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  1 / 6801 MEDLINE  
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[PMID]:29351301
[Au] Autor:Chang HC; Kung CC; Chang TT; Jao SC; Hsu YT; Li WS
[Ad] Endereço:Institute of Chemistry, Academia Sinica, Taipei, Taiwan.
[Ti] Título:Investigation of the proton relay system operative in human cystosolic aminopeptidase P.
[So] Source:PLoS One;13(1):e0190816, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aminopeptidase P, a metalloprotease, targets Xaa-Proline peptides for cleavage [1-4]. There are two forms of human AMPP, a membrane-bound form (hmAMPP) and a soluble cytosolic form (hcAMPP)[5]. Similar to the angiotensin-I-converting enzyme, AMPP plays an important role in the catabolism of inflammatory and vasoactive peptides, known as kinins. The plasma kinin, bradykinin, was used as the substrate to conduct enzymatic activity analyses and to determine the Michaelis constant (Km) of 174 µM and the catalytic rate constant (kcat) of 10.8 s-1 for hcAMPP. Significant differences were observed in the activities of Y527F and R535A hcAMPP mutants, which displayed a 6-fold and 13.5-fold for decrease in turnover rate, respectively. Guanidine hydrochloride restored the activity of R535A hcAMPP, increasing the kcat/Km 20-fold, yet it had no impact on the activities of the wild-type or Y527F mutant hcAMPPs. Activity restoration by guanidine derivatives followed the order guanidine hydrochloride >> methyl-guanidine > amino-guanidine > N-ethyl-guanidine. Overall, the results indicate the participation of R535 in the hydrogen bond network that forms a proton relay system. The quaternary structure of hcAMPP was determined by using analytical ultracentrifugation (AUC). The results show that alanine replacement of Arg535 destabilizes the hcAMPP dimer and that guanidine hydrochloride restores the native monomer-dimer equilibrium. It is proposed that Arg535 plays an important role in hcAMMP catalysis and in stabilization of the catalytically active dimeric state.
[Mh] Termos MeSH primário: Aminopeptidases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Aminopeptidases/química
Aminopeptidases/genética
Catálise
Citosol/enzimologia
Estabilidade Enzimática
Guanidina/farmacologia
Seres Humanos
Ligações de Hidrogênio
Cinética
Modelos Moleculares
Mutagênese Sítio-Dirigida
Desnaturação Proteica
Multimerização Proteica
Estrutura Quaternária de Proteína
Prótons
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protons); 0 (Recombinant Proteins); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.9 (X-Pro aminopeptidase); JU58VJ6Y3B (Guanidine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190816


  2 / 6801 MEDLINE  
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[PMID]:29278768
[Au] Autor:Tang Y; Yang P; Wang F; Xu H; Zong SY
[Ad] Endereço:Department of Clinical Laboratory, Zhangjiagang Hospital of Traditional Chinese Medicine, Zhangjiagang, Jiangsu 215600, China.
[Ti] Título:Association of polymorphisms in ERAP1 and risk of ankylosing spondylitis in a Chinese population.
[So] Source:Gene;646:8-11, 2018 Mar 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:To explore the association between five polymorphisms in endoplasmic reticulum associated aminopeptidase 1 (ERAP1) gene and risk of ankylosing spondylitis (AS) in a Chinese population. A case-control study enrolled 250 AS patients and 250 healthy controls was carried out. The genotypes of involved polymorphisms (rs27037, rs27038, rs469876, rs27044 and rs27980) in ERAP1 were detected by Sequenom Mass-Array platform. There were significant differences of the level of WBC (white blood cell), Platelets, CRP (C-reactive protein) and ESR (erythrocyte sedimentation rate) between AS patients and controls (P <0.05). There was statistically association between ERAP1 rs27044 polymorphism and risk of AS, and the carriers with rs27044 CG genotype have an increased the risk for AS (CG versus GG, OR=1.70, 95% CI=1.10-2.62, P=0.015). However, we found no evidence for the association of rs27037, rs469876, and rs27980 polymorphisms in ERAP1 with AS risk. Our findings indicated that ERAP1 rs27044 polymorphism was associated with the susceptibility of AS.
[Mh] Termos MeSH primário: Aminopeptidases/genética
Grupo com Ancestrais do Continente Asiático/genética
Antígenos de Histocompatibilidade Menor/genética
Polimorfismo de Nucleotídeo Único
Espondilite Anquilosante/genética
[Mh] Termos MeSH secundário: Adulto
Grupo com Ancestrais do Continente Asiático/etnologia
Estudos de Casos e Controles
China/etnologia
Feminino
Estudos de Associação Genética
Predisposição Genética para Doença
Seres Humanos
Masculino
Meia-Idade
Análise de Sequência de DNA
Espondilite Anquilosante/etnologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Minor Histocompatibility Antigens); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.- (ERAP1 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


  3 / 6801 MEDLINE  
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[PMID]:29253000
[Au] Autor:Lin S; Wang S; Si Y; Yang W; Zhu S; Ni W
[Ad] Endereço:College of Environmental and Resource Sciences, Zhejiang University, Key Laboratory of Agricultural Resource and Environment of Zhejiang Province, Hangzhou, P. R. China.
[Ti] Título:Variations in eco-enzymatic stoichiometric and microbial characteristics in paddy soil as affected by long-term integrated organic-inorganic fertilization.
[So] Source:PLoS One;12(12):e0189908, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To investigate the effects of different nutrient management regimes on the soil chemical, eco-enzymatic stoichiometric and microbial characteristics, soil samples were collected from a 30-year, long-term field experiment with six plots growing rice. The results showed that as integrated fertilization increased, so did the concentrations of soil total or available nutrients and microbial biomass carbon (MBC). Our results also found enhanced soil basal respiration and cumulative carbon mineralization compared to chemical fertilization alone at the same nutrient doses. The activities of soil protease (Pro), ß-glucosidase (ßG), N-acetyl-glucosaminidase (NAG) and acid phosphatase (AP) from the integrated fertilization treatments were significantly higher than those of the treatments without organic manure, so did the activities of soil leucyl aminopeptidase (LAP) and urease (Ure) from the treatment with organic manure in addition to farmer practise fertilization (NPKM2). The stoichiometric ratios, expressed as lnßG/ln(NAG+LAP)/lnPro/lnUre/lnAP, ranged from 1:0.94:1.04:0.67:1.01 to 1:0.98:1.10:0.78:1.25, indicating that the acquisition of C, N and P changed consistently and synchronously under different nutrient management strategies. Integrated fertilization was more beneficial to the acquisition and utilization of soil organic carbon compared to low-molecular-weight organic nitrogen. We concluded that protease and urease should be considered in eco-enzymatic stoichiometric assessments for the hydrolysis of proteins, amino acids, carbohydrates and phosphomonoesters in soil, and integrated fertilization with chemical fertilizers and organic manure should be recommended as a preferable nutrient management system for intensive rice cultivation.
[Mh] Termos MeSH primário: Agricultura/métodos
Carbono/química
Fertilizantes
Microbiologia do Solo
Solo/química
[Mh] Termos MeSH secundário: Acetilglucosaminidase/metabolismo
Fosfatase Ácida/metabolismo
Aminopeptidases/metabolismo
Biomassa
China
Esterco
Nitrogênio/química
Oryza
Fósforo/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fertilizers); 0 (Manure); 0 (Soil); 27YLU75U4W (Phosphorus); 7440-44-0 (Carbon); EC 3.1.3.2 (Acid Phosphatase); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.52 (Acetylglucosaminidase); EC 3.4.11.- (Aminopeptidases); N762921K75 (Nitrogen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189908


  4 / 6801 MEDLINE  
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[PMID]:29220658
[Au] Autor:Veling MT; Reidenbach AG; Freiberger EC; Kwiecien NW; Hutchins PD; Drahnak MJ; Jochem A; Ulbrich A; Rush MJP; Russell JD; Coon JJ; Pagliarini DJ
[Ad] Endereço:Morgridge Institute for Research, Madison, WI 53715, USA; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
[Ti] Título:Multi-omic Mitoprotease Profiling Defines a Role for Oct1p in Coenzyme Q Production.
[So] Source:Mol Cell;68(5):970-977.e11, 2017 Dec 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitoproteases are becoming recognized as key regulators of diverse mitochondrial functions, although their direct substrates are often difficult to discern. Through multi-omic profiling of diverse Saccharomyces cerevisiae mitoprotease deletion strains, we predicted numerous associations between mitoproteases and distinct mitochondrial processes. These include a strong association between the mitochondrial matrix octapeptidase Oct1p and coenzyme Q (CoQ) biosynthesis-a pathway essential for mitochondrial respiration. Through Edman sequencing and in vitro and in vivo biochemistry, we demonstrated that Oct1p directly processes the N terminus of the CoQ-related methyltransferase, Coq5p, which markedly improves its stability. A single mutation to the Oct1p recognition motif in Coq5p disrupted its processing in vivo, leading to CoQ deficiency and respiratory incompetence. This work defines the Oct1p processing of Coq5p as an essential post-translational event for proper CoQ production. Additionally, our data visualization tool enables efficient exploration of mitoprotease profiles that can serve as the basis for future mechanistic investigations.
[Mh] Termos MeSH primário: Aminopeptidases/metabolismo
Metabolismo Energético
Metabolômica/métodos
Metiltransferases/metabolismo
Mitocôndrias/enzimologia
Proteômica/métodos
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
Ubiquinona/biossíntese
[Mh] Termos MeSH secundário: Aminopeptidases/genética
Estabilidade Enzimática
Genótipo
Metiltransferases/genética
Mutação
Fenótipo
Domínios Proteicos
Processamento de Proteína Pós-Traducional
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Tempo
Ubiquinona/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); 1339-63-5 (Ubiquinone); EC 2.1.1.- (COQ5 protein, S cerevisiae); EC 2.1.1.- (Methyltransferases); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.- (Oct1 protein, S cerevisiae)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


  5 / 6801 MEDLINE  
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[PMID]:28946286
[Au] Autor:Gao X; Yin Y; Zhou C
[Ad] Endereço:School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China. Electronic address: gaoxianli@ujs.edu.cn.
[Ti] Título:Purification, characterisation and salt-tolerance molecular mechanisms of aspartyl aminopeptidase from Aspergillus oryzae 3.042.
[So] Source:Food Chem;240:377-385, 2018 Feb 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A salt-tolerant aspartyl aminopeptidase (approximately 57kDa) from Aspergillus oryzae 3.042 was purified and identified. Specific inhibitor experiments indicated that it was an aminopeptidase containing Zn . Its optimal and stable pH values and temperatures were 7 and 50°C, respectively. Its relative activity remained beyond 30% in 3M NaCl solution for 15d, and its K and V were slightly affected in 3M NaCl solution, indicating its excellent salt-tolerance. A comprehensive analysis including protein homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrated that aspartyl aminopeptidase had a greater stability than non-salt-tolerant protease in high salinity. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues and stronger hydrophobicity of interior residues were the salt-tolerance mechanisms of aspartyl aminopeptidase.
[Mh] Termos MeSH primário: Aspergillus oryzae
Glutamil Aminopeptidase/metabolismo
[Mh] Termos MeSH secundário: Aminopeptidases
Concentração de Íons de Hidrogênio
Tolerância a Sal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.11.- (Aminopeptidases); EC 3.4.11.7 (Glutamyl Aminopeptidase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE


  6 / 6801 MEDLINE  
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[PMID]:28803047
[Au] Autor:Singh R; Williams J; Vince R
[Ad] Endereço:Center for Drug Design, Academic Health Center, University of Minnesota, Minneapolis, MN 55455, USA. Electronic address: singh109@umn.edu.
[Ti] Título:Puromycin based inhibitors of aminopeptidases for the potential treatment of hematologic malignancies.
[So] Source:Eur J Med Chem;139:325-336, 2017 Oct 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Substantial progress has been described in the study of puromycin and its analogs for antibiotic properties. However, the peptidase inhibitory activity of related analogs has not been explored as extensively. Specifically, inhibiting aminopeptidases for achieving antitumor effect has been sparsely investigated. Herein, we address this challenge by reporting the synthesis of a series of analogs based on the structural template of puromycin. We also present exhaustive biochemical and in vitro analyses in support of our thesis. Analyzing the structure-activity relationship revealed a steric requirement for maximum potency. Effective inhibitors of Puromycin-Sensitive Aminopeptidase (PSA) are disclosed here. These potential therapeutic agents display superior in vitro antitumor potency against two leukemic cell lines, as compared to known inhibitors of aminopeptidases.
[Mh] Termos MeSH primário: Aminopeptidases/antagonistas & inibidores
Antineoplásicos/farmacologia
Inibidores Enzimáticos/farmacologia
Neoplasias Hematológicas/tratamento farmacológico
Puromicina/farmacologia
[Mh] Termos MeSH secundário: Aminopeptidases/metabolismo
Animais
Antineoplásicos/síntese química
Antineoplásicos/química
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Ensaios de Seleção de Medicamentos Antitumorais
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Células HL-60
Neoplasias Hematológicas/metabolismo
Neoplasias Hematológicas/patologia
Seres Humanos
Estrutura Molecular
Puromicina/síntese química
Puromicina/química
Relação Estrutura-Atividade
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Enzyme Inhibitors); 4A6ZS6Q2CL (Puromycin); EC 3.4.11.- (Aminopeptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170814
[St] Status:MEDLINE


  7 / 6801 MEDLINE  
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[PMID]:28776986
[Au] Autor:Zhang N; Yin S; Zhang W; Gong X; Zhang N; Fang K; Ge H
[Ad] Endereço:Institute of Health Sciences, School of Life Sciences, Anhui University , Hefei, Anhui 230601, China.
[Ti] Título:Crystal Structure and Biochemical Characterization of an Aminopeptidase LapB from Legionella pneumophila.
[So] Source:J Agric Food Chem;65(34):7569-7578, 2017 Aug 30.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aminopeptidases are a group of exopeptidases that catalyze the removal of a wide range of N-terminal amino acid residues from peptides and proteins. They have many important commercial applications in the food industry. We determined the crystal structure of an aminopeptidase LapB from Legionella pneumophila. The overall structure reveals that the N-terminal protease-associated (PA) domain presents a new fold and shields the active site cavity of the conserved C-terminal peptidase domain. The steady-state kinetic analysis of LapB and the PA domain deletion mutant indicate that the PA domain inhibited enzyme activity of the peptidase domain. Interestingly, the activity of LapB was largely increased by various organic solvents such as ethanol, propanol, and methanol at the concentration of 60% (v/v). CD analysis provided evidence that organic solvents induce the PA domain conformational changes that eliminate the inhibition role. The unique properties indicate the application potential of LapB in the food processing industry.
[Mh] Termos MeSH primário: Aminopeptidases/química
Proteínas de Bactérias/química
Legionella pneumophila/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminopeptidases/genética
Aminopeptidases/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Cristalização
Cristalografia por Raios X
Legionella pneumophila/química
Legionella pneumophila/genética
Dados de Sequência Molecular
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.4.11.- (Aminopeptidases)
[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:170805
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02849


  8 / 6801 MEDLINE  
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[PMID]:28767648
[Au] Autor:Harrison SE; Harvey MS; Cooper SJB; Austin AD; Rix MG
[Ad] Endereço:Australian Centre for Evolutionary Biology and Biodiversity, School of Biological Sciences, The University of Adelaide, Adelaide, SA, Australia.
[Ti] Título:Across the Indian Ocean: A remarkable example of trans-oceanic dispersal in an austral mygalomorph spider.
[So] Source:PLoS One;12(8):e0180139, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Migidae are a family of austral trapdoor spiders known to show a highly restricted and disjunct distribution pattern. Here, we aim to investigate the phylogeny and historical biogeography of the group, which was previously thought to be vicariant in origin, and examine the biogeographic origins of the genus Moggridgea using a dated multi-gene phylogeny. Moggridgea specimens were sampled from southern Australia and Africa, and Bertmainus was sampled from Western Australia. Sanger sequencing methods were used to generate a robust six marker molecular dataset consisting of the nuclear genes 18S rRNA, 28S rRNA, ITS rRNA, XPNPEP3 and H3 and the mitochondrial gene COI. Bayesian and Maximum Likelihood methods were used to analyse the dataset, and the key dispersal nodes were dated using BEAST. Based on our data, we demonstrate that Moggridgea rainbowi from Kangaroo Island, Australia is a valid member of the otherwise African genus Moggridgea. Molecular clock dating analyses show that the inter-specific divergence of M. rainbowi from African congeners is between 2.27-16.02 million years ago (Mya). This divergence date significantly post-dates the separation of Africa from Gondwana (95 Mya) and therefore does not support a vicariant origin for Australian Moggridgea. It also pre-dates human colonisation of Kangaroo Island, a result which is further supported by the intra-specific divergence date of 1.10-6.39 Mya between separate populations on Kangaroo Island. These analyses provide strong support for the hypothesis that Moggridgea colonised Australia via long-distance trans-Indian Ocean dispersal, representing the first such documented case in a mygalomorph spider.
[Mh] Termos MeSH primário: Distribuição Animal
Especiação Genética
Filogenia
Aranhas/classificação
[Mh] Termos MeSH secundário: África
Aminopeptidases/genética
Animais
Austrália
Teorema de Bayes
Citocromos b/genética
DNA/química
DNA/genética
DNA Mitocondrial/química
DNA Mitocondrial/genética
Histonas/genética
Oceano Índico
Filogeografia
RNA Ribossômico 18S/genética
RNA Ribossômico 28S/genética
Análise de Sequência de DNA
Aranhas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Histones); 0 (RNA, Ribosomal, 18S); 0 (RNA, Ribosomal, 28S); 9007-49-2 (DNA); 9035-37-4 (Cytochromes b); EC 3.4.11.- (Aminopeptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180139


  9 / 6801 MEDLINE  
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[PMID]:28738674
[Au] Autor:Mochizuki S; Morishita H; Sakurai K
[Ad] Endereço:Department of Chemistry and Biochemistry, The University of Kitakyushu , 1-1 Hibikino, Wakamatsu-ku, Kitakyushu, Fukuoka 808-0135, Japan.
[Ti] Título:Complex Consisting of ß-Glucan and Antigenic Peptides with Cleavage Site for Glutathione and Aminopeptidases Induces Potent Cytotoxic T Lymphocytes.
[So] Source:Bioconjug Chem;28(9):2246-2253, 2017 Sep 20.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The efficient induction of antigen-specific immune responses requires not only promotion of the uptake of antigens and adjuvant molecules into antigen-presenting cells but also control of their intracellular behavior. We previously demonstrated that the ß-glucan schizophyllan (SPG) can form complexes with CpG oligonucleotides with attached dA (CpG-dA/SPG), which can accumulate in macrophages in the draining inguinal lymph nodes and induce strong immune responses. In this study, we prepared various conjugates composed of antigenic peptide (OVA ) and dA and made complexes with SPG. The conjugates with a disulfide bond between OVA and dA were easily cleaved by glutathione. The resultant peptides with a hydrophobic amino acid at the C-terminal end was recognized by puromycin-insensitive leucine aminopeptidase (PILS-AP), which trims antigenic peptide precursors and prepares peptides of eight or nine amino acids in length, which is the optimal length for binding to major histocompatibility complex (MHC)-I. The conjugate exposed to such enzymes induced a high antigen presentation level. The antigen presentation level was almost the same before and after the complexation with SPG. Immunization with a mixture of dA-OVA /SPG and CpG-dA/SPG induced high antigen-specific cytotoxic T-lymphocyte activity at a much lower peptide dose than in previous studies. These results can be strongly ascribed to not only the cell-specific delivery by SPG but also the control of the intracellular behavior by the introduction of cleavage sites. Therefore, peptide-dA/SPG complexes could be used as potent vaccine antigens for the treatment of cancers and infectious diseases.
[Mh] Termos MeSH primário: Aminopeptidases/metabolismo
Glutationa/metabolismo
Oligodesoxirribonucleotídeos/imunologia
Ovalbumina/imunologia
Sizofirano/imunologia
Linfócitos T Citotóxicos/imunologia
[Mh] Termos MeSH secundário: Animais
Células Apresentadoras de Antígenos/imunologia
Células Apresentadoras de Antígenos/metabolismo
Controle de Doenças Transmissíveis
Doenças Transmissíveis/imunologia
Doenças Transmissíveis/metabolismo
Imunização
Macrófagos/imunologia
Camundongos
Neoplasias/imunologia
Neoplasias/metabolismo
Neoplasias/prevenção & controle
Oligodesoxirribonucleotídeos/química
Oligodesoxirribonucleotídeos/metabolismo
Ovalbumina/química
Ovalbumina/metabolismo
Sizofirano/química
Sizofirano/metabolismo
Linfócitos T Citotóxicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CPG-oligonucleotide); 0 (Oligodeoxyribonucleotides); 9006-59-1 (Ovalbumin); 9050-67-3 (Sizofiran); EC 3.4.11.- (Aminopeptidases); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00159


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[PMID]:28670957
[Au] Autor:Cheng T; Wei R; Jiang G; Zhou Y; Lv M; Dai Y; Yuan Y; Luo D; Ma D; Li F; Xi L
[Ad] Endereço:Cancer Biology Research Center (Key Laboratory of the Ministry of Education), Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
[Ti] Título:XPNPEP2 is overexpressed in cervical cancer and promotes cervical cancer metastasis.
[So] Source:Tumour Biol;39(7):1010428317717122, 2017 Jul.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:XPNPEP2 is a proline hydrolytic enzyme that hydrolyzes several biologically active peptides and causes a loss of substrate activity. However, its function in cancer is still unknown. Our study showed that XPNPEP2 expression was significantly upregulated in cervical cancer tissues compared with normal cervical tissues and cervical intraepithelial neoplasm tissues. Statistical analysis showed that XPNPEP2 expression was associated with the International Federation of Gynecology and Obstetrics stage and lymph node metastasis. Overexpression of XPNPEP2 in SiHa and HeLa cells promoted cell invasion and migration without affecting cell proliferation and apoptosis. Mechanistically, we found that XPNPEP2 facilitated cervical cancer cell invasion and migration by inducing epithelial-mesenchymal transition. Furthermore, we demonstrated that XPNPEP2 had significant effects on the metastasis of xenografted tumors in vivo. Collectively, our findings identify the novel function of XPNPEP2 in the metastasis of cervical cancer and suggest that XPNPEP2 could be a novel potential therapeutic target for the treatment of cervical cancer.
[Mh] Termos MeSH primário: Aminopeptidases/biossíntese
Proliferação Celular/genética
Prognóstico
Neoplasias do Colo do Útero/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Aminopeptidases/genética
Animais
Apoptose/genética
Movimento Celular/genética
Transição Epitelial-Mesenquimal/genética
Feminino
Regulação Neoplásica da Expressão Gênica
Células HeLa
Seres Humanos
Metástase Linfática/genética
Camundongos
Meia-Idade
Invasividade Neoplásica/genética
Invasividade Neoplásica/patologia
Estadiamento de Neoplasias
Neoplasias do Colo do Útero/patologia
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.11.- (Aminopeptidases); EC 3.4.11.9 (X-Pro aminopeptidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317717122



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