL
Óxido Nítrico/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antihypertensive Agents); 0 (Haptoglobins); 0 (Hemoglobins); 31C4KY9ESH (Nitric Oxide); 9013-71-2 (Hemopexin)
[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:170319
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00851.2016


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[PMID]:28186971
[Au] Autor:Jiang B; Zhang Y; Liu J; Tsigkou A; Rapti M; Lee MH
[Ad] Endereço:Department of Biological Sciences, Xian Jiaotong Liverpool University, Suzhou 215123, China.
[Ti] Título:Ensnaring membrane type 1-matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase (TIMP)-2 using the haemopexin domain of the protease as a carrier: a targeted approach in cancer inhibition.
[So] Source:Oncotarget;8(14):22685-22699, 2017 Apr 04.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metastatic cancer cells express Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) to degrade the extracellular matrix in order to facilitate migration and proliferation. Tissue Inhibitor of Metalloproteinase (TIMP)-2 is the endogenous inhibitor of the MMP. Here, we describe a novel and highly effective fusion strategy to enhance the delivery of TIMP-2 to MT1-MMP. We can reveal that TIMP-2 fused to the haemopexin +/- transmembrane domains of MT1-MMP (two chimeras named T2PEX+TM and T2PEX) are able to interact with MT1-MMP on the cell surface as well as intracellularly. In the case of T2PEX+TM, there is even a clear sign of MT1-MMP:T2PEX+TM aggregation by the side of the nucleus to form aggresomes. In vitro, T2PEX+TM and T2PEX suppress the gelatinolytic and invasive abilities of cervical carcinoma (HeLa) and HT1080 fibrosarcoma cancer cells significantly better than wild type TIMP-2. In mouse xenograft, we further demonstrate that T2PEX diminishes cervical carcinoma growth by 85% relative to the control. Collectively, our findings indicate the effectiveness of the fusion strategy as a potential targeted approach in cancer inhibition.
[Mh] Termos MeSH primário: Fibrossarcoma/tratamento farmacológico
Hemopexina/química
Metaloproteinase 14 da Matriz/química
Inibidores de Metaloproteinases de Matriz/farmacologia
Inibidor Tecidual de Metaloproteinase-2/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Apoptose/efeitos dos fármacos
Biomarcadores Tumorais/metabolismo
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Matriz Extracelular/metabolismo
Fibrossarcoma/metabolismo
Fibrossarcoma/patologia
Células HeLa
Seres Humanos
Metaloproteinase 14 da Matriz/metabolismo
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Matrix Metalloproteinase Inhibitors); 0 (TIMP2 protein, human); 127497-59-0 (Tissue Inhibitor of Metalloproteinase-2); 9013-71-2 (Hemopexin); EC 3.4.24.80 (MMP14 protein, human); EC 3.4.24.80 (Matrix Metalloproteinase 14)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15165


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[PMID]:28030762
[Au] Autor:Mary S; Kulkarni MJ; Malakar D; Joshi SR; Mehendale SS; Giri AP
[Ad] Endereço:Division of Biochemical Sciences, CSIR-National Chemical Laboratory , Homi Bhabha Road, Pune, Maharashtra 411008, India.
[Ti] Título:Placental Proteomics Provides Insights into Pathophysiology of Pre-Eclampsia and Predicts Possible Markers in Plasma.
[So] Source:J Proteome Res;16(2):1050-1060, 2017 Feb 03.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pre-eclampsia is a hypertensive disorder characterized by the new onset of hypertension >140/90 mmHg and proteinuria after the 20th week of gestation. The disorder is multifactorial and originates with abnormal placentation. Comparison of the placental proteome of normotensive (n = 25) and pre-eclamptic (n = 25) patients by gel-free proteomic techniques identified a total of 2145 proteins in the placenta of which 180 were differentially expressed (>1.3 fold, p < 0.05). Gene ontology enrichment analysis of biological process suggested that the differentially expressed proteins belonged to various physiological processes such as angiogenesis, apoptosis, oxidative stress, hypoxia, and placental development, which are implicated in the pathophysiology of pre-eclampsia. Some of the differentially expressed proteins were monitored in the plasma by multiple reaction monitoring analysis, which showed an increase in apolipoproteins A-I and A-II in gestational weeks 26-30 (2-fold, p < 0.01), while haptoglobin and hemopexin decreased in gestational weeks 26-30 and week 40/at delivery (1.8 fold, p < 0.01) in pre-eclamptic patients. This study provides a proteomic insight into the pathophysiology of pre-eclampsia. Identified candidate proteins can be evaluated further for the development of potential biomarkers associated with pre-eclampsia pathogenesis.
[Mh] Termos MeSH primário: Hipóxia/sangue
Neovascularização Patológica/sangue
Placenta/metabolismo
Pré-Eclâmpsia/sangue
Proteoma/genética
Proteômica/métodos
[Mh] Termos MeSH secundário: Adulto
Apolipoproteína A-I/sangue
Apolipoproteína A-I/genética
Apolipoproteína A-II/sangue
Apolipoproteína A-II/genética
Apoptose/genética
Biomarcadores/sangue
Estudos de Casos e Controles
Feminino
Perfilação da Expressão Gênica
Regulação da Expressão Gênica
Ontologia Genética
Idade Gestacional
Haptoglobinas/genética
Haptoglobinas/metabolismo
Hemopexina/genética
Hemopexina/metabolismo
Seres Humanos
Hipóxia/diagnóstico
Hipóxia/genética
Hipóxia/patologia
Anotação de Sequência Molecular
Neovascularização Patológica/diagnóstico
Neovascularização Patológica/genética
Neovascularização Patológica/patologia
Estresse Oxidativo
Placenta/irrigação sanguínea
Placenta/patologia
Pré-Eclâmpsia/diagnóstico
Pré-Eclâmpsia/genética
Pré-Eclâmpsia/patologia
Gravidez
Mapeamento de Interação de Proteínas
Proteoma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoprotein A-I); 0 (Apolipoprotein A-II); 0 (Biomarkers); 0 (Haptoglobins); 0 (Proteome); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.6b00955


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[PMID]:27768920
[Au] Autor:Nardiello D; Prattichizzo C; Rocchetti MT; Gesualdo L; Centonze D
[Ad] Endereço:Dipartimento di Scienze Agrarie, degli Alimenti e dell'Ambiente and CSRA- Centro Servizi di Ricerca Applicata, Università degli Studi di Foggia, Via Napoli, 25 - 71122 Foggia, Italy. Electronic address: donatella.nardiello@unifg.it.
[Ti] Título:Nano-LC-MS/MS for the identification of proteins trapped in sorbent cartridges used for coupled plasma filtration-adsorption treatments of healthy pigs.
[So] Source:J Pharm Biomed Anal;132:215-222, 2017 Jan 05.
[Is] ISSN:1873-264X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A dedicated proteomic approach based on nano-Liquid Chromatography coupled with tandem mass spectrometry in ion trap is proposed for the analysis of proteins trapped in sorbent resin cartridges used to remove inflammatory mediators from blood by coupled plasma filtration adsorption (CPFA). The final purpose of the proposed proteomic approach was to obtain a reference map of plasma proteins trapped in CPFA sorbents used for the extracorporeal blood purification of healthy pigs, with the potential impact to design new bio-filters able to control the inflammatory imbalance under pathological conditions, such as severe sepsis. The five main steps of the proteomics analysis, (i) protein extraction from resin cartridges, (ii) two-dimensional gel electrophoresis (2D-PAGE) for protein separation and profiling, (iii) in-gel proteolytic digestion, (iv) tandem mass analysis of peptides resulting from enzymatic cleavage and (v) bioinformatics, for protein identification and post-processing validation of MS/MS data sets, have been carefully evaluated. Prior to electrophoresis, the efficiency of different extraction solutions and procedures to recovery plasma proteins trapped into the sorbents were tested. Then, a rapid one-step procedure for protein extraction was optimized. Protein bands corresponding to the main plasma proteins, namely porcine serum albumin, serotransferrin and immunoglobulins, were identified. In addition, the presence of haptoglobin, hemopexin, α-1 acid glycoprotein and fetuin-A, that are known as acute-phase reaction proteins, was observed, suggesting that CPFA resins led to a non-specifically protein depletion from plasma, rather than targeting specific molecules.
[Mh] Termos MeSH primário: Cromatografia Líquida/métodos
Proteínas/química
Espectrometria de Massas em Tandem/métodos
[Mh] Termos MeSH secundário: Reação de Fase Aguda
Animais
Bovinos
Biologia Computacional
Citocromos c/química
Eletroforese em Gel Bidimensional
Eletroforese em Gel de Poliacrilamida
Filtração
Haptoglobinas/química
Hemopexina/química
Inflamação
Orosomucoide/química
Proteólise
Sepse/sangue
Sepse/terapia
Software
Desintoxicação por Sorção/métodos
Suínos
alfa-2-Glicoproteína-HS/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Haptoglobins); 0 (Orosomucoid); 0 (Proteins); 0 (alpha-2-HS-Glycoprotein); 9007-43-6 (Cytochromes c); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161108
[St] Status:MEDLINE


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[PMID]:27317656
[Au] Autor:Wang G; Manaenko A; Shao A; Ou Y; Yang P; Budbazar E; Nowrangi D; Zhang JH; Tang J
[Ad] Endereço:1 Department of Physiology, Loma Linda University, Loma Linda, CA, USA.
[Ti] Título:Low-density lipoprotein receptor-related protein-1 facilitates heme scavenging after intracerebral hemorrhage in mice.
[So] Source:J Cereb Blood Flow Metab;37(4):1299-1310, 2017 Apr.
[Is] ISSN:1559-7016
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heme-degradation after erythrocyte lysis plays an important role in the pathophysiology of intracerebral hemorrhage. Low-density lipoprotein receptor-related protein-1 is a receptor expressed predominately at the neurovascular interface, which facilitates the clearance of the hemopexin and heme complex. In the present study, we investigated the role of low-density lipoprotein receptor-related protein-1 in heme removal and neuroprotection in a mouse model of intracerebral hemorrhage. Endogenous low-density lipoprotein receptor-related protein-1 and hemopexin were increased in ipsilateral brain after intracerebral hemorrhage, accompanied by increased hemoglobin levels, brain water content, blood-brain barrier permeability and neurological deficits. Exogenous human recombinant low-density lipoprotein receptor-related protein-1 protein reduced hematoma volume, brain water content surrounding hematoma, blood-brain barrier permeability and improved neurological function three days after intracerebral hemorrhage. The expression of malondialdehyde, fluoro-Jade C positive cells and cleaved caspase 3 was increased three days after intracerebral hemorrhage in the ipsilateral brain tissues and decreased with recombinant low-density lipoprotein receptor-related protein-1. Intracerebral hemorrhage decreased and recombinant low-density lipoprotein receptor-related protein-1 increased the levels of superoxide dismutase 1. Low-density lipoprotein receptor-related protein-1 siRNA reduced the effect of human recombinant low-density lipoprotein receptor-related protein-1 on all outcomes measured. Collectively, our findings suggest that low-density lipoprotein receptor-related protein-1 contributed to heme clearance and blood-brain barrier protection after intracerebral hemorrhage. The use of low-density lipoprotein receptor-related protein-1 as supplement provides a novel approach to ameliorating intracerebral hemorrhage brain injury via its pleiotropic neuroprotective effects.
[Mh] Termos MeSH primário: Hemorragia Cerebral/metabolismo
Heme/metabolismo
Fármacos Neuroprotetores/uso terapêutico
Receptores de LDL/metabolismo
Receptores de LDL/uso terapêutico
Proteínas Supressoras de Tumor/metabolismo
Proteínas Supressoras de Tumor/uso terapêutico
[Mh] Termos MeSH secundário: Animais
Comportamento Animal/efeitos dos fármacos
Barreira Hematoencefálica/efeitos dos fármacos
Barreira Hematoencefálica/metabolismo
Permeabilidade Capilar/efeitos dos fármacos
Hemorragia Cerebral/tratamento farmacológico
Hemopexina/metabolismo
Masculino
Camundongos Endogâmicos
Fármacos Neuroprotetores/administração & dosagem
Receptores de LDL/administração & dosagem
Proteínas Recombinantes
Proteínas Supressoras de Tumor/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lrp1 protein, mouse); 0 (Neuroprotective Agents); 0 (Receptors, LDL); 0 (Recombinant Proteins); 0 (Tumor Suppressor Proteins); 42VZT0U6YR (Heme); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160619
[St] Status:MEDLINE
[do] DOI:10.1177/0271678X16654494


  9 / 742 MEDLINE  
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[PMID]:27716784
[Au] Autor:Ji X; Feng Y; Tian H; Meng W; Wang W; Liu N; Zhang J; Wang L; Wang J; Gao H
[Ad] Endereço:Geriatric Department Qilu Hospital of Shandong Univeristy; Shandong Key Laboratory of Proteomics, Jinan 250012, Shandong, China.
[Ti] Título:The Mechanism of Proinflammatory HDL Generation in Sickle Cell Disease Is Linked to Cell-Free Hemoglobin via Haptoglobin.
[So] Source:PLoS One;11(10):e0164264, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In sickle cell disease (SCD), the inflammatory properties of high-density lipoprotein (HDL) can be changed by cell-free hemoglobin (Hb), which is released into the blood during hemolysis. Hb in the plasma of SCD patients or mice can bind with HDL specifically inducing an inflammatory reaction. In our study, we found increased amounts of inflammatory factor proteins in the chronic oxidative state of SCD with higher levels of Hb, haptoglobin (Hp) and hemopexin (Hx) in the apolipoprotein A-I (ApoA-1) particles of HDL and the role of HDL is changed from being anti-inflammatory to proinflammatory. Our results also suggest Hp and Hx, the scavengers of Hb in HDL, are positively associated with inflammatory levels in SCD patients. HDL retained its inflammatory inhibition role in Hp-/- mice, with less Hb accumulation. Hx may further prevent inflammatory reaction because its level will be even higher when lack of Hx. We therefore demonstrated that Hp is indispensable during the process whereby Hb associates with HDL and plays a clear proinflammatory role. Therefore, it is essential to break the binding between Hb and Hp for treatment. The dissociation of Hb/Hp/Hx complexes may also play an important role in the study of other inflammatory angiogenesis-related diseases.
[Mh] Termos MeSH primário: Anemia Falciforme/metabolismo
Haptoglobinas/metabolismo
Hemoglobinas/metabolismo
Inflamação/sangue
Inflamação/metabolismo
[Mh] Termos MeSH secundário: Adulto
Anemia Falciforme/sangue
Animais
Apolipoproteína A-I/metabolismo
Feminino
Testes Hematológicos/métodos
Hemólise/fisiologia
Hemopexina/metabolismo
Seres Humanos
Lipoproteínas HDL/sangue
Camundongos
Camundongos Endogâmicos C57BL
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoprotein A-I); 0 (Haptoglobins); 0 (Hemoglobins); 0 (Lipoproteins, HDL); 0 (haptoglobin-hemoglobin complex); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161008
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0164264


  10 / 742 MEDLINE  
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[PMID]:27515862
[Au] Autor:Elphinstone RE; Conroy AL; Hawkes M; Hermann L; Namasopo S; Warren HS; John CC; Liles WC; Kain KC
[Ad] Endereço:Sandra Rotman Centre for Global Health, University Health Network-Toronto General Hospital Department of Laboratory Medicine and Pathobiology.
[Ti] Título:Alterations in Systemic Extracellular Heme and Hemopexin Are Associated With Adverse Clinical Outcomes in Ugandan Children With Severe Malaria.
[So] Source:J Infect Dis;214(8):1268-75, 2016 Oct 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Malaria remains a major cause of global mortality. Extracellular heme, released during malaria-induced hemolysis, mediates a number of pathogenic processes associated with vascular and organ injury. Hemopexin (hpx) facilitates the degradation of extracellular heme. In this study, we explore the hypothesis that dysregulation of the heme-hpx axis is associated with disease severity, acute kidney injury (AKI), and outcome. METHODS: Plasma levels of hemin and hpx (at admission, day 3, and day 14) were assessed in children with severe malaria in Jinja, Uganda. RESULTS: The ratio of heme to hpx was higher at admission and decreased with recovery (median, 0.043 [interquartile range {IQR}, 0.007-0.239] on day 1, 0.024 [IQR, 0.005-0.126] on day 3, and 0.008 [IQR, 0.002-0.022] on day 14; P < .001). Ratios of heme to hpx at admission were higher in children with as compared to those without severe anemia (median, 0.124 [IQR, 0.024-0.431] vs 0.016 [IQR, 0.003-0.073]; P < .0001), children with as compared to those without respiratory distress (median, 0.063 [IQR, 0.017-0.413] vs 0.020 [IQR, 0.004-0.124]; P < .01), and children with as opposed to those without stage 3 AKI (median, 0.354 [IQR, 0.123-2.481] vs 0.037 [IQR, 0.005-0.172], P < .01). The heme to hpx ratio at admission was associated with 6-month mortality (median, 0.148 [IQR, 0.042-0.500] vs 0.039 [IQR, 0.007-0.172]; P = .012). CONCLUSIONS: The ratio of heme to hpx is associated with disease severity and adverse clinical outcomes in Ugandan children, and dysregulation of the heme axis may contribute to malaria pathogenesis.
[Mh] Termos MeSH primário: Heme/metabolismo
Hemopexina/metabolismo
Malária/sangue
Malária/metabolismo
Plasma/metabolismo
[Mh] Termos MeSH secundário: Lesão Renal Aguda/metabolismo
Pré-Escolar
Método Duplo-Cego
Feminino
Seres Humanos
Masculino
Índice de Gravidade de Doença
Uganda
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
42VZT0U6YR (Heme); 9013-71-2 (Hemopexin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160813
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jiw357



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