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[PMID]:29288051
[Au] Autor:Tanaka M; Kawakami T; Okino N; Sasaki K; Nakanishi K; Takase H; Yamada T; Mukai T
[Ad] Endereço:Department of Biophysical Chemistry, Kobe Pharmaceutical University, Kobe 658-8558, Japan. Electronic address: masatnk@kobepharma-u.ac.jp.
[Ti] Título:Acceleration of amyloid fibril formation by carboxyl-terminal truncation of human serum amyloid A.
[So] Source:Arch Biochem Biophys;639:9-15, 2018 02 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human serum amyloid A (SAA) is a precursor protein of AA amyloidosis. Although the full-length SAA is 104 amino acids long, the C-terminal-truncated SAA lacking mainly residues 77-104 is predominantly deposited in AA amyloidosis. Nevertheless, the amyloid fibril formation of such truncated forms of human SAA has never been investigated. In the present study, we examined the effect of C-terminal truncation on amyloid fibril formation of human SAA induced by heparan sulfate (HS). Circular dichroism (CD) measurements demonstrated that the C-terminal truncation induces a reduced α-helical structure of the SAA molecule. HS-induced increases in thioflavin T fluorescence for SAA (1-76) peptide and less significant increases for full-length SAA were observed. CD spectral changes of SAA (1-76) peptide but not full-length SAA were observed when incubated with HS, although the spectrum was not typical for a ß-structure. Fourier transform infrared experiments clearly revealed that SAA (1-76) peptide forms a ß-sheet structure. Transmission electron microscopy revealed that short fibrillar aggregates of SAA (1-76) peptides, which became longer with increasing peptide concentrations, were observed under conditions in which full-length SAA scarcely formed fibrillar aggregates. These results suggested that the C-terminal truncation of human SAA accelerates amyloid fibril formation.
[Mh] Termos MeSH primário: Heparitina Sulfato/química
Agregados Proteicos
Proteína Amiloide A Sérica/química
[Mh] Termos MeSH secundário: Dicroísmo Circular
Seres Humanos
Domínios Proteicos
Estrutura Secundária de Proteína
Proteína Amiloide A Sérica/genética
Proteína Amiloide A Sérica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Aggregates); 0 (Serum Amyloid A Protein); 9050-30-0 (Heparitin Sulfate)
[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:171231
[St] Status:MEDLINE


  2 / 3538 MEDLINE  
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[PMID]:28865214
[Au] Autor:Krakowski L; Bartoszek P; Krakowska I; Olcha P; Piech T; Stachurska A; Brodzki P
[Ad] Endereço:.
[Ti] Título:Serum amyloid A protein (SAA), haptoglobin (Hp) and selected hematological and biochemical parameters in wild mares before and after parturition.
[So] Source:Pol J Vet Sci;20(2):299-305, 2017 Mar 01.
[Is] ISSN:1505-1773
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The aim of the study was to evaluate physiological changes in hematological and biochemical parameters in mares in perinatal period. Blood samples were collected from 24 pregnant Polish Konik breed mares which were divided into two groups. The first group (Group - I, n=12) comprised mares living in the wild, in the reserve. The second group (Group - II, n=12) consisted of mares kept in stables. The blood was collected 2 weeks prior to the parturition, then 24 hours after the delivery, and then at the 7th and 21st day after foaling. When comparing the two groups before the parturition, no significant differences in terms of WBC, RBC, and Hb were found, however, there was a significant difference in MCV, MCH, LYM, NEU and SEG NEU (p≤0.05). In Group II, 24 hours after the parturition and at the 21st day after foaling, a significant raise in WBC, NEU and SEG NEU (p≤0.05) was detected. No significant differences in serum concentrations of proteins such as TP, Alb or Glb were observed. As to acute phase proteins, significant rise in SAA and Hp (p≤0.05) was found in the two examined groups 24 hours after the parturition. Yet, this rise remained within physiological range. The study revealed a certain degree of fluctuations in hematological parameters, in serum concentrations of acute-phase proteins and total proteins in the mares in the perinatal period. However, these changes remained still within physiological ranges and thus they do not indicate potential susceptibility to disorders of perinatal period.
[Mh] Termos MeSH primário: Haptoglobinas/metabolismo
Cavalos/fisiologia
Prenhez
Proteína Amiloide A Sérica/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Selvagens
Análise Química do Sangue/veterinária
Contagem de Eritrócitos/veterinária
Feminino
Contagem de Linfócitos/veterinária
Parto
Gravidez
Prenhez/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Haptoglobins); 0 (Serum Amyloid A Protein)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE


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[PMID]:28834898
[Au] Autor:Esatoglu SN; Hatemi G; Ugurlu S; Gokturk A; Tascilar K; Ozdogan H
[Ad] Endereço:aDivision of Rheumatology, Department of Internal Medicine, Cerrahpasa Medical School, Istanbul University bDepartment of Internal Medicine, Cerrahpasa Medical School, Istanbul University, Istanbul, Turkey.
[Ti] Título:Long-term follow-up of secondary amyloidosis patients treated with tumor necrosis factor inhibitor therapy: A STROBE-compliant observational study.
[So] Source:Medicine (Baltimore);96(34):e7859, 2017 Aug.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There are no treatment modalities, which were proven to prevent the deposition of amyloid, proteinuria, and loss of renal function due to amyloidosis. Anti-tumor necrosis factor agents (anti-TNFs) were shown to decrease the production of serum amyloid A protein.We aimed to evaluate the long-term efficacy and safety of anti-TNFs in secondary (AA) amyloidosis patients treated in a single center.Thirty-seven patients with AA amyloidosis were started an anti-TNF for AA amyloidosis between March 2001 and June 2008 and followed until May 2016 unless deceased. They were surveyed for the endpoints of death, development of end-stage renal disease (ESRD), switch to another agent due to worsening of amyloidosis and adverse events.Among the 37 patients, 12 (32%) had died, 9 (24%) had ESRD, and 8 (22%) had started another group of biologic due to worsening of amyloidosis indicated by an increase in proteinuria, 5 (14%) patients are still doing well with anti-TNFs, and 3 (8%) are off treatment at the end of a median follow-up of 10 (interquartile range [IQR]: 5.5-10.5) years since the start of anti-TNFs and 10 (IQR: 8-13) years since the diagnosis of AA amyloidosis. Most common serious adverse events were sepsis and thrombotic events observed in 8 and 4 patients, respectively.Treatment with anti-TNFs may be associated with a higher survival rate compared with historic cohorts of AA amyloidosis, especially when started early with a lower serum creatinine level at baseline. Caution is needed regarding serious adverse events, especially infections.
[Mh] Termos MeSH primário: Amiloidose/tratamento farmacológico
Fator de Necrose Tumoral alfa/antagonistas & inibidores
[Mh] Termos MeSH secundário: Adulto
Amiloidose/complicações
Amiloidose/mortalidade
Feminino
Seguimentos
Seres Humanos
Falência Renal Crônica/etiologia
Masculino
Meia-Idade
Proteinúria
Proteína Amiloide A Sérica
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Serum Amyloid A Protein); 0 (Tumor Necrosis Factor-alpha)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000007859


  4 / 3538 MEDLINE  
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[PMID]:28806760
[Au] Autor:Li XK; Yang ZD; Du J; Xing B; Cui N; Zhang PH; Li H; Zhang XA; Lu QB; Liu W
[Ad] Endereço:State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, P. R. China.
[Ti] Título:Endothelial activation and dysfunction in severe fever with thrombocytopenia syndrome.
[So] Source:PLoS Negl Trop Dis;11(8):e0005746, 2017 Aug.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pathogenesis of severe fever with thrombocytopenia syndrome (SFTS) has not been well described yet. Recent studies indicate that SFTSV could replicate in endothelial cells. Here we performed a case-control study to determine whether endothelial activation/dysfunction occurred in SFTSV infection and to identify the biomarkers reflecting endothelial dysfunction. METHODOLOGY/PRINCIPAL FINDINGS: In a case-control study of 134 SFTS patients and 68 healthy controls, serum levels of plasminogen activator inhibitor 1, tissue plasminogen activator, P-selectin, platelet endothelial cell adhesion molecular, CD40 ligand, E-selectin, vascular endothelial growth factor A, serum amyloid antigen 1 (SAA-1) and vascular cell adhesion molecular 1 were significantly enhanced in the patients than the controls (all P<0.05), indicating the occurrence of endothelial activation/dysfunction in SFTS. The intercellular adhesion molecular 1 (ICAM-1) and SAA-1 at the convalescent phase were also significantly associated with severe patients, after adjusting for the potential confounders. The odds ratio was estimated to be 3.364 (95% CI 1.074-10.534) for ICAM-1, and 1.881 (95% CI 1.166-3.034) for SAA-1, respectively. Cutoff value of 1.1×107 pg/mL SAA-1 or 1.2×106 pg/mL ICAM-1 were found to have moderate power of predicting fatal cases. CONCLUSIONS: The endothelial dysfunction may be one of the pathogenic mechanism of SFTS. The serum levels of ICAM-1 and SAA-1 might be used to predict adverse outcome.
[Mh] Termos MeSH primário: Biomarcadores/sangue
Infecções por Bunyaviridae/fisiopatologia
Células Endoteliais/fisiologia
Células Endoteliais/virologia
Molécula 1 de Adesão Intercelular/sangue
Phlebovirus/fisiologia
Proteína Amiloide A Sérica/análise
[Mh] Termos MeSH secundário: Infecções por Bunyaviridae/virologia
Estudos de Casos e Controles
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (SAA1 protein, human); 0 (Serum Amyloid A Protein); 126547-89-5 (Intercellular Adhesion Molecule-1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170917
[Lr] Data última revisão:
170917
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005746


  5 / 3538 MEDLINE  
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[PMID]:28791746
[Au] Autor:Rising A; Cederlund E; Palmberg C; Uhlhorn H; Gaunitz S; Nordling K; Ågren E; Ihse E; Westermark GT; Tjernberg L; Jörnvall H; Johansson J; Westermark P
[Ad] Endereço:Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, 750 07, Sweden.
[Ti] Título:Systemic AA amyloidosis in the red fox (Vulpes vulpes).
[So] Source:Protein Sci;26(11):2312-2318, 2017 Nov.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amyloid A (AA) amyloidosis occurs spontaneously in many mammals and birds, but the prevalence varies considerably among different species, and even among subgroups of the same species. The Blue fox and the Gray fox seem to be resistant to the development of AA amyloidosis, while Island foxes have a high prevalence of the disease. Herein, we report on the identification of AA amyloidosis in the Red fox (Vulpes vulpes). Edman degradation and tandem MS analysis of proteolyzed amyloid protein revealed that the amyloid partly was composed of full-length SAA. Its amino acid sequence was determined and found to consist of 111 amino acid residues. Based on inter-species sequence comparisons we found four residue exchanges (Ser31, Lys63, Leu71, Lys72) between the Red and Blue fox SAAs. Lys63 seems unique to the Red fox SAA. We found no obvious explanation to how these exchanges might correlate with the reported differences in SAA amyloidogenicity. Furthermore, in contrast to fibrils from many other mammalian species, the isolated amyloid fibrils from Red fox did not seed AA amyloidosis in a mouse model.
[Mh] Termos MeSH primário: Amiloidose/patologia
Monitoramento Epidemiológico/veterinária
Proteína Amiloide A Sérica/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Amiloidose/diagnóstico
Amiloidose/epidemiologia
Amiloidose/metabolismo
Animais
Feminino
Raposas
Expressão Gênica
Rim/química
Rim/patologia
Masculino
Camundongos
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Proteína Amiloide A Sérica/química
Proteína Amiloide A Sérica/metabolismo
Baço/química
Baço/patologia
Suécia/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Serum Amyloid A Protein)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3264


  6 / 3538 MEDLINE  
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[PMID]:28765498
[Au] Autor:Robinson CS; Singer ER; Piviani M; Rubio-Martinez LM
[Ad] Endereço:Department of Equine Clinical Science, Institute of Veterinary Science, University of Liverpool, Wirral, UK.
[Ti] Título:Are serum amyloid A or D-lactate useful to diagnose synovial contamination or sepsis in horses?
[So] Source:Vet Rec;181(16):425, 2017 Oct 21.
[Is] ISSN:2042-7670
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Synovial sepsis in horses is life threatening and accurate diagnosis allowing prompt treatment is warranted. This study assessed the diagnostic value of serum amyloid A (SAA) and D-lactate in blood and synovial fluid (SF) as diagnostic markers of synovial sepsis in horses and correlated them with total nucleated cell count (TNCC), percentage of neutrophils (%N) and total protein (TP) in SF. Blood and SF SAA and D-lactate concentrations were determined in a case-control observational study including 112 horses (38 with synovial contamination or sepsis (SCS), 66 with non-septic intra-synovial pathology (NSISP) and 8 controls). Blood and SF SAA were significantly higher in SCS than in NSISP and control horses. SAA values were similar in NSISP and control horses. SF SAA was moderately correlated with synovial TNCC, TP and blood SAA. Blood and SF SAA were 82.4 per cent and 80 per cent sensitive and 88.9 per cent and 73 per cent specific for diagnosis of SCS, with cut-off values of 60.7 and 1.14 µg/ml, respectively. Blood and SF D-lactate concentrations were not significantly different between groups. This study shows that blood and SF SAA concentrations can aid to distinguish SCS from non-septic synovial pathology; however, D-lactate was not useful.
[Mh] Termos MeSH primário: Doenças dos Cavalos/diagnóstico
Lactato Desidrogenases/sangue
Sepse/veterinária
Proteína Amiloide A Sérica/análise
Líquido Sinovial/química
[Mh] Termos MeSH secundário: Animais
Estudos de Casos e Controles
Feminino
Doenças dos Cavalos/sangue
Cavalos
Masculino
Sepse/sangue
Sepse/diagnóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Serum Amyloid A Protein); EC 1.1.- (Lactate Dehydrogenases); EC 1.1.1.28 (D-lactate dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1136/vr.104386


  7 / 3538 MEDLINE  
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[PMID]:28738073
[Au] Autor:Tashiro M; Iwata A; Yamauchi M; Shimizu K; Okada A; Ishiguro N; Inoshima Y
[Ad] Endereço:Laboratory of Food and Environmental Hygiene, Cooperative Department of Veterinary Medicine, Faculty of Applied Biological Sciences, Gifu University, Gifu, Japan.
[Ti] Título:The N-terminal region of serum amyloid A3 protein activates NF-κB and up-regulates MUC2 mucin mRNA expression in mouse colonic epithelial cells.
[So] Source:PLoS One;12(7):e0181796, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serum amyloid A (SAA) is the major acute-phase protein and a precursor of amyloid A (AA) in AA amyloidosis in humans and animals. SAA isoforms have been identified in a wide variety of animals, such as SAA1, SAA2, SAA3, and SAA4 in mouse. Although the biological functions of SAA isoforms are not completely understood, recent studies have suggested that SAA3 plays a role in host defense. Expression of SAA3 is increased on the mouse colon surface in the presence of microbiota in vivo, and it increases mRNA expression of mucin 2 (MUC2) in murine colonic epithelial cells in vitro, which constitutes a protective mucus barrier in the intestinal tract. In this study, to identify responsible regions in SAA3 for MUC2 expression, recombinant murine SAA1 (rSAA1), rSAA3, and rSAA1/3, a chimera protein constructed with mature SAA1 (amino acids 1-36) and SAA3 (amino acids 37-103), and vice versa for rSAA3/1, were added to murine colonic epithelial CMT-93 cells, and the mRNA expressions of MUC2 and cytokines were measured. Inhibition assays with NF-κB inhibitor or TLR4/MD2 inhibitor were also performed. Up-regulation of MUC2 mRNA expression was strongly stimulated by rSAA3 and rSAA3/1, but not by rSAA1 or rSAA1/3. Moreover, NF-κB and TLR4/MD2 inhibitors suppressed the increase of MUC2 mRNA expression. These results suggest that the major responsible region for MUC2 expression exists in amino acids 1-36 of SAA3, and that up-regulations of MUC2 expression by SAA3 and SAA3/1 are involved with activation of NF-κB via the TLR4/MD2 complex.
[Mh] Termos MeSH primário: Colo/metabolismo
Células Epiteliais/metabolismo
Mucina-2/genética
NF-kappa B/genética
RNA Mensageiro/genética
Proteína Amiloide A Sérica/genética
Regulação para Cima/genética
[Mh] Termos MeSH secundário: Proteínas Amiloidogênicas/genética
Proteínas Amiloidogênicas/metabolismo
Amiloidose/genética
Amiloidose/metabolismo
Animais
Sequência de Bases
Linhagem Celular
Citocinas/genética
Citocinas/metabolismo
Camundongos
Mucina-2/metabolismo
NF-kappa B/metabolismo
Alinhamento de Sequência
Proteína Amiloide A Sérica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloidogenic Proteins); 0 (Cytokines); 0 (Muc2 protein, mouse); 0 (Mucin-2); 0 (NF-kappa B); 0 (RNA, Messenger); 0 (Serum Amyloid A Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181796


  8 / 3538 MEDLINE  
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[PMID]:28708859
[Au] Autor:Couderc E; Morel F; Levillain P; Buffière-Morgado A; Camus M; Paquier C; Bodet C; Jégou JF; Pohin M; Favot L; Garcia M; Huguier V; Mcheik J; Lacombe C; Yssel H; Guillet G; Bernard FX; Lecron JC
[Ad] Endereço:Laboratoire Inflammation, Tissus Epithéliaux et Cytokines, UPRES EA4331, Pôle Biologie Santé, Université de Poitiers, TSA, POITIERS, France.
[Ti] Título:Interleukin-17A-induced production of acute serum amyloid A by keratinocytes contributes to psoriasis pathogenesis.
[So] Source:PLoS One;12(7):e0181486, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Acute-serum Amyloid A (A-SAA), one of the major acute-phase proteins, is mainly produced in the liver but extra-hepatic synthesis involving the skin has been reported. Its expression is regulated by the transcription factors NF-κB, C/EBPß, STAT3 activated by proinflammatory cytokines. OBJECTIVES: We investigated A-SAA synthesis by resting and cytokine-activated Normal Human Epidermal Keratinocytes (NHEK), and their inflammatory response to A-SAA stimulation. A-SAA expression was also studied in mouse skin and liver in a model mimicking psoriasis and in the skin and sera of psoriatic and atopic dermatitis (AD) patients. METHODS: NHEK were stimulated by A-SAA or the cytokines IL-1α, IL-17A, IL-22, OSM, TNF-α alone or in combination, previously reported to reproduce features of psoriasis. Murine skins were treated by imiquimod cream. Human skins and sera were obtained from patients with psoriasis and AD. A-SAA mRNA was quantified by RT qPCR. A-SAA proteins were dosed by ELISA or immunonephelemetry assay. RESULTS: IL-1α, TNF-α and mainly IL-17A induced A-SAA expression by NHEK. A-SAA induced its own production and the synthesis of hBD2 and CCL20, both ligands for CCR6, a chemokine receptor involved in the trafficking of Th17 lymphocytes. A-SAA expression was increased in skins and livers from imiquimod-treated mice and in patient skins with psoriasis, but not significantly in those with AD. Correlations between A-SAA and psoriasis severity and duration were observed. CONCLUSION: Keratinocytes could contribute to psoriasis pathogenesis via A-SAA production, maintaining a cutaneous inflammatory environment, activating innate immunity and Th17 lymphocyte recruitment.
[Mh] Termos MeSH primário: Dermatite Atópica/patologia
Interleucina-17/farmacologia
Psoríase/patologia
Proteína Amiloide A Sérica/metabolismo
Pele/efeitos dos fármacos
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adulto
Idoso
Aminoquinolinas/farmacologia
Animais
Células Cultivadas
Quimiocina CCL20/metabolismo
Quimiocina CCL20/farmacologia
Citocinas/genética
Citocinas/metabolismo
Dermatite Atópica/metabolismo
Modelos Animais de Doenças
Feminino
Seres Humanos
Interleucina-17/genética
Interleucina-17/metabolismo
Queratinócitos/citologia
Queratinócitos/efeitos dos fármacos
Queratinócitos/metabolismo
Fígado/efeitos dos fármacos
Fígado/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Meia-Idade
Psoríase/metabolismo
Receptores CCR6/metabolismo
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/farmacologia
Proteína Amiloide A Sérica/análise
Proteína Amiloide A Sérica/genética
Pele/metabolismo
Células Th17/citologia
Células Th17/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoquinolines); 0 (Chemokine CCL20); 0 (Cytokines); 0 (Interleukin-17); 0 (Receptors, CCR6); 0 (Recombinant Proteins); 0 (Serum Amyloid A Protein); P1QW714R7M (imiquimod)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181486


  9 / 3538 MEDLINE  
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[PMID]:28674180
[Au] Autor:Zhou H; Chen M; Zhang G; Ye RD
[Ad] Endereço:Engineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, School of Pharmacy, Shanghai Jiao Tong University, Shanghai 200240, China; and.
[Ti] Título:Suppression of Lipopolysaccharide-Induced Inflammatory Response by Fragments from Serum Amyloid A.
[So] Source:J Immunol;199(3):1105-1112, 2017 Aug 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serum amyloid A (SAA) is known as an acute-phase protein and a biomarker for inflammatory diseases. Published studies have shown that SAA possesses proinflammatory cytokine-like activity and is chemotactic for phagocytes, but the structural basis for these activities remains unidentified. In this article, we report that truncated SAA1 proteins lacking N- and C-terminal sequences exhibit reduced proinflammatory activity and strongly suppress LPS-induced expression of IL-1ß, IL-6, and TNF-α in macrophages. A truncated SAA1 containing aa 11-58 was examined further and found to facilitate p38 MAPK phosphorylation while reducing LPS-stimulated phosphorylation of ERK and JNK. In LPS-challenged mice, aa 11-58 reduced the severity of acute lung injury, with significantly less neutrophil infiltration in the lungs and attenuated pulmonary expression of IL-1ß, IL-6, and TNF-α. Coadministration of aa 11-58 markedly improved mouse survival in response to a lethal dose of LPS. A potent induction of IL-10 was observed in a TLR2-dependent, but TLR4-independent, manner in macrophages stimulated with aa 11-58. However, the aa 11-58 fragment of SAA1 was unable to induce chemotaxis or calcium flux through formyl peptide receptor 2. These results indicate that the N- and C-terminal sequences contain structural determinants for the proinflammatory and chemotactic activities of SAA1, and their removal switches SAA1 to an anti-inflammatory role. Given that proteolytic processing of SAA is associated with the pathological changes in several diseases, including secondary amyloidosis, our findings may shed light on the structure-function relationship of SAA1 with respect to its role in inflammation.
[Mh] Termos MeSH primário: Inflamação/imunologia
Lipopolissacarídeos/imunologia
Macrófagos/imunologia
Proteína Amiloide A Sérica/química
Proteína Amiloide A Sérica/imunologia
[Mh] Termos MeSH secundário: Animais
Quimiotaxia/efeitos dos fármacos
Interleucina-10/biossíntese
Interleucina-10/genética
Interleucina-10/imunologia
Interleucina-1beta/biossíntese
Interleucina-1beta/genética
Interleucina-1beta/imunologia
Interleucina-6/biossíntese
Interleucina-6/genética
Interleucina-6/imunologia
Lipopolissacarídeos/administração & dosagem
Camundongos
Receptores de Formil Peptídeo/imunologia
Receptores de Formil Peptídeo/metabolismo
Proteína Amiloide A Sérica/metabolismo
Proteína Amiloide A Sérica/farmacologia
Transdução de Sinais
Receptor 2 Toll-Like/imunologia
Receptor 3 Toll-Like/imunologia
Fator de Necrose Tumoral alfa/biossíntese
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL10 protein, mouse); 0 (Interleukin-1beta); 0 (Interleukin-6); 0 (Lipopolysaccharides); 0 (Receptors, Formyl Peptide); 0 (Serum Amyloid A Protein); 0 (TLR3 protein, mouse); 0 (Tlr2 protein, mouse); 0 (Toll-Like Receptor 2); 0 (Toll-Like Receptor 3); 0 (Tumor Necrosis Factor-alpha); 0 (formyl peptide receptor 2, mouse); 0 (interleukin-6, mouse); 130068-27-8 (Interleukin-10)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700470


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[PMID]:28544777
[Au] Autor:Flores RJ; Kelly AJ; Li Y; Chen X; McGee C; Krailo M; Barkauskas DA; Hicks J; Man TK
[Ad] Endereço:Texas Children's Cancer and Hematology Centers, Texas Children's Hospital, Houston, Texas.
[Ti] Título:The prognostic significance of circulating serum amyloid A and CXC chemokine ligand 4 in osteosarcoma.
[So] Source:Pediatr Blood Cancer;64(12), 2017 Dec.
[Is] ISSN:1545-5017
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Osteosarcoma (OS) is the most common pediatric bone cancer.  Despite advances in treatment regimens, the survival rate remains 60-70%.  There is an urgent need to identify prognostic biomarkers, so that targeted therapies can be developed to improve the outcome. PROCEDURE: Our laboratory has previously identified that circulating serum amyloid A (SAA) and CXC chemokine ligand 4 (CXCL4) are upregulated in patients with OS.  In this study, we tested if they could be used as prognostic biomarkers.  We used enzyme-linked immunosorbent assays to measure their concentrations in serum samples (n = 233) and immunohistochemistry to examine their expressions in primary tumors (n = 37).  Prognostic significance of the serum concentrations and tumor expressions of the biomarkers was then evaluated. RESULTS: Patients with "high SAA" and "low CXCL4" circulating levels at diagnosis significantly correlated with a worse outcome (HR = 1.68, P = 0.014), which was independent of the metastatic status.  These patients also exhibited a significantly higher rate of poor histologic response to chemotherapy.  Furthermore, low tumor expression of CXCL4 correlated with poor survival (HR = 3.57, P = 0.005). CONCLUSIONS: Our results demonstrate that circulating SAA and CXCL4 may serve as prognostic biomarkers in OS.  Targeting CXCL4 has been reported, suggesting that it may be exploited as a therapeutic target in OS.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/sangue
Neoplasias Ósseas/mortalidade
Osteossarcoma/mortalidade
Fator Plaquetário 4/sangue
Proteína Amiloide A Sérica/análise
[Mh] Termos MeSH secundário: Adolescente
Adulto
Neoplasias Ósseas/sangue
Neoplasias Ósseas/diagnóstico
Criança
Pré-Escolar
Seres Humanos
Osteossarcoma/sangue
Osteossarcoma/diagnóstico
Prognóstico
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Serum Amyloid A Protein); 37270-94-3 (Platelet Factor 4)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1002/pbc.26659



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