Base de dados : MEDLINE
Pesquisa : D08.811.277.656.262.500.350 [Categoria DeCS]
Referências encontradas : 144 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 15 ir para página                         

  1 / 144 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29072706
[Au] Autor:Schopper S; Kahraman A; Leuenberger P; Feng Y; Piazza I; Müller O; Boersema PJ; Picotti P
[Ad] Endereço:Institute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
[Ti] Título:Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry.
[So] Source:Nat Protoc;12(11):2391-2410, 2017 Nov.
[Is] ISSN:1750-2799
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein structural changes induced by external perturbations or internal cues can profoundly influence protein activity and thus modulate cellular physiology. A number of biophysical approaches are available to probe protein structural changes, but these are not applicable to a whole proteome in a biological extract. Limited proteolysis-coupled mass spectrometry (LiP-MS) is a recently developed proteomics approach that enables the identification of protein structural changes directly in their complex biological context on a proteome-wide scale. After perturbations of interest, proteome extracts are subjected to a double-protease digestion step with a nonspecific protease applied under native conditions, followed by complete digestion with the sequence-specific protease trypsin under denaturing conditions. This sequential treatment generates structure-specific peptides amenable to bottom-up MS analysis. Next, a proteomics workflow involving shotgun or targeted MS and label-free quantification is applied to measure structure-dependent proteolytic patterns directly in the proteome extract. Possible applications of LiP-MS include discovery of perturbation-induced protein structural alterations, identification of drug targets, detection of disease-associated protein structural states, and analysis of protein aggregates directly in biological samples. The approach also enables identification of the specific protein regions involved in the structural transition or affected by the binding event. Sample preparation takes approximately 2 d, followed by one to several days of MS and data analysis time, depending on the number of samples analyzed. Scientists with basic biochemistry training can implement the sample preparation steps. MS measurement and data analysis require a background in proteomics.
[Mh] Termos MeSH primário: Proteólise
Proteoma/análise
Proteômica/métodos
Espectrometria de Massas em Tandem/métodos
[Mh] Termos MeSH secundário: Biomarcadores/análise
Misturas Complexas/química
Desenho de Drogas
Endopeptidase K/química
Ficina/química
Células HeLa
Seres Humanos
Pronase/química
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteoma/química
Proteômica/instrumentação
Controle de Qualidade
Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/metabolismo
Termolisina/química
Tripsina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Complex Mixtures); 0 (Proteome); EC 3.4.21.4 (Trypsin); EC 3.4.21.64 (Endopeptidase K); EC 3.4.22.3 (Ficain); EC 3.4.24.- (Pronase); EC 3.4.24.27 (Thermolysin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171027
[St] Status:MEDLINE
[do] DOI:10.1038/nprot.2017.100


  2 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26751400
[Au] Autor:Shamsi A; Ahmed A; Bano B
[Ad] Endereço:Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.
[Ti] Título:Biochemical, immunological and kinetic characterization and partial sequence analysis of a thiol proteinase inhibitor from Bubalus bubalis kidney: An attempt targeting kidney disorders.
[So] Source:Int J Biol Macromol;94(Pt B):819-826, 2017 Jan.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In the present study a thiol proteinase inhibitor was isolated from buffalo kidney making use of ammonium sulphate precipitation and gel filtration chromatography on Sephacryl S-100HR column. Purified inhibitor is homogeneous as it displayed a single band in gel electrophoresis both under reducing and non-reducing environment and is of 65KDa as revealed by gel filtration and SDS PAGE. Kinetic studies revealed the presence of reversible accompanied with competitive mode of inhibition; showing maximum efficacy against papain (K =2.90×10 ). It was maximally active at pH 8.0 and was stable for a period of 30, 60 and 90 days at 37, 4 and -20°C respectively. Immunological studies confirmed its purity of epitopes as a single precipitin line is obtained in immunodiffusion. N-terminal analysis revealed that it shared a good homology with mouse kidney cystatin as well as with Human Cys C and Cys E thereby advocating its use as a model for various human oriented studies which targets how the kidney cystatin level varies in accordance with various drugs that are currently being used as a target for variety of diseases.
[Mh] Termos MeSH primário: Cistatinas/química
Rim/química
Papaína/química
Inibidores de Proteases/química
Compostos de Sulfidrila/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bromelaínas/antagonistas & inibidores
Bromelaínas/química
Búfalos
Cistatinas/imunologia
Cistatinas/isolamento & purificação
Ficina/antagonistas & inibidores
Ficina/química
Seres Humanos
Concentração de Íons de Hidrogênio
Rim/imunologia
Cinética
Camundongos
Peso Molecular
Papaína/antagonistas & inibidores
Inibidores de Proteases/imunologia
Inibidores de Proteases/isolamento & purificação
Estabilidade Proteica
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cystatins); 0 (Protease Inhibitors); 0 (Sulfhydryl Compounds); 9001-00-7 (Bromelains); EC 3.4.22.2 (Papain); EC 3.4.22.3 (Ficain)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170320
[Lr] Data última revisão:
170320
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160112
[St] Status:MEDLINE


  3 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26748819
[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:Purification and biochemical characterization of phytocystatin from Brassica alba.
[So] Source:J Mol Recognit;29(5):223-31, 2016 May.
[Is] ISSN:1099-1352
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phytocystatins belong to the family of cysteine proteinases inhibitors. They are ubiquitously found in plants and carry out various significant physiological functions. These plant derived inhibitors are gaining wide consideration as potential candidate in engineering transgenic crops and in drug designing. Hence it is crucial to identify these inhibitors from various plant sources. In the present study a phytocystatin has been isolated and purified by a simple two-step procedure using ammonium sulfate saturation and gel filtration chromatography on Sephacryl S-100HR from Brassica alba seeds (yellow mustard seeds).The protein was purified to homogeneity with 60.3% yield and 180-fold of purification. The molecular mass of the mustard seed cystatin was estimated to be nearly 26,000 Da by sodium dodecyl sulfate polyacrylamide gel electrophoresis as well as by gel filtration chromatography. The stokes radius and diffusion coefficient of the mustard cystatin were found to be 23A° and 9.4 × 10(-7) cm(2) s(-1) respectively. The isolated phytocystatin was found to be stable in the pH range of 6-8 and is thermostable up to 60 °C. Kinetic analysis revealed that the phytocystatin exhibited non-competitive type of inhibition and inhibited papain more efficiently (K(i) = 3 × 10(-7) M) than ficin (K(i) = 6.6 × 10(-7) M) and bromelain (K(i) = 7.7 × 10(-7) M respectively). CD spectral analysis shows that it possesses 17.11% alpha helical content.
[Mh] Termos MeSH primário: Cistatinas/isolamento & purificação
Cistatinas/farmacologia
Inibidores de Cisteína Proteinase/isolamento & purificação
Inibidores de Cisteína Proteinase/farmacologia
Sinapis/metabolismo
[Mh] Termos MeSH secundário: Bromelaínas/antagonistas & inibidores
Cromatografia em Gel
Dicroísmo Circular
Cistatinas/química
Inibidores de Cisteína Proteinase/química
Ficina/antagonistas & inibidores
Peso Molecular
Papaína/antagonistas & inibidores
Proteínas de Plantas/química
Proteínas de Plantas/isolamento & purificação
Proteínas de Plantas/farmacologia
Estrutura Secundária de Proteína
Sementes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cystatins); 0 (Cysteine Proteinase Inhibitors); 0 (Plant Proteins); 9001-00-7 (Bromelains); EC 3.4.22.2 (Papain); EC 3.4.22.3 (Ficain)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160111
[St] Status:MEDLINE
[do] DOI:10.1002/jmr.2522


  4 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26718871
[Au] Autor:Zare H; Moosavi-Movahedi AA; Salami M; Sheibani N; Khajeh K; Habibi-Rezaei M
[Ad] Endereço:Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran; Estahban Fig Research Station, Fars Agricultural and Natural Resources Research and Training Center, AREEO, Shiraz, Iran.
[Ti] Título:Autolysis control and structural changes of purified ficin from Iranian fig latex with synthetic inhibitors.
[So] Source:Int J Biol Macromol;84:464-71, 2016 Mar.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The fig's ficin is a cysteine endoproteolytic enzyme, which plays fundamental roles in many plant physiological processes, and has many applications in different industries such as pharmaceutical and food. In this work, we report the inhibition and activation of autolysis and structural changes associated with reaction of ficin with iodoacetamide and tetrathionate using high-performance liquid chromatography (HPLC), ultra filtration membrane, and dynamic light scattering (DLS) methods. The ficin structural changes were also determined using UV-absorption, circular dichroism (CD), fluorescence spectroscopy, and differential scanning calorimetry (DSC) techniques. These techniques demonstrated that iodoacetamide completely inhibited ficin autolysis, which was irreversible. However, tetrathionate partially and reversibility inhibited its autolysis. The ficin structural changes with two synthetic inhibitors were associated with secondary structural changes related to decreased alpha-helix and increased beta sheet and random coil conformations, contributing to its aggregation.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/química
Ficina/química
Ficus/química
Látex/química
[Mh] Termos MeSH secundário: Varredura Diferencial de Calorimetria
Cromatografia Líquida de Alta Pressão
Dicroísmo Circular
Inibidores Enzimáticos/isolamento & purificação
Inibidores Enzimáticos/farmacologia
Ficina/isolamento & purificação
Ficina/farmacologia
Hidrólise
Agregados Proteicos
Análise Espectral/métodos
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Latex); 0 (Protein Aggregates); EC 3.4.22.3 (Ficain)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160101
[St] Status:MEDLINE


  5 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25664689
[Au] Autor:Raskovic B; Lazic J; Polovic N
[Ad] Endereço:University of Belgrade, Faculty of Chemistry, Department of Biochemistry, Studentski trg 12-16, 11000, Belgrade, Republic of Serbia.
[Ti] Título:Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening.
[So] Source:J Sci Food Agric;96(2):576-82, 2016 Jan 30.
[Is] ISSN:1097-0010
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The physiological role of fig latex is to protect the plant from pathogens. Latex is a rich source of proteases, predominantly ficin. Fig latex also contains collagenolytic protease and chitinolytic enzymes. Our aim was to investigate changes in protein composition, enzyme and antifungal activities of fig latex during fruit ripening. RESULTS: Comparison of latex samples in different time periods showed a uniform increase of protein concentration in chronological order. The content of collagenolytic protease did not differ significantly in the latex samples, while the content of ficin decreased. Ficin-specific activity towards casein was the highest at the beginning of fruit development (about 80 U mg(-1)). Specific milk clotting activity increased as well as the abundance of casein band in the clots. Specific chitinolytic activity at the beginning of flowering was 6.5 times higher than the activity in the period when fruits are ripe. Antifungal activity is the most extensive in spring. CONCLUSION: Ficin forms with different casein specificities are present in different proportions during fruit ripening, which is of importance for applications in the dairy industry. The protection mechanism against insects and fungi, which relies on chitinolytic activity, is the most important in the early phases of flowering and is replaced with other strategies over time.
[Mh] Termos MeSH primário: Ficina/análise
Ficus/química
Frutas/crescimento & desenvolvimento
Fungicidas Industriais/análise
Látex/química
Peptídeo Hidrolases/análise
[Mh] Termos MeSH secundário: Animais
Caseínas/metabolismo
Quitina/metabolismo
Ficina/metabolismo
Frutas/química
Inseticidas
Látex/farmacologia
Leite/química
Leite/metabolismo
Proteínas de Plantas/análise
Saccharomyces cerevisiae/efeitos dos fármacos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caseins); 0 (Fungicides, Industrial); 0 (Insecticides); 0 (Latex); 0 (Plant Proteins); 1398-61-4 (Chitin); EC 3.4.- (Peptide Hydrolases); EC 3.4.22.3 (Ficain)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151223
[Lr] Data última revisão:
151223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150210
[St] Status:MEDLINE
[do] DOI:10.1002/jsfa.7126


  6 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26083455
[Au] Autor:Baeyens-Volant D; Matagne A; El Mahyaoui R; Wattiez R; Azarkan M
[Ad] Endereço:Université Libre de Bruxelles, Faculty of Medicine, Protein Chemistry Unit, Campus Erasme (CP 609), 808 route de Lennik, 1070 Brussels, Belgium.
[Ti] Título:A novel form of ficin from Ficus carica latex: Purification and characterization.
[So] Source:Phytochemistry;117:154-67, 2015 Sep.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel ficin form, named ficin E, was purified from fig tree latex by a combination of cation-exchange chromatography on SP-Sepharose Fast Flow, Thiopropyl Sepharose 4B and fplc-gel filtration chromatography. The new ficin appeared not to be sensitive to thiol derivatization by a polyethylene glycol derivative, allowing its purification. The protease is homogeneous according to PAGE, SDS-PAGE, mass spectrometry, N-terminal micro-sequencing analyses and E-64 active site titration. N-terminal sequencing of the first ten residues has shown high identity with the other known ficin (iso)forms. The molecular weight was found to be (24,294±10)Da by mass spectrometry, a lower value than the apparent molecular weight observed on SDS-PAGE, around 27 kDa. Far-UV CD data revealed a secondary structure content of 22% α-helix and 26% ß-sheet. The protein is not glycosylated as shown by carbohydrate analysis. pH and temperature measurements indicated maxima activity at pH 6.0 and 50 °C, respectively. Preliminary pH stability analyses have shown that the protease conserved its compact structure in slightly acidic, neutral and alkaline media but at acidic pH (<3), the formation of some relaxed or molten state was evidenced by 8-anilino-1-naphtalenesulfonic acid binding characteristics. Comparison with the known ficins A, B, C, D1 and D2 (iso)forms revealed that ficin E showed activity profile that looked like ficin A against two chromogenic substrates while it resembled ficins D1 and D2 against three fluorogenic substrates. Enzymatic activity of ficin E was not affected by Mg(2+), Ca(2+) and Mn(2+) at a concentration up to 10mM. However, the activity was completely suppressed by Zn(2+) at a concentration of 1mM. Inhibitory activity measurements clearly identified the enzyme as a cysteine protease, being unaffected by synthetic (Pefabloc SC, benzamidine) and by natural proteinaceous (aprotinin) serine proteases inhibitors, by aspartic proteases inhibitors (pepstatin A) and by metallo-proteases inhibitors (EDTA, EGTA). Surprisingly, it was well affected by the metallo-protease inhibitor o-phenanthroline. The enzymatic activity was however completely blocked by cysteine proteases inhibitors (E-64, iodoacetamide), by thiol-blocking compounds (HgCl2) and by cysteine/serine proteases inhibitors (TLCK and TPCK). This is a novel ficin form according to peptide mass fingerprint analysis, specific amidase activity, SDS-PAGE and PAGE electrophoretic mobility, N-terminal sequencing and unproneness to thiol pegylation.
[Mh] Termos MeSH primário: Cisteína Proteases/metabolismo
Ficina/isolamento & purificação
Ficus/química
Látex/química
[Mh] Termos MeSH secundário: Cromatografia em Gel
Cisteína Proteases/efeitos dos fármacos
Inibidores de Cisteína Proteinase/farmacologia
Eletroforese em Gel de Poliacrilamida
Ficina/química
Ficina/metabolismo
Concentração de Íons de Hidrogênio
Látex/isolamento & purificação
Leucina/análogos & derivados
Leucina/farmacologia
Peso Molecular
Ressonância Magnética Nuclear Biomolecular
Fenantrolinas/farmacologia
Polietilenoglicóis
Estrutura Secundária de Proteína
Compostos de Sulfidrila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cysteine Proteinase Inhibitors); 0 (Latex); 0 (Phenanthrolines); 0 (Sulfhydryl Compounds); 30IQX730WE (Polyethylene Glycols); EC 3.4.- (Cysteine Proteases); EC 3.4.22.3 (Ficain); EC 3.4.22.3 (ficin E, Ficus); GMW67QNF9C (Leucine); R76F7856MV (E 64); W4X6ZO7939 (1,10-phenanthroline)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150828
[Lr] Data última revisão:
150828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150618
[St] Status:MEDLINE


  7 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24817133
[Au] Autor:Andre M; Kühl B; Brenner-Weiss G; Syldatk C; Rudat J
[Ad] Endereço:Institute of Process Engineering in Life Sciences, Section II: Technical Biology, Karlsruhe Institute of Technology, Karlsruhe, Baden-Württemberg, 76131, Germany.
[Ti] Título:Cationic heterooligopeptides by ficain-catalyzed co-oligomerization of lysine and methionine ethylesters.
[So] Source:J Pept Sci;20(8):625-9, 2014 Aug.
[Is] ISSN:1099-1387
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Oligopeptides are of high importance for various industrial applications, e.g. cosmetical or medical. Homooligomerizations and co-oligomerizations with anionic amino acid esters are well described but a successful synthesis of cationic heterooligopeptides has been missing so far. The present study reports the ficain-catalyzed heterooligomerizations of LysOEt with MetOEt, leading to cationic heterooligopeptides with a yield up to 49.5% (w/w). MALDI-ToF/ToF-MS analyses proved successful syntheses of cationic heterooligopeptides with a DP between 7 and 10 amino acid residues, with the enzyme exhibiting a clear preference for methionine.
[Mh] Termos MeSH primário: Ficina/metabolismo
Lisina/análogos & derivados
Lisina/metabolismo
Metionina/análogos & derivados
Oligopeptídeos/biossíntese
[Mh] Termos MeSH secundário: Cátions
Ésteres
Metionina/metabolismo
Oligopeptídeos/química
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cations); 0 (Esters); 0 (Oligopeptides); 452-95-9 (methionine ethyl ester); AE28F7PNPL (Methionine); EC 3.4.22.3 (Ficain); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:140721
[Lr] Data última revisão:
140721
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140513
[St] Status:MEDLINE
[do] DOI:10.1002/psc.2639


  8 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24499119
[Au] Autor:Bekhit AA; Hopkins DL; Geesink G; Bekhit AA; Franks P
[Ad] Endereço:a Department of Food Science, Division of Sciences , University of Otago , PO Box 56 , Dunedin , New Zealand.
[Ti] Título:Exogenous proteases for meat tenderization.
[So] Source:Crit Rev Food Sci Nutr;54(8):1012-31, 2014.
[Is] ISSN:1549-7852
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The use of exogenous proteases to improve meat tenderness has attracted much interest recently, with a view to consistent production of tender meat and added value to lower grade meat cuts. This review discusses the sources, characteristics, and use of exogenous proteases in meat tenderization to highlight the specificity of the proteases toward meat proteins and their impact on meat quality. Plant enzymes (such as papain, bromelain, and ficin) have been extensively investigated as meat tenderizers. New plant proteases (actinidin and zingibain) and microbial enzyme preparations have been of recent interest due to controlled meat tenderization and other advantages. Successful use of these enzymes in fresh meat requires their enzymatic kinetics and characteristics to be determined, together with an understanding of the impact of the surrounding environmental conditions of the meat (pH, temperature) on enzyme function. This enables the optimal conditions for tenderizing fresh meat to be established, and the elimination or reduction of any negative impacts on other quality attributes.
[Mh] Termos MeSH primário: Manipulação de Alimentos/métodos
Carne
Papaína
Peptídeo Hidrolases
Sódio na Dieta
[Mh] Termos MeSH secundário: Animais
Bactérias/enzimologia
Bromelaínas
Cisteína Endopeptidases
Combinação de Medicamentos
Ficina
Hipersensibilidade Alimentar
Indústria Alimentícia/economia
Indústria Alimentícia/métodos
Qualidade dos Alimentos
Fungos/enzimologia
Seres Humanos
Carne/análise
Carne/economia
Proteínas Musculares/metabolismo
Peptídeo Hidrolases/efeitos adversos
Peptídeo Hidrolases/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Drug Combinations); 0 (Muscle Proteins); 0 (Sodium, Dietary); 0 (meat tenderizer); 9001-00-7 (Bromelains); EC 3.4.- (Peptide Hydrolases); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.14 (actinidain); EC 3.4.22.2 (Papain); EC 3.4.22.3 (Ficain)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:140206
[Lr] Data última revisão:
140206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140207
[St] Status:MEDLINE
[do] DOI:10.1080/10408398.2011.623247


  9 / 144 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24112727
[Au] Autor:Yao JW; Xiao Y; Zuo QL; Zhang Y; Tao T; Lin CJ
[Ad] Endereço:Department of Oral Biology and Biomaterial, Xiamen Stomatological Research Institute, Fujian Medical University, Fujian, China. Electronic address: dentyjw@126.com.
[Ti] Título:Effectiveness of cysteine proteases on protein/pigment film removal.
[So] Source:Arch Oral Biol;58(11):1618-26, 2013 Nov.
[Is] ISSN:1879-1506
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Theaflavin (TF) from the black tea can react to human salivary proline-rich proteins (PRPs) to form stains on exposed dental surfaces. Here, we employed a model of protein/pigment film using TF and dephosphorylated bovine ß-casein (Dß-CN), which has an extended conformation, similar to that of salivary PRPs, on a sensor surface to assess the efficacy of cysteine proteases (CPs) including papain, stem bromelain, and ficin, on removing TF bound to Dß-CN and the control TF readsorption on the residual substrate surfaces was also measured. METHODS: The protein/pigment complex film was built by using a quartz crystal microbalance with dissipation (QCM-D). The efficacies of CPs were assessed by Boltzman equation model. The surface details were detected by grazing angle infrared spectroscopy spectra, atomic force microscopy images, and contact angles. RESULTS: The efficacy order of CPs on hydrolyzing protein/pigment complex film is ficin>papain>bromelain. The results from grazing angle infrared spectroscopy spectra, atomic force microscopy images, and contact angles demonstrated that TF bound on the Dß-CN was effectively removed by the CPs, and the amount of TF readsorption on both the residual film of the Dß-CN/TF and the Dß-CN was markedly decreased after hydrolysis. CONCLUSION: This study indicates the potential application of the CPs for tooth stain removal and suggests that these enzymes are worthy of further investigation for use in oral healthcare.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Biflavonoides/química
Catequina/química
Cisteína Endopeptidases/farmacologia
Proteínas Salivares Ricas em Prolina/química
Chá/química
Descoloração de Dente/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Antioxidantes/uso terapêutico
Biflavonoides/metabolismo
Bromelaínas/farmacologia
Caseínas/química
Catequina/metabolismo
Bovinos
Cisteína Endopeptidases/uso terapêutico
Ficina/farmacologia
Seres Humanos
Hidrólise
Microscopia de Força Atômica
Papaína/farmacologia
Técnicas de Microbalança de Cristal de Quartzo
Proteínas Salivares Ricas em Prolina/metabolismo
Espectroscopia de Infravermelho com Transformada de Fourier
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Biflavonoids); 0 (Caseins); 0 (Salivary Proline-Rich Proteins); 0 (Tea); 1IA46M0D13 (theaflavin); 8R1V1STN48 (Catechin); 9001-00-7 (Bromelains); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.2 (Papain); EC 3.4.22.3 (Ficain)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:131011
[Lr] Data última revisão:
131011
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:131012
[St] Status:MEDLINE


  10 / 144 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24053149
[Au] Autor:Mohr T; Desser L
[Ad] Endereço:ScienceConsult, Enzianweg 10a, A-2353, Guntramsdorf, Austria. thomas.mohr@mohrkeg.co.at.
[Ti] Título:Plant proteolytic enzyme papain abrogates angiogenic activation of human umbilical vein endothelial cells (HUVEC) in vitro.
[So] Source:BMC Complement Altern Med;13:231, 2013 Sep 21.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Vascular endothelial growth factor (VEGF) is a key regulator of physiologic and pathogenic angiogenesis in diseases such as cancer and diabetic retinopathy. It is known that cysteine proteases from plants, like bromelain and papain are capable to suppress inflammatory activation. Recent studies have demonstrated that they may interfere with angiogenesis related pathways as well. The aim of this study was to investigate the anti-angiogenic effects of papain on human umbilical vein endothelial cells (HUVEC) in vitro. METHODS: Cell viability after prolonged treatment with papain was investigated by life cell staining and lactate dehydrogenase release assay. Angiogenic activation was assessed by ELISA against phosphorylated proteins AKT, MEK1/2, ERK1/2, SAPK/JNK and p38-MAPK. Growth inhibition was determined by means of an MTT-assay and cell migration by means of a scratch assay. Capability to form a capillary network was investigated using a tube formation assay. RESULTS: Papain did not induce proteolysis or cell detachment of HUVEC in a concentration range between 0 and 25 µg/mL. Four hours treatment with 10 µg/mL papain resulted in a reduced susceptibility of endothelial cells to activation by VEGF as determined by phosphorylation levels of Akt, MEK1/2, SAPK/JNK. Papain exerted a distinct inhibitory effect on cell growth, cell migration and tube formation with inhibition of tube formation detectable at concentrations as low as 1 µg/mL. Bromelain and ficin displayed similar effects with regard to cell growth and tube formation. CONCLUSION: Papain showed a strong anti-angiogenic effect in VEGF activated HUVEC. This effect may be due to interference with AKT, MEK1/2 and SAPK/JNK phosphorylation. Two other plant derived cysteine proteases displayed similar inhibition of HUVEC cell growth and tube formation. These findings indicate that plant proteolytic enzymes may have potential as preventive and therapeutic agents against angiogenesis related human diseases.
[Mh] Termos MeSH primário: Indutores da Angiogênese/farmacologia
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Papaína/farmacologia
[Mh] Termos MeSH secundário: Análise de Variância
Bromelaínas/farmacologia
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Ficina/farmacologia
Seres Humanos
Neovascularização Patológica
Fator A de Crescimento do Endotélio Vascular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Angiogenesis Inducing Agents); 0 (Vascular Endothelial Growth Factor A); 9001-00-7 (Bromelains); EC 3.4.22.2 (Papain); EC 3.4.22.3 (Ficain)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:150422
[Lr] Data última revisão:
150422
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130924
[St] Status:MEDLINE
[do] DOI:10.1186/1472-6882-13-231



página 1 de 15 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde