Base de dados : MEDLINE
Pesquisa : D12.776.215 [Categoria DeCS]
Referências encontradas : 2578 [refinar]
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[PMID]:28792192
[Au] Autor:Benli E; Ayyildiz SN; Cirrik S; Noyan T; Ayyildiz A; Cirakoglu A
[Ad] Endereço:Department of Urology, Faculty of Medicine, Ordu University, Ordu, Turkey.
[Ti] Título:Early term effect of ureterorenoscopy (URS) on the Kidney: research measuring NGAL, KIM-1, FABP and CYS C levels in urine.
[So] Source:Int Braz J Urol;43(5):887-895, 2017 Sep-Oct.
[Is] ISSN:1677-6119
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:AIM: URS is a very commonly used procedure for treatment of ureter stones. Increased hydrostatic pressure in the collecting system linked to fluids used during the procedure may cause harmful effects on the kidney. The aim of this study is to determine whether the URS procedure has a negative effect on the kidney by investigating NGAL, KIM-1, FABP and Cys C levels in urine. MATERIAL AND METHODS: This study included 30 patients undergoing ureterorenoscopy (URS) for ureter stones. Urine samples were collected 5 times; before the URS procedure (control) and at 1, 3, 5 and 12 hours following the procedure. NGAL, KIM-1, FBAP and Cys C levels were measured in urine and compared with the control values. RESULTS: The NGAL levels in urine before the procedure and at 1, 3, 5 and 12 hours after the procedure were 34.59±35.34; 62.72±142.32; 47.15±104.48; 45.23±163.16 and 44.99±60.79ng/mL, respectively (p=0.001). Similarly, the urinary KIM-1, FABP and Cys C levels were found to increase compared to control values; however this increase did not reach statistical significance (p >0.05). CONCLUSIONS: After the URS procedure, there were important changes in NGAL, FABP, KIM-1 and Cys C levels. These changes reached statistical significance for NGAL, but did not reach significance for the other parameters. In conclusion, the URS procedure significantly affects the kidney; however, this effect disappears over time.
[Mh] Termos MeSH primário: Biomarcadores/urina
Cálculos Ureterais/cirurgia
Cálculos Ureterais/urina
Ureteroscopia/métodos
[Mh] Termos MeSH secundário: Adulto
Idoso
Cistatinas/urina
Proteínas de Ligação a Ácido Graxo/urina
Feminino
Receptor Celular 1 do Vírus da Hepatite A/análise
Seres Humanos
Lipocalina-2/urina
Masculino
Meia-Idade
Ureteroscopia/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Cystatins); 0 (FABP1 protein, human); 0 (Fatty Acid-Binding Proteins); 0 (HAVCR1 protein, human); 0 (Hepatitis A Virus Cellular Receptor 1); 0 (Lipocalin-2)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1590/S1677-5538.IBJU.2016.0638


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[PMID]:28654769
[Au] Autor:Prabucka B; Mielecki M; Chojnacka M; Bielawski W; Czarnocki-Cieciura M; Orzechowski S
[Ad] Endereço:Department of Biochemistry, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159, 02-776 Warsaw, Poland. Electronic address: beata_prabucka@sggw.pl.
[Ti] Título:Structural and functional characterization of the triticale (x Triticosecale Wittm.) phytocystatin TrcC-8 and its dimerization-dependent inhibitory activity.
[So] Source:Phytochemistry;142:1-10, 2017 Oct.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phytocystatins are a group of proteins with significant potential to regulate activities of cysteine proteinases of native and pest/pathogen origins. The two-domain triticale (x Triticosecale Wittm.) phytocystatin TrcC-8 was characterized in this study. This protein belongs to the second group of phytocystatins and contains all the conserved sequences and motifs as well as both N-terminal (CY) and C-terminal (CY-L) domains that are characteristic of phytocystatins with the C-terminal extension. We demonstrated that TrcC-8 forms stable dimers with a significantly reduced inhibitory activity against papain compared to the activity of monomers, indicating the regulatory nature of the oligomerization. Moreover, according to our research, only the N-terminal domain possesses the ability to form dimers, indicating that this part of TrcC-8 is involved in the dimerization of the full-length protein. Homology modelling of TrcC-8 strongly suggests distinct specificities for the CY and CY-L domains, confirmed in experiments with inhibition of the papain. Our results suggest that the CY domain of TrcC-8 may, although markedly weakly and suboptimally, interact with papain in an analogous mode to tarocystatin, while the CY-L domain of TrcC-8 has distinct specificity than tarocystatin.
[Mh] Termos MeSH primário: Cisteína Proteases/metabolismo
Papaína/metabolismo
Proteínas de Plantas/química
Triticale/química
[Mh] Termos MeSH secundário: Cistatinas/química
Cistatinas/metabolismo
Dimerização
Proteínas de Plantas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cystatins); 0 (Plant Proteins); EC 3.4.- (Cysteine Proteases); EC 3.4.22.2 (Papain)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE


  3 / 2578 MEDLINE  
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[PMID]:28630039
[Au] Autor:Wallin H; Apelqvist J; Andersson F; Ekström U; Abrahamson M
[Ad] Endereço:From the Department of Laboratory Medicine, Lund University, SE-221 85 Lund, Sweden.
[Ti] Título:Low-level internalization of cystatin E/M affects legumain activity and migration of melanoma cells.
[So] Source:J Biol Chem;292(35):14413-14424, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ratio between proteases and their inhibitors is unbalanced in cancer. The cysteine protease inhibitor cystatin C is internalized by some cancer cells, which affects cellular properties. Here we aimed to investigate if uptake of cystatin C and the related inhibitor cystatin E/M occur in melanoma cell lines and to evaluate to what extent the uptake affects the legumain activity that is typically increased in melanoma. First we studied the basic expression, secretion, and intracellular content of all type 2 cystatins as well as expression and activity of their possible target enzymes legumain and cathepsin B in MDA-MB-435S, A375, and C8161 melanoma cells. Legumain activity was measureable in all cell lines, and of the potential legumain inhibitors, cystatin C, E/M, and F, cystatin C was the one mainly produced. All cells internalized cystatin C added to culture media, leading to increased intracellular cystatin C levels by 120-200%. Cystatin E/M was internalized as well but at a modest rate. The effects on intracellular legumain activity were nevertheless pronounced, probably because the cells lacked this inhibitor, and its affinity for legumain is 100-fold higher than that of cystatin C. Likewise, the low-degree uptake resulted in reduced migration and invasion of A375 cells in Matrigel to an extent comparable with the W106F variant of cystatin C with optimal uptake properties and resulting in much higher intracellular levels. Thus, cystatin E/M appears to be a good candidate to efficiently down-regulate the increased legumain activity, possibly important for the malignant phenotype of melanoma cells.
[Mh] Termos MeSH primário: Absorção Fisiológica
Cistatina C/metabolismo
Cistatina M/metabolismo
Cisteína Endopeptidases/metabolismo
Regulação Neoplásica da Expressão Gênica
Melanoma/metabolismo
Proteínas de Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Biomarcadores Tumorais/genética
Biomarcadores Tumorais/metabolismo
Biomarcadores Tumorais/secreção
Catepsina B/genética
Catepsina B/metabolismo
Linhagem Celular Tumoral
Movimento Celular
Cistatina C/genética
Cistatina C/secreção
Cistatina M/genética
Cistatina M/secreção
Cistatinas/genética
Cistatinas/metabolismo
Cistatinas/secreção
Cisteína Endopeptidases/química
Cisteína Endopeptidases/genética
Corantes Fluorescentes/química
Seres Humanos
Cinética
Melanoma/patologia
Melanoma/secreção
Mutação
Invasividade Neoplásica/patologia
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/genética
Proteínas de Neoplasias/secreção
Transporte Proteico
Proteólise
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/secreção
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CST3 protein, human); 0 (CST6 protein, human); 0 (CST7 protein, human); 0 (Cystatin C); 0 (Cystatin M); 0 (Cystatins); 0 (Fluorescent Dyes); 0 (Neoplasm Proteins); 0 (Recombinant Proteins); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.1 (CTSB protein, human); EC 3.4.22.1 (Cathepsin B); EC 3.4.22.34 (asparaginylendopeptidase)
[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:170621
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.776138


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[PMID]:28605601
[Au] Autor:Santiago AC; Khan ZN; Miguel MC; Gironda CC; Soares-Costa A; Pelá VT; Leite AL; Edwardson JM; Buzalaf MAR; Henrique-Silva F
[Ad] Endereço:1 Laboratory of Molecular Biology, Department of Genetics and Evolution, Federal University of São Carlos, São Carlos, Brazil.
[Ti] Título:A New Sugarcane Cystatin Strongly Binds to Dental Enamel and Reduces Erosion.
[So] Source:J Dent Res;96(9):1051-1057, 2017 Aug.
[Is] ISSN:1544-0591
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cystatin B was recently identified as an acid-resistant protein in acquired enamel pellicle; it could therefore be included in oral products to protect against caries and erosion. However, human recombinant cystatin is very expensive, and alternatives to its use are necessary. Phytocystatins are reversible inhibitors of cysteine peptidases that are found naturally in plants. In plants, they have several biological and physiological functions, such as the regulation of endogenous processes, defense against pathogens, and response to abiotic stress. Previous studies performed by our research group have reported high inhibitory activity and potential agricultural and medical applications of several sugarcane cystatins, including CaneCPI-1, CaneCPI-2, CaneCPI-3, and CaneCPI-4. In the present study, we report the characterization of a novel sugarcane cystatin, named CaneCPI-5. This cystatin was efficiently expressed in Escherichia coli, and inhibitory assays demonstrated that it was a potent inhibitor of human cathepsins B, K, and L ( K = 6.87, 0.49, and 0.34 nM, respectively). The ability of CaneCPI-5 to bind to dental enamel was evaluated using atomic force microscopy. Its capacity to protect against initial enamel erosion was also tested in vitro via changes in surface hardness. CaneCPI-5 showed a very large force of interaction with enamel (e.g., compared with mucin and casein) and significantly reduced initial enamel erosion. These results suggest that the inclusion of CaneCPIs in dental products might confer protection against enamel erosion.
[Mh] Termos MeSH primário: Cistatinas/farmacologia
Esmalte Dentário/efeitos dos fármacos
Saccharum
Erosão Dentária/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Catepsinas/metabolismo
Bovinos
Escherichia coli
Técnicas In Vitro
Incisivo
Microscopia de Força Atômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cystatins); EC 3.4.- (Cathepsins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE
[do] DOI:10.1177/0022034517712981


  5 / 2578 MEDLINE  
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[PMID]:28295446
[Au] Autor:Coronado S; Barrios L; Zakzuk J; Regino R; Ahumada V; Franco L; Ocampo Y; Caraballo L
[Ad] Endereço:Institute for Immunological Research, Universidad de Cartagena, Cartagena, Colombia.
[Ti] Título:A recombinant cystatin from Ascaris lumbricoides attenuates inflammation of DSS-induced colitis.
[So] Source:Parasite Immunol;39(4), 2017 Apr.
[Is] ISSN:1365-3024
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Helminthiasis may ameliorate inflammatory diseases, such as inflammatory bowel disease and asthma. Information about immunomodulators from Ascaris lumbricoides is scarce, but could be important considering the co-evolutionary relationships between helminths and humans. We evaluated the immunomodulatory effects of a recombinant cystatin from A. lumbricoides on an acute model of dextran sodium sulphate (DSS)-induced colitis in mice. From an A. lumbricoides cDNA library, we obtained a recombinant cystatin (rAl-CPI). Protease activity inhibition was demonstrated on cathepsin B and papain. Immunomodulatory effects were evaluated at two intraperitoneal doses (0.5 and 0.25 µg/G) on mice with DSS-induced colitis. Body weight, colon length, Disease Activity Index (DAI), histological inflammation score, myeloperoxidase (MPO) activity, gene expression of cytokines and cytokines levels in colon tissue were analysed. Treatment with rAl-CPI significantly reduced DAI, MPO activity and inflammation score without toxic effects. Also, IL-10 and TGF-B gene overexpression was observed in rAl-CPI-treated group compared to DSS-exposed control and healthy mice. Furthermore, a reduction in IL-6 and TNF-A expression was found, and this was confirmed by the levels of these cytokines in colonic tissue. In conclusion, rAl-CPI reduces inflammation in a mouse model of DSS-induced colitis, probably by increasing the expression of anti-inflammatory cytokines and reducing pro-inflammatory ones.
[Mh] Termos MeSH primário: Colite/imunologia
Colite/terapia
Cistatinas/administração & dosagem
Imunossupressores/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Ascaris lumbricoides/genética
Colite/induzido quimicamente
Colite/patologia
Colo/metabolismo
Cistatinas/genética
Cistatinas/imunologia
Citocinas/análise
Sulfato de Dextrana
Modelos Animais de Doenças
Feminino
Seres Humanos
Imunossupressores/imunologia
Inflamação/patologia
Camundongos
Camundongos Endogâmicos BALB C
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cystatins); 0 (Cytokines); 0 (Immunosuppressive Agents); 0 (Recombinant Proteins); 9042-14-2 (Dextran Sulfate)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1111/pim.12425


  6 / 2578 MEDLINE  
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[PMID]:28251676
[Au] Autor:Shimizu T; Wisessmith W; Li J; Abe M; Sakimura K; Chetsawang B; Sahara Y; Tohyama K; Tanaka KF; Ikenaka K
[Ad] Endereço:Division of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Okazaki, Japan.
[Ti] Título:The balance between cathepsin C and cystatin F controls remyelination in the brain of Plp1-overexpressing mouse, a chronic demyelinating disease model.
[So] Source:Glia;65(6):917-930, 2017 Jun.
[Is] ISSN:1098-1136
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In demyelinating diseases such as multiple sclerosis (MS), an imbalance between the demyelination and remyelination rates underlies the degenerative processes. Microglial activation is observed in demyelinating lesions; however, the molecular mechanism responsible for the homeostatic/environmental change remains elusive. We previously found that cystatin F (CysF), a cysteine protease inhibitor, is selectively expressed in microglia only in actively demyelinating/remyelinating lesions but ceases expression in chronic lesions, suggesting its role in remyelination. Here, we report the effects of manipulating the expression of CysF and cathepsin C (CatC), a key target of CysF, in a murine model of transgenic demyelinating disease, Plp . During the active remyelinating phase, both CysF knockdown (CysFKD) and microglial-selective CatC overexpression (CatCOE) showed a worsening of the demyelination in Plp transgenic mice. Conversely, during the chronic demyelinating phase, CatC knockdown (CatCKD) ameliorated the demyelination. Our results suggest that the balance between CatC and CysF expression controls the demyelination and remyelination process.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Catepsina C/metabolismo
Cistatinas/metabolismo
Doenças Desmielinizantes/metabolismo
Bainha de Mielina/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/patologia
Proteínas de Ligação ao Cálcio/metabolismo
Catepsina C/genética
Células Cultivadas
Cistatinas/genética
Doenças Desmielinizantes/patologia
Modelos Animais de Doenças
Progressão da Doença
Marcação de Genes
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Proteínas dos Microfilamentos/metabolismo
Microglia/metabolismo
Microglia/patologia
Proteína Proteolipídica de Mielina/genética
Proteína Proteolipídica de Mielina/metabolismo
Bainha de Mielina/patologia
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aif1 protein, mouse); 0 (Calcium-Binding Proteins); 0 (Cystatins); 0 (Microfilament Proteins); 0 (Myelin Proteolipid Protein); 0 (Plp1 protein, mouse); 0 (RNA, Messenger); 0 (cystatin F, mouse); EC 3.4.14.1 (Cathepsin C); EC 3.4.14.1 (Ctsc protein, mouse)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE
[do] DOI:10.1002/glia.23134


  7 / 2578 MEDLINE  
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[PMID]:28214581
[Au] Autor:Ahmed A; Shamsi A; Bano B
[Ad] Endereço:Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, 202002, India.
[Ti] Título:Oxadiargyl induced conformational transition of cystatin isolated from yellow mustard seeds: Biophysical and biochemical approach.
[So] Source:Int J Biol Macromol;98:802-809, 2017 May.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Phytocystatins are thiol proteinase inhibitors crucial due to their inhibitory activity in plants. These play important roles in improving crop yield, protection against insects and pathogens and modulation of apoptosis. In this chemical era, various pesticides are being used globally to increase the crop biomass. These pesticides accumulate in plant body and produce harmful effects on plants itself by interacting with essential proteins. In this present study, we have monitored the interaction of a herbicide; oxadiargyl, with phytocystatin isolated from yellow mustard seeds (YMP) by employing spectroscopic techniques viz. UV, fluorescence, FTIR and CD spectroscopy and Isothermal titration calorimetry (ITC). UV and fluorescence spectroscopy shows YMP transformation from native to non-native form apparent by decreased absorbance and decreased fluorescence. FTIR and CD spectroscopy further confirmed secondary structural disruption of YMP. Anti-papain activity assay was also carried out; a reduction in activity was observed in presence of oxadiargyl. Thermodynamic parameters obtained from ITC and stern-volmer plot shows affinity of oxadiargyl towards phytocystatin. Oxadiargyl was also found to induce ROS generation in YMP as evident by DNPH assay. Thus oxadiargyl binds to phytocystatin causing structural alterations reducing its physiological benefits and altering its functionality and ultimately leading to reduced crop yield.
[Mh] Termos MeSH primário: Cistatinas/química
Conformação Molecular/efeitos dos fármacos
Mostardeira/química
Oxidiazóis/química
[Mh] Termos MeSH secundário: Fenômenos Biofísicos
Oxidiazóis/farmacologia
Sementes/química
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cystatins); 0 (Oxadiazoles); F33159G4WG (oxadiargyl)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170324
[Lr] Data última revisão:
170324
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170220
[St] Status:MEDLINE


  8 / 2578 MEDLINE  
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[PMID]:28185933
[Au] Autor:Siddiqui AA; Feroz A; Khaki PS; Bano B
[Ad] Endereço:Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, U.P., India.
[Ti] Título:Binding of λ-carrageenan (a food additive) to almond cystatin: An insight involving spectroscopic and thermodynamic approach.
[So] Source:Int J Biol Macromol;98:684-690, 2017 May.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Carrageenan is a high molecular weight linear sulphated polysaccharide, primarily used in food industry as gelling, thickening, and stabilizing agent. Almond milk prepared from almonds is low in fat, but high in antioxidants, energy, proteins, lipids and fibre. Purified almond cystatin was incubated with increasing concentrations of carrageenan at 25°C for different time interval and significant loss in inhibitory activity was observed. Interaction between carrageenan and cystatin resulted in complex formation as depicted by the decrease in fluorescence intensity with increase in the concentration of carrageenan. Stern-volmer analysis of fluorescence quenching data showed binding constant to be 1.84±0.20×10 M and number of binding sites close to unity. These results were further confirmed by supporting results obtained in UV-vis spectroscopy. FTIR analysis shows significant shift in the peak intensity and this change clearly depict change in the structure of cystatin from that of α helix to ß-sheet. CD spectra further confirmed the structural transition of the cystatin from α helix to ß-sheet structure on interaction with increased concentrations of carrageenan. The contributing thermodynamic parameters were determined by ITC. The negative ΔH° and positive TΔS° values suggest involvement of electrostatic forces and hydrophobic interaction in the formation of the λ-carrageenan-cystatin complex.
[Mh] Termos MeSH primário: Carragenina/química
Cistatinas/química
Aditivos Alimentares/química
[Mh] Termos MeSH secundário: Antioxidantes/química
Sítios de Ligação
Carragenina/síntese química
Dicroísmo Circular
Cistatinas/síntese química
Aditivos Alimentares/síntese química
Prunus dulcis/química
Espectrometria de Fluorescência
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Cystatins); 0 (Food Additives); 9000-07-1 (Carrageenan)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170324
[Lr] Data última revisão:
170324
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE


  9 / 2578 MEDLINE  
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[PMID]:28178353
[Au] Autor:Nuvolone M; Schmid N; Miele G; Sorce S; Moos R; Schori C; Beerli RR; Bauer M; Saudan P; Dietmeier K; Lachmann I; Linnebank M; Martin R; Kallweit U; Kana V; Rushing EJ; Budka H; Aguzzi A
[Ad] Endereço:Institute of Neuropathology, University Hospital of Zurich, Zurich, Switzerland.
[Ti] Título:Cystatin F is a biomarker of prion pathogenesis in mice.
[So] Source:PLoS One;12(2):e0171923, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases. Experimental and epidemiological evidence point toward a protracted, clinically silent phase in prion diseases, yet there is no diagnostic test capable of identifying asymptomatic individuals incubating prions. In an effort to identify early biomarkers of prion diseases, we have compared global transcriptional profiles in brains from pre-symptomatic prion-infected mice and controls. We identified Cst7, which encodes cystatin F, as the most strongly upregulated transcript in this model. Early and robust upregulation of Cst7 mRNA levels and of its cognate protein was validated in additional mouse models of prion disease. Surprisingly, we found no significant increase in cystatin F levels in both cerebrospinal fluid or brain parenchyma of patients with Creutzfeldt-Jakob disease compared to Alzheimer's disease or non-demented controls. Our results validate cystatin F as a useful biomarker of early pathogenesis in experimental models of prion disease, and point to unexpected species-specific differences in the transcriptional responses to prion infections.
[Mh] Termos MeSH primário: Cistatinas/metabolismo
Doenças Priônicas/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores
Encéfalo/metabolismo
Encéfalo/patologia
Cistatinas/líquido cefalorraquidiano
Cistatinas/genética
Ensaio de Imunoadsorção Enzimática
Expressão Gênica
Perfilação da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Masculino
Camundongos
Doenças Priônicas/líquido cefalorraquidiano
Doenças Priônicas/genética
Doenças Priônicas/patologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Cystatins); 0 (RNA, Messenger); 0 (cystatin F, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0171923


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[PMID]:28174118
[Au] Autor:Rangel CK; Parizi LF; Sabadin GA; Costa EP; Romeiro NC; Isezaki M; Githaka NW; Seixas A; Logullo C; Konnai S; Ohashi K; da Silva Vaz I
[Ad] Endereço:Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Avenida Bento Gonçalves, 9500, Prédio 43421, Porto Alegre 91501-970, RS, Brazil.
[Ti] Título:Molecular and structural characterization of novel cystatins from the taiga tick Ixodes persulcatus.
[So] Source:Ticks Tick Borne Dis;8(3):432-441, 2017 Mar.
[Is] ISSN:1877-9603
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cystatins are cysteine peptidase inhibitors that in ticks mediate processes such as blood feeding and digestion. The ixodid tick Ixodes persulcatus is endemic to the Eurasia, where it is the principal vector of Lyme borreliosis. To date, no I. persulcatus cystatin has been characterized. In the present work, we describe three novel cystatins from I. persulcatus, named JpIpcys2a, JpIpcys2b and JpIpcys2c. In addition, the potential of tick cystatins as cross-protective antigens was evaluated by vaccination of hamsters using BrBmcys2c, a cystatin from Rhipicephalus microplus, against I. persulcatus infestation. Sequence analysis showed that motifs that are characteristic of cystatins type 2 are fully conserved in JpIpcys2b, while mutations are present in both JpIpcys2a and JpIpcys2c. Protein-protein docking simulations further revealed that JpIpcys2a, JpIpcys2b and JpIpcys2c showed conserved binding sites to human cathepsins L, all of them covering the active site cleft. Cystatin transcripts were detected in different I. persulcatus tissues and instars, showing their ubiquitous expression during I. persulcatus development. Serological analysis showed that although hamsters immunized with BrBmcys2c developed a humoral immune response, this response was not adequate to protect against a heterologous challenge with I. persulcatus adult ticks. The lack of cross-protection provided by BrBmcys2c immunization is perhaps linked to the fact that cystatins cluster into multigene protein families that are expressed differentially and exhibit functional redundancy. How to target such small proteins that are secreted in low quantities remains a challenge in the development of suitable anti-tick vaccine antigens.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/química
Proteínas de Artrópodes/genética
Cistatinas/química
Cistatinas/genética
Ixodes/metabolismo
Infestações por Carrapato/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Anticorpos/sangue
Anticorpos/imunologia
Proteínas de Artrópodes/imunologia
Proteínas de Artrópodes/isolamento & purificação
Sítios de Ligação
Catepsina L/química
Cricetinae
Seres Humanos
Imunidade Humoral
Ixodes/imunologia
Modelos Moleculares
Simulação de Acoplamento Molecular
Família Multigênica
Filogenia
Reação em Cadeia da Polimerase em Tempo Real
Rhipicephalus/metabolismo
Alinhamento de Sequência
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Arthropod Proteins); 0 (Cystatins); EC 3.4.22.15 (Cathepsin L)
[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:170209
[St] Status:MEDLINE



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