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[PMID]:28870811
[Au] Autor:Islam MM; Kuroda Y
[Ad] Endereço:Department of Biotechnology and Life Sciences, Tokyo University of Agriculture and Technology, 2-24-16 Nakamachi, Koganei-shi, Tokyo 184-8588, Japan; Department of Biochemistry and Molecular Biology, University of Chittagong, Chittagong, 4331, Bangladesh.
[Ti] Título:A hetero-micro-seeding strategy for readily crystallizing closely related protein variants.
[So] Source:Biochem Biophys Res Commun;493(1):504-508, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein crystallization remains difficult to rationalize and screening for optimal crystallization conditions is a tedious and time consuming procedure. Here, we report a hetero-micro-seeding strategy for producing high resolution crystals of closely related protein variants, where micro crystals from a readily crystallized variant are used as seeds to develop crystals of other variants less amenable to crystallization. We applied this strategy to Bovine Pancreatic Trypsin Inhibitor (BPTI) variants, which would not crystallize using standard crystallization practice. Out of six variants in our analysis, only one called BPTI-[5,55]A14G formed well behaving crystals; and the remaining five (A14GA38G, A14GA38V, A14GA38L, A14GA38I, and A14GA38K) could be crystallized only using micro-seeds from the BPTI-[5,55]A14G crystal. All hetero-seeded crystals diffracted at high resolution with minimum mosaicity, retaining the same space group and cell dimension. Moreover, hetero-micro-seeding did not introduce any biases into the mutant's structure toward the seed structure, as demonstrated by A14GA38I structures solved using micro-seeds from A14GA38G, A14GA38L and A14GA38I. Though hetero-micro-seeding is a simple and almost naïve strategy, this is the first direct demonstration of its workability. We believe that hetero-micro-seeding, which is contrasting with the popular idea that crystallization requires highly purified proteins, could contribute a new tool for rapidly solving protein structures in mutational analysis studies.
[Mh] Termos MeSH primário: Aprotinina/síntese química
Aprotinina/ultraestrutura
Cristalização/métodos
Microfluídica/métodos
Manejo de Espécimes/métodos
[Mh] Termos MeSH secundário: Aprotinina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9087-70-1 (Aprotinin)
[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:170906
[St] Status:MEDLINE


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[PMID]:28478438
[Au] Autor:Sasamoto K; Marunaka R; Niisato N; Sun H; Taruno A; Pezzotti G; Yamamoto T; Kanamura N; Zhu W; Nishio K; Inui T; Eaton DC; Marunaka Y
[Ad] Endereço:Department of Molecular Cell Physiology, Kyoto, Japan.
[Ti] Título:Analysis of Aprotinin, a Protease Inhibitor, Action on the Trafficking of Epithelial Na+ Channels (ENaC) in Renal Epithelial Cells Using a Mathematical Model.
[So] Source:Cell Physiol Biochem;41(5):1865-1880, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Epithelial Na+ channels (ENaC) play a crucial role in control of blood pressure by regulating renal Na+ reabsorption. Intracellular trafficking of ENaC is one of the key regulators of ENaC function, but a quantitative description of intracellular recycling of endogenously expressed ENaC is unavailable. We attempt here to provide a model for intracellular recycling after applying a protease inhibitor under hypotonic conditions. METHODS: We simulated the ENaC-mediated Na+ transport in renal epithelial A6 cells measured as short-circuit currents using a four-state mathematical ENaC trafficking model. RESULTS: We developed a four-state mathematical model of ENaC trafficking in the cytosol of renal epithelial cells that consists of: an insertion state of ENaC that can be trafficked to the apical membrane state (insertion rate); an apical membrane state of ENaC conducting Na+ across the apical membrane; a recycling state containing ENaC that are retrieved from the apical membrane state (endocytotic rate) and then to the insertion state (recycling rate) communicating with the apical membrane state or to a degradation state (degradation rate). We studied the effect of aprotinin (a protease inhibitor) blocking protease-induced cleavage of the extracellular loop of γ ENaC subunit on the rates of intracellular ENaC trafficking using the above-defined four-state mathematical model of ENaC trafficking and the recycling number relative to ENaC staying in the apical membrane. We found that aprotinin significantly reduced the insertion rate of ENaC to the apical membrane by 40%, the recycling rate of ENaC by 81%, the cumulative time of an individual ENaC staying in the apical membrane by 32%, the cumulative life-time after the first endocytosis of ENaC by 25%, and the cumulative Na+ absorption by 31%. The most interesting result of the present study is that cleavage of ENaC affects the intracellular ENaC trafficking rate and determines the residency time of ENaC, indicating that more active cleaved ENaCs stay longer at the apical membrane contributing to transcellular Na+ transport via an increase in recycling of ENaC to the apical membrane. CONCLUSION: The extracellular protease-induced cleavage of the extracellular loop of γ ENaC subunit increases transcellular epithelial Na+ transport by elevating the recycling rate of ENaC due to an increase in the recycling rate of ENaCs associated with increases in the insertion rate of ENaC.
[Mh] Termos MeSH primário: Aprotinina/farmacologia
Células Epiteliais/metabolismo
Canais Epiteliais de Sódio/metabolismo
Rim/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Transporte Proteico/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epithelial Sodium Channels); 9087-70-1 (Aprotinin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170508
[St] Status:MEDLINE
[do] DOI:10.1159/000471934


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[PMID]:28366297
[Au] Autor:Godier A; Hunt BJ
[Ad] Endereço:Department of Anesthesia and Critical Care, Fondation Ophtalmologique Rothschild, 75019 Paris, France; Inserm UMR-S1140, faculté de pharmacie, université Paris Descartes, Paris, France. Electronic address: annegodier@yahoo.fr.
[Ti] Título:Aprotinin as an alternative to tranexamic acid in cardiac surgery - Is this where we started from?
[So] Source:Anaesth Crit Care Pain Med;36(2):79-81, 2017 04.
[Is] ISSN:2352-5568
[Cp] País de publicação:France
[La] Idioma:eng
[Mh] Termos MeSH primário: Aprotinina
Ácido Tranexâmico
[Mh] Termos MeSH secundário: Antifibrinolíticos
Procedimentos Cirúrgicos Cardíacos
Seres Humanos
[Pt] Tipo de publicação:EDITORIAL; COMMENT
[Nm] Nome de substância:
0 (Antifibrinolytic Agents); 6T84R30KC1 (Tranexamic Acid); 9087-70-1 (Aprotinin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE


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[PMID]:28298600
[Au] Autor:Lin KH; Ali A; Rusere L; Soumana DI; Kurt Yilmaz N; Schiffer CA
[Ad] Endereço:Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
[Ti] Título:Dengue Virus NS2B/NS3 Protease Inhibitors Exploiting the Prime Side.
[So] Source:J Virol;91(10), 2017 May 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mosquito-transmitted dengue virus (DENV) infects millions of people in tropical and subtropical regions. Maturation of DENV particles requires proper cleavage of the viral polyprotein, including processing of 8 of the 13 substrate cleavage sites by dengue virus NS2B/NS3 protease. With no available direct-acting antiviral targeting DENV, NS2/NS3 protease is a promising target for inhibitor design. Current design efforts focus on the nonprime side of the DENV protease active site, resulting in highly hydrophilic and nonspecific scaffolds. However, the prime side also significantly modulates DENV protease binding affinity, as revealed by engineering the binding loop of aprotinin, a small protein with high affinity for DENV protease. In this study, we designed a series of cyclic peptides interacting with both sides of the active site as inhibitors of dengue virus protease. The design was based on two aprotinin loops and aimed to leverage both key specific interactions of substrate sequences and the entropic advantage driving aprotinin's high affinity. By optimizing the cyclization linker, length, and amino acid sequence, the tightest cyclic peptide achieved a value of 2.9 µM against DENV3 wild-type (WT) protease. These inhibitors provide proof of concept that both sides of DENV protease active site can be exploited to potentially achieve specificity and lower hydrophilicity in the design of inhibitors targeting DENV. Viruses of the flaviviral family, including DENV and Zika virus transmitted by , continue to be a threat to global health by causing major outbreaks in tropical and subtropical regions, with no available direct-acting antivirals for treatment. A better understanding of the molecular requirements for the design of potent and specific inhibitors against flaviviral proteins will contribute to the development of targeted therapies for infections by these viruses. The cyclic peptides reported here as DENV protease inhibitors provide novel scaffolds that enable exploiting the prime side of the protease active site, with the aim of achieving better specificity and lower hydrophilicity than those of current scaffolds in the design of antiflaviviral inhibitors.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Vírus da Dengue/efeitos dos fármacos
Peptídeos Cíclicos/farmacologia
Inibidores de Proteases/farmacologia
Serina Endopeptidases/química
Serina Endopeptidases/metabolismo
Proteínas não Estruturais Virais/antagonistas & inibidores
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antivirais/síntese química
Antivirais/metabolismo
Aprotinina/química
Aprotinina/metabolismo
Aprotinina/farmacologia
Domínio Catalítico
Simulação por Computador
Vírus da Dengue/química
Vírus da Dengue/enzimologia
Descoberta de Drogas/métodos
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Cinética
Peptídeos Cíclicos/síntese química
Inibidores de Proteases/síntese química
Inibidores de Proteases/metabolismo
Ligação Proteica
Proteínas não Estruturais Virais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Peptides, Cyclic); 0 (Protease Inhibitors); 0 (Viral Nonstructural Proteins); 9087-70-1 (Aprotinin); EC 3.4.21.- (NS3 protease, dengue virus); EC 3.4.21.- (Serine Endopeptidases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171028
[Lr] Data última revisão:
171028
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE


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[PMID]:28070896
[Au] Autor:Li J; Hu R; Li X; Tong X; Yu D; Zhao Q
[Ad] Endereço:State Key Laboratory for Mesoscopic Physics and Electron Microscopy Laboratory, School of Physics, Peking University, Beijing, P. R. China.
[Ti] Título:Tiny protein detection using pressure through solid-state nanopores.
[So] Source:Electrophoresis;38(8):1130-1138, 2017 04.
[Is] ISSN:1522-2683
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Solid-state nanopore is a promising tool to detect proteins and its complexes. Small proteins (sub-35 kDa) translocate very fast which could not be detected by normal patch-clamp recording instrument due to low temporal resolution. We first introduce pressure into protein study and detection. The pressure-derived force, combined with the voltage bias, makes very tiny protein (MW < 6.5 kDa) detection possible. Capture rate for Aprotinin is enhanced five times more than that in traditional voltage-driven method by fine tuning of pressure and voltage. Temporal resolution of Aprotinin detection has improved by decreasing effective driving force. Moreover, we provide potential method to locate the equilibrium range for BSA movement in ionic solution by modulating driving pressure and retard voltage. Our study is of fundamental significance in nanopore research and provides unique platforms to study small proteins and other tiny biomolecules.
[Mh] Termos MeSH primário: Nanoporos
Pressão
Proteínas/análise
[Mh] Termos MeSH secundário: Aprotinina/análise
Eletrodos
Eletroforese Capilar/instrumentação
Desenho de Equipamento
Proteínas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteins); 9087-70-1 (Aprotinin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170111
[St] Status:MEDLINE
[do] DOI:10.1002/elps.201600410


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[PMID]:27899430
[Au] Autor:Higashiyama M; Tokunaga T; Kusu T; Ishida H; Okami J; Kodama K
[Ad] Endereço:1 Department of General Thoracic Surgery, Osaka Medical Center for Cancer and Cardiovascular Diseases, Osaka, Japan.
[Ti] Título:Prophylactic middle lobe fixation for postoperative pulmonary torsion.
[So] Source:Asian Cardiovasc Thorac Ann;25(1):41-46, 2017 Jan.
[Is] ISSN:1816-5370
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Background To prevent postoperative middle lobe torsion after a right upper lobectomy, we introduced a novel technique of interlobar fixation using collagen fleece coated with fibrin. In this study, the prophylactic effects of this method on the incidence of postoperative pulmonary torsion were analyzed. Methods Between April 2001 and December 2015, 3786 pulmonary resection procedures (excluding total pneumonectomy) were performed in our institution, and prophylactic interlobar fixation was selectively applied when intraoperative examination indicated that the patient was at high risk of postoperative pulmonary lobe torsion. As a control group, 842 patients who underwent pulmonary resection procedures between January 1996 and April 2001 were reviewed. Results During the study period, 10 (0.3%) patients underwent prophylactic middle lobe fixation (to the lower lobe after a right upper lobectomy in 9, and to the upper lobe after a right lower lobectomy in one). Pulmonary lobar (middle lobe) torsion occurred in only one patient (after right upper lobectomy); thus the incidence of this complication was 0.1% among patients who underwent a right upper lobectomy and 0.03% among all pulmonary resection procedures. The rates during the study period were marginally significantly lower than those in the control period (1.3% and 0.24%, respectively; p = 0.071 and p = 0.087, respectively). Conclusion Prophylactic middle lobe fixation might be useful for preventing postoperative pulmonary middle lobe torsion.
[Mh] Termos MeSH primário: Aprotinina/uso terapêutico
Fibrinogênio/uso terapêutico
Pneumopatias/prevenção & controle
Neoplasias Pulmonares/cirurgia
Pneumonectomia/efeitos adversos
Trombina/uso terapêutico
Anormalidade Torcional/prevenção & controle
[Mh] Termos MeSH secundário: Idoso
Combinação de Medicamentos
Feminino
Seres Humanos
Pneumopatias/diagnóstico
Pneumopatias/etiologia
Masculino
Meia-Idade
Seleção de Pacientes
Estudos Retrospectivos
Medição de Risco
Fatores de Risco
Fatores de Tempo
Anormalidade Torcional/diagnóstico
Anormalidade Torcional/etiologia
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drug Combinations); 0 (TachoSil); 0 (tachocomb); 9001-32-5 (Fibrinogen); 9087-70-1 (Aprotinin); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170213
[Lr] Data última revisão:
170213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161201
[St] Status:MEDLINE
[do] DOI:10.1177/0218492316682669


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[PMID]:27705885
[Au] Autor:Cegla J; Jones BJ; Howard J; Kay R; Creaser CS; Bloom SR; Tan TM
[Ad] Endereço:1 Division of Diabetes, Endocrinology and Metabolism, Imperial College London, London, UK.
[Ti] Título:The preanalytical stability of glucagon as measured by liquid chromatography tandem mass spectrometry and two commercially available immunoassays.
[So] Source:Ann Clin Biochem;54(2):293-296, 2017 Mar.
[Is] ISSN:1758-1001
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Background One of the main challenges in the measurement of glucagon is the premise that it is unstable in human plasma. Traditionally, protease inhibitors have been used to prevent its degradation; however, their use is controversial. Here, we investigated the optimal method of sample collection for glucagon, with measurement by liquid chromatography tandem mass spectrometry (LC-MS/MS) and two commercially available immunoassays. Methods Blood from healthy fasting volunteers (n = 10) was processed under a variety of preanalytical conditions including collection in EDTA vs. lithium heparin tubes and the addition of aprotinin and/or a dipeptidyl-peptidase IV (DPPIV) inhibitor. Additionally, the effect of freeze thaw was assessed. Plasma glucagon concentrations were measured by LC-MS/MS and two commercially available immunoassays (HTRF® sandwich immunoassay, Cisbio and Milliplex MAP Human Metabolic Hormone Panel, Merck Millipore). Results A systematic bias of Milliplex > LC-MS/MS > HTRF was noted and plasma glucagon concentrations were significantly different between methods (Milliplex vs. LC-MS/MS P < 0.01; Milliplex vs. HTRF P < 0.0001; LC-MS/MS vs. HTRF P < 0.001). The addition of aprotinin, DPPIV inhibitor or a combination of aprotinin and DPPIV inhibitor had no effect on plasma glucagon concentrations when compared to 'non-stabilized' samples or each other. Whether samples were taken in EDTA tubes or lithium heparin tubes made no difference to plasma glucagon concentrations. These findings were consistent for all three methods. Plasma glucagon concentrations were not significantly different after two freeze-thaw cycles (performed on samples in EDTA tubes containing aprotinin and DPPIV inhibitor). Conclusions This study demonstrates that glucagon is stable in both EDTA and lithium heparin tubes when stored at -80℃. Furthermore, the addition of aprotinin and DPPIV inhibitors is unnecessary.
[Mh] Termos MeSH primário: Coleta de Amostras Sanguíneas/normas
Cromatografia Líquida/normas
Glucagon/sangue
Imunoensaio/normas
Espectrometria de Massas em Tandem/normas
[Mh] Termos MeSH secundário: Anticoagulantes/química
Aprotinina/química
Inibidores da Dipeptidil Peptidase IV/química
Ácido Edético/química
Congelamento
Voluntários Saudáveis
Heparina/química
Seres Humanos
Transição de Fase
Estabilidade Proteica
Inibidores de Serino Proteinase/química
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticoagulants); 0 (Dipeptidyl-Peptidase IV Inhibitors); 0 (Serine Proteinase Inhibitors); 9005-49-6 (Heparin); 9007-92-5 (Glucagon); 9087-70-1 (Aprotinin); 9G34HU7RV0 (Edetic Acid)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE
[do] DOI:10.1177/0004563216675648


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[PMID]:27810896
[Au] Autor:Kayode O; Wang R; Pendlebury DF; Cohen I; Henin RD; Hockla A; Soares AS; Papo N; Caulfield TR; Radisky ES
[Ad] Endereço:From the Departments of Cancer Biology and.
[Ti] Título:An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.
[So] Source:J Biol Chem;291(51):26304-26319, 2016 Dec 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The molecular basis of enzyme catalytic power and specificity derives from dynamic interactions between enzyme and substrate during catalysis. Although considerable effort has been devoted to understanding how conformational dynamics within enzymes affect catalysis, the role of conformational dynamics within protein substrates has not been addressed. Here, we examine the importance of substrate dynamics in the cleavage of Kunitz-bovine pancreatic trypsin inhibitor protease inhibitors by mesotrypsin, finding that the varied conformational dynamics of structurally similar substrates can profoundly impact the rate of catalysis. A 1.4-Å crystal structure of a mesotrypsin-product complex formed with a rapidly cleaved substrate reveals a dramatic conformational change in the substrate upon proteolysis. By using long all-atom molecular dynamics simulations of acyl-enzyme intermediates with proteolysis rates spanning 3 orders of magnitude, we identify global and local dynamic features of substrates on the nanosecond-microsecond time scale that correlate with enzymatic rates and explain differential susceptibility to proteolysis. By integrating multiple enhanced sampling methods for molecular dynamics, we model a viable conformational pathway between substrate-like and product-like states, linking substrate dynamics on the nanosecond-microsecond time scale with large collective substrate motions on the much slower time scale of catalysis. Our findings implicate substrate flexibility as a critical determinant of catalysis.
[Mh] Termos MeSH primário: Aprotinina/química
Simulação de Dinâmica Molecular
Proteólise
Tripsina/química
[Mh] Termos MeSH secundário: Animais
Catálise
Bovinos
Cristalografia por Raios X
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9087-70-1 (Aprotinin); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170529
[Lr] Data última revisão:
170529
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE


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[PMID]:27801403
[Au] Autor:Shimanskiy VN; Poshataev VK; Odamanov DA; Shevchenko KV
[Ad] Endereço:Burdenko Neurosurgical Institute, Moscow, Russia.
[Ti] Título:[A technique of TachoComb application in dura mater reconstruction in surgery for posterior cranial fossa tumors].
[Ti] Título:Metodika primeneniya materiala TakhoKomb dlya plastiki tverdoi mozgovoi obolochki v khirurgii opukholei zadnei cherepnoi yamki..
[So] Source:Zh Vopr Neirokhir Im N N Burdenko;80(5):85-89, 2016.
[Is] ISSN:0042-8817
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:INTRODUCTION: Liquorrhea is a condition characterized by cerebrospinal fluid (CSF) leakage from the cranial cavity due to injury to the integrity of the dura mater (DM) and bone structures of the skull base. Surgery for posterior cranial fossa (PCF) lesions distinguishes wound CSF leakage when CSF leaks from a surgical wound as well as basal CSF leakage (nasal liquorrhea and, less often, otoliquorrhea). The main cause of basal CSF leakage is injury (including surgical injury) resulting in a defect in the DM and bone structures (cells of the mastoid process in the case of a suboccipital retrosigmoid approach). There are a variety of DM restoration techniques ranging from DM closure or placement of a synthetic or autologous patch to application of various synthetic adhesives in the form of adhesive compositions (Tissucol) and adhesive substances (TachoComb). This article describes the experience with application of a TachoComb® sponge gained at the 5th Clinical Department of the Burdenko Neurosurgical Institute. MATERIAL AND METHODS: The study included 176 patients with acoustic neurinomas. At the final stage of surgery, all the patients underwent DM reconstruction with a TachoComb® collagen sponge. CSF leakage occurred in 3 (1.7%) patients, with each of them having Koos grade 4 tumor. One (0.56%) patient had wound liquorrhea, and 2 (1.1%) patients had nasal liquorrhea. CSF leakage was managed by placement of a lumbar drain; postoperative wound revision was not required. CONCLUSION: Using the TachoComb® sponge for DM reconstruction in PCF surgery is an effective way to prevent postoperative CSF leakage, provided that the algorithm of manipulations described in the article is followed.
[Mh] Termos MeSH primário: Aprotinina/administração & dosagem
Dura-Máter
Fibrinogênio/administração & dosagem
Neoplasias Infratentoriais
Procedimentos Cirúrgicos Reconstrutivos/métodos
Trombina/administração & dosagem
[Mh] Termos MeSH secundário: Adulto
Idoso
Combinação de Medicamentos
Dura-Máter/patologia
Dura-Máter/cirurgia
Feminino
Seres Humanos
Neoplasias Infratentoriais/patologia
Neoplasias Infratentoriais/cirurgia
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drug Combinations); 0 (tachocomb); 9001-32-5 (Fibrinogen); 9087-70-1 (Aprotinin); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE
[do] DOI:10.17116/neiro201680585-89


  10 / 6109 MEDLINE  
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[PMID]:27685427
[Au] Autor:Jozawa H; Kabir MG; Zako T; Maeda M; Chiba K; Kuroda Y
[Ad] Endereço:Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei-shi, Japan.
[Ti] Título:Amorphous protein aggregation monitored using fluorescence self-quenching.
[So] Source:FEBS Lett;590(20):3501-3509, 2016 Oct.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Biophysical understanding of amorphous protein aggregation can significantly impact diverse area of biotechnology. Here, we report the time dependent salt-induced formation of amorphous aggregation as monitored by fluorescence self-quenching and compare the results with conventional methods for detecting protein aggregation [static light scattering (LS) and dynamic light scattering (DLS)]. As a model protein, we used a bovine pancreatic trypsin inhibitor (BPTI) variant extended by two glycines (C2G) at its C terminus, and three variants where three types of Solubility Controlling Peptide tags (SCP tags) made of five serines (C5S), alanines (C5A) or aspartic acids (C5D) were added to the C terminus of C2G. All variants have a native-like BPTI structure and trypsin inhibitory activity, but different solubilities controlled by the SCP tags. The BPTIs were labeled using NHS-Fluorescein (FAM) conjugated to BPTI's lysines, and we measured the changes in fluorescence intensity occurring upon the addition of NaCl. The fluorescence of all FAM-BPTIs decreased almost immediately, albeit to a different extent, upon addition of salt and became constant after 10 min for 24 h or more. On the other hand, LS and DLS signal changes were dependent on the type of tags. Namely, C2G's LS and DLS signals changed immediately, the signals of C5S and C5A tagged FAM-BPTIs increased slowly from 10 min to 24 h, and those of C5D remained constant. These observations indicated the presence of at least one intermediate step, with increased protein-protein interaction yielding a 'molecular condensation' phase. According to this model, C2G would rapidly turn from 'condensates' to aggregates, whereas C5S and C5A tagged FAM-BPTIs would do so slowly, and the soluble C5D tagged variant would remain in the molecular condensation state.
[Mh] Termos MeSH primário: Aminoácidos/química
Aprotinina/química
Aprotinina/genética
Fluoresceína/química
Cloreto de Sódio/farmacologia
[Mh] Termos MeSH secundário: Animais
Bovinos
Difusão Dinâmica da Luz
Fluorescência
Mutação
Conformação Proteica/efeitos dos fármacos
Solubilidade
Coloração e Rotulagem
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Amino Acids); 451W47IQ8X (Sodium Chloride); 9087-70-1 (Aprotinin); TPY09G7XIR (Fluorescein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160930
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12439



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