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  1 / 1389 MEDLINE  
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[PMID]:29399876
[Au] Autor:Martínez-García S; Rodríguez-Martínez S; Cancino-Diaz ME; Cancino-Diaz JC
[Ad] Endereço:Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Ciudad de México, Mexico.
[Ti] Título:Extracellular proteases of Staphylococcus epidermidis: roles as virulence factors and their participation in biofilm.
[So] Source:APMIS;126(3):177-185, 2018 Mar.
[Is] ISSN:1600-0463
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:Staphylococci produce a large number of extracellular proteases, some of which are considered as potential virulence factors. Staphylococcus epidermidis is a causative agent of nosocomial infections in medical devices by the formation of biofilms. It has been proposed that proteases contribute to the different stages of biofilm formation. S. epidermidis secretes a small number of extracellular proteases, such as serine protease Esp, cysteine protease EcpA, and metalloprotease SepA that have a relatively low substrate specificity. Recent findings indicate a significant contribution of extracellular proteases in biofilm formation through the proteolytic inactivation of adhesion molecules. The objective of this work is to provide an overview of the current knowledge of S. epidermidis' extracellular proteases during pathogenicity, especially in the different stages of biofilm formation.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Biofilmes/crescimento & desenvolvimento
Cisteína Proteases/metabolismo
Metaloendopeptidases/metabolismo
Serina Proteases/metabolismo
Staphylococcus epidermidis/enzimologia
[Mh] Termos MeSH secundário: Moléculas de Adesão Celular/metabolismo
Infecção Hospitalar/microbiologia
Infecção Hospitalar/patologia
Seres Humanos
Infecções Estafilocócicas/microbiologia
Infecções Estafilocócicas/patologia
Staphylococcus epidermidis/metabolismo
Staphylococcus epidermidis/patogenicidade
Fatores de Virulência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cell Adhesion Molecules); 0 (Virulence Factors); EC 3.4.- (Cysteine Proteases); EC 3.4.- (Serine Proteases); EC 3.4.24.- (Metalloendopeptidases); EC 3.4.24.- (SepA protein, Staphylococcus epidermidis)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180206
[St] Status:MEDLINE
[do] DOI:10.1111/apm.12805


  2 / 1389 MEDLINE  
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[PMID]:28467359
[Au] Autor:Yoshida K; Hai H; Tamori A; Teranishi Y; Kozuka R; Motoyama H; Kawamura E; Hagihara A; Uchida-Kobayashi S; Morikawa H; Enomoto M; Murakami Y; Kawada N
[Ad] Endereço:Department of Hepatology, Osaka City University Graduate School of Medicine, Osaka 545-8585, Japan. m2028081@med.osaka-cu.ac.jp.
[Ti] Título:Long-Term Follow-Up of Resistance-Associated Substitutions in Hepatitis C Virus in Patients in Which Direct Acting Antiviral-Based Therapy Failed.
[So] Source:Int J Mol Sci;18(5), 2017 May 03.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:We evaluated the transition of dominant resistance-associated substitutions (RASs) in hepatitis C virus during long-term follow-up after the failure of DAAs (direct acting antivirals)-based therapy. RASs in non-structure (NS)3/4A, NS5A, NS5B, and deletions in NS5A from 20 patients who failed simeprevir/pegylated-interferon/ribavirin (SMV/PEG-IFN/RBV) and 25 patients who failed daclatasvir/asunaprevir (DCV/ASV) treatment were examined by direct sequencing. With respect to SMV/PEG-IFN/RBV treatment, RAS was detected at D168 in NS3/4A but not detected in NS5A and NS5B at treatment failure in 16 of 20 patients. During the median follow-up period of 64 weeks, the RAS at D168 became less dominant in 9 of 16 patients. Among 25 DCV/ASV failures, RASs at D168, L31, and Y93 were found in 57.1%, 72.2%, and 76.9%, respectively. NS5A deletions were detected in 3 of 10 patients treated previously with SMV/PEG-IFN/RBV. The number of RASs in the breakthrough patients exceeded that in relapsers (mean 3.9 vs. 2.7, < 0.05). RAS at D168 in NS3/4A became less dominant in 6 of 15 patients within 80 weeks. Y93H emerged at the time of relapse, then decreased gradually by 99% at 130 weeks post-treatment. Emerged RASs were associated with the clinical course of treatment and could not be detected during longer follow-up.
[Mh] Termos MeSH primário: Farmacorresistência Viral/genética
Hepacivirus/genética
Hepatite C Crônica/tratamento farmacológico
Serina Proteases/genética
Proteínas não Estruturais Virais/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Antivirais/farmacologia
Antivirais/uso terapêutico
Quimioterapia Combinada
Feminino
Seguimentos
Hepacivirus/efeitos dos fármacos
Hepatite C Crônica/virologia
Seres Humanos
Imidazóis/farmacologia
Imidazóis/uso terapêutico
Interferon-alfa/uso terapêutico
Isoquinolinas/farmacologia
Isoquinolinas/uso terapêutico
Masculino
Meia-Idade
Polietilenoglicóis/uso terapêutico
Inibidores de Proteases/farmacologia
Inibidores de Proteases/uso terapêutico
Proteínas Recombinantes/uso terapêutico
Ribavirina/farmacologia
Ribavirina/uso terapêutico
Simeprevir/farmacologia
Simeprevir/uso terapêutico
Sulfonamidas/farmacologia
Sulfonamidas/uso terapêutico
Fatores de Tempo
Falha de Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (BMS-790052); 0 (Imidazoles); 0 (Interferon-alpha); 0 (Isoquinolines); 0 (NS-5 protein, hepatitis C virus); 0 (Protease Inhibitors); 0 (Recombinant Proteins); 0 (Sulfonamides); 0 (Viral Nonstructural Proteins); 30IQX730WE (Polyethylene Glycols); 49717AWG6K (Ribavirin); 9WS5RD66HZ (Simeprevir); EC 3.4.- (NS3-4A serine protease, Hepatitis C virus); EC 3.4.- (Serine Proteases); G8RGG88B68 (peginterferon alfa-2b); S9X0KRJ00S (asunaprevir)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  3 / 1389 MEDLINE  
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[PMID]:28460881
[Au] Autor:Düsterhöft S; Künzel U; Freeman M
[Ad] Endereço:Dunn School of Pathology, University of Oxford, OX1 3RE, United Kingdom.
[Ti] Título:Rhomboid proteases in human disease: Mechanisms and future prospects.
[So] Source:Biochim Biophys Acta;1864(11 Pt B):2200-2209, 2017 11.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Rhomboids are intramembrane serine proteases that cleave the transmembrane helices of substrate proteins, typically releasing luminal/extracellular domains from the membrane. They are conserved in all branches of life and there is a growing recognition of their association with a wide range of human diseases. Human rhomboids, for example, have been implicated in cancer, metabolic disease and neurodegeneration, while rhomboids in apicomplexan parasites appear to contribute to their invasion of host cells. Recent advances in our knowledge of the structure and the enzyme function of rhomboids, and increasing efforts to identify specific inhibitors, are beginning to provide important insight into the prospect of rhomboids becoming future therapeutic targets. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.
[Mh] Termos MeSH primário: Filogenia
Proteólise
Serina Proteases/genética
[Mh] Termos MeSH secundário: Seres Humanos
Doenças Metabólicas/genética
Terapia de Alvo Molecular
Neoplasias/genética
Degeneração Neural/genética
Serina Proteases/uso terapêutico
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
EC 3.4.- (Serine Proteases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  4 / 1389 MEDLINE  
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Alves, Carlos Roberto
Côrtes, Luzia Monteiro de Castro
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[PMID]:29175018
[Au] Autor:Alves CR; Souza RS; Charret KDS; Côrtes LMC; Sá-Silva MP; Barral-Veloso L; Oliveira LFG; da Silva FS
[Ad] Endereço:Fundação Oswaldo Cruz, Instituto Oswaldo Cruz, Laboratório de Biologia Molecular e Doenças Endêmicas, Avenida Brasil, 4365, Manguinhos, Rio de Janeiro, RJ, CEP: 21040-360, Brazil. Electronic address: calves@ioc.fiocruz.br.
[Ti] Título:Understanding serine proteases implications on Leishmania spp lifecycle.
[So] Source:Exp Parasitol;184:67-81, 2018 Jan.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serine proteases have significant functions over a broad range of relevant biological processes to the Leishmania spp lifecycle. Data gathered here present an update on the Leishmania spp serine proteases and the status of these enzymes as part of the parasite degradome. The serine protease genes (n = 26 to 28) in Leishmania spp, which encode proteins with a wide range of molecular masses (35 kDa-115 kDa), are described along with their degrees of chromosomal and allelic synteny. Amid 17 putative Leishmania spp serine proteases, only ∼18% were experimentally demonstrated, as: signal peptidases that remove the signal peptide from secretory pre-proteins, maturases of other proteins and with metacaspase-like activity. These enzymes include those of clans SB, SC and SF. Classical inhibitors of serine proteases are used as tools for the characterization and investigation of Leishmania spp. Endogenous serine protease inhibitors, which are ecotin-like, can act modulating host actions. However, crude or synthetic based-natural serine protease inhibitors, such as potato tuber extract, Stichodactyla helianthus protease inhibitor I, fukugetin and epoxy-α-lapachone act on parasitic serine proteases and are promising leishmanicidal agents. The functional interrelationship between serine proteases and other Leishmania spp proteins demonstrate essential functions of these enzymes in parasite physiology and therefore their value as targets for leishmaniasis treatment.
[Mh] Termos MeSH primário: Leishmania/enzimologia
Leishmania/crescimento & desenvolvimento
Estágios do Ciclo de Vida
Serina Proteases/metabolismo
Inibidores de Serino Proteinase/farmacologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Leishmania/classificação
Leishmania/genética
Leishmaniose/tratamento farmacológico
Serina Proteases/química
Serina Proteases/classificação
Serina Proteases/genética
Inibidores de Serino Proteinase/química
Inibidores de Serino Proteinase/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Serine Proteinase Inhibitors); EC 3.4.- (Serine Proteases)
[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:171128
[St] Status:MEDLINE


  5 / 1389 MEDLINE  
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[PMID]:27777178
[Au] Autor:Pla D; Sanz L; Sasa M; Acevedo ME; Dwyer Q; Durban J; Pérez A; Rodriguez Y; Lomonte B; Calvete JJ
[Ad] Endereço:Structural and Functional Venomics Laboratory, Instituto de Biomedicina de Valencia, CSIC, Valencia, Spain.
[Ti] Título:Proteomic analysis of venom variability and ontogeny across the arboreal palm-pitvipers (genus Bothriechis).
[So] Source:J Proteomics;152:1-12, 2017 01 30.
[Is] ISSN:1876-7737
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Bothriechis is a genus of eleven currently recognized slender and arboreal venomous snakes, commonly called palm-pitvipers that range from southern Mexico to northern South America. Despite dietary studies suggesting that palm-pitvipers are generalists with an ontogenetic shift toward endothermic prey, venom proteomic analyses have revealed remarkable divergence between the venoms of the Costa Rican species, B. lateralis, B. schlegelii, B. supraciliaris, and B. nigroviridis. To achieve a more complete picture of the venomic landscape across Bothriechis, the venom proteomes of biodiversity of the northern Middle American highland palm-pitvipers, B. thalassinus, B. aurifer, and B. bicolor from Guatemala, B. marchi from Honduras, and neonate Costa Rican B. lateralis and B. schlegelii, were investigated. B. thalassinus and B. aurifer venoms are comprised by similar toxin arsenals dominated by SVMPs (33-39% of the venom proteome), CTLs (11-16%), BPP-like molecules (10-13%), and CRISPs (5-10%), and are characterized by the absence of PLA proteins. Conversely, the predominant (35%) components of B. bicolor are D49-PLA molecules. The venom proteome of B. marchi is similar to B. aurifer and B. thalassinus in that it is rich in SVMPs and BPPs, but also contains appreciable amounts (14.3%) of PLA s. The major toxin family found in the venoms of both neonate B. lateralis and B. schlegelii, is serine proteinase (SVSP), comprising about 20% of their toxin arsenals. The venom of neonate B. schlegelii is the only palm-pitviper venom where relative high amounts of Kunitz-type (6.3%) and γPLA (5.2%) inhibitors have been identified. Despite notable differences between their proteomes, neonate venoms are more similar to each other than to adults of their respective species. However, the ontogenetic changes taking place in the venom of B. lateralis strongly differ from those that occur in the venom of B. schlegelii. Thus, the ontogenetic change in B. lateralis produces a SVMP-rich venom, whereas in B. schlegelii the age-dependent compositional shift generates a PLA -rich venom. Overall, genus-wide venomics illustrate the high evolvability of palm-pitviper venoms. The integration of the pattern of venom variation across Bothriechis into a phylogenetic and biogeographic framework may lay the foundation for assessing, in future studies, the evolutionary path that led to the present-day variability of the venoms of palm-pitvipers. SIGNIFICANCE: Bothriechis represents a monophyletic basal genus of eleven arboreal palm-pitvipers that range from southern Mexico to northern South America. Despite palm-pitvipers' putative status as diet generalists, previous proteomic analyses have revealed remarkable divergence between the venoms of Costa Rican species, B. lateralis, B. schlegelii, B. supraciliaris, and B. nigroviridis. Our current proteomic study of Guatemalan species, B. thalassinus, B. aurifer, and B. bicolor, Honduran B. marchi, and neonate B. lateralis and B. schlegelii from Costa Rica was undertaken to deepen our understanding of the evolutionary pattern of venom proteome diversity across Bothriechis. Ancestral characters are often, but not always, preserved in an organism's development. Venoms of neonate B. lateralis and B. schlegelii are more similar to each other than to adults of their respective species, suggesting that the high evolvability of palm-pitviper venoms may represent an inherent feature of Bothriechis common ancestor. Our genus-wide data identified four nodes of venom phenotype differentiation across the phylogeny of Bothriechis. Integrated into a phylogenetic and biogeographic framework, the pattern of venom variation across Bothriechis may lay the groundwork to establish whether divergence was driven by selection for efficient resource exploitation in arboreal 'islands', thereby contributing to the ecological speciation of the genus.
[Mh] Termos MeSH primário: Biodiversidade
Venenos de Crotalídeos/química
Proteoma/análise
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Evolução Biológica
Venenos de Crotalídeos/enzimologia
Fosfolipases A2/análise
Filogenia
Proteômica/métodos
Serina Proteases/análise
Toxinas Biológicas/análise
Viperidae
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Crotalid Venoms); 0 (Proteome); 0 (Toxins, Biological); EC 3.1.1.4 (Phospholipases A2); EC 3.4.- (Serine Proteases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


  6 / 1389 MEDLINE  
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[PMID]:29244879
[Au] Autor:Lentini G; El Hajj H; Papoin J; Fall G; Pfaff AW; Tawil N; Braun-Breton C; Lebrun M
[Ad] Endereço:UMR 5235 CNRS, Université de Montpellier, Montpellier, France.
[Ti] Título:Characterization of Toxoplasma DegP, a rhoptry serine protease crucial for lethal infection in mice.
[So] Source:PLoS One;12(12):e0189556, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During the infection process, Apicomplexa discharge their secretory organelles called micronemes, rhoptries and dense granules to sustain host cell invasion, intracellular replication and to modulate host cell pathways and immune responses. Herein, we describe the Toxoplasma gondii Deg-like serine protein (TgDegP), a rhoptry protein homologous to High temperature requirement A (HtrA) or Deg-like family of serine proteases. TgDegP undergoes processing in both types I and II strains as most of the rhoptries proteins. We show that genetic disruption of the degP gene does not impact the parasite lytic cycle in vitro but affects virulence in mice. While in a type I strain DegPI appears dispensable for the establishment of an infection, removal of DegPII in a type II strain dramatically impairs the virulence. Finally, we show that KO-DegPII parasites kill immunodeficient mice as efficiently as the wild-type strain indicating that the protease might be involved in the complex crosstalk that the parasite engaged with the host immune response. Thus, this study unravels a novel rhoptry protein in T. gondii important for the establishment of lethal infection.
[Mh] Termos MeSH primário: Proteínas de Protozoários/fisiologia
Serina Proteases/fisiologia
Toxoplasma/enzimologia
Toxoplasmose/parasitologia
[Mh] Termos MeSH secundário: Animais
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos NOD
Camundongos SCID
Processamento de Proteína Pós-Traducional
Proteólise
Toxoplasma/genética
Toxoplasma/patogenicidade
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protozoan Proteins); EC 3.4.- (Serine Proteases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189556


  7 / 1389 MEDLINE  
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[PMID]:29175302
[Au] Autor:Muñoz D; Serrano MK; Hernandez ME; Haller R; Swanson T; Slaton JW; Sinha AA; Wilson MJ
[Ad] Endereço:Investigaciones Cerebrales, Universidad Veracruzana, Xalapa, Veracruz, Mexico; Centro de Investigaciones Cerebrales, Universidad Veracruzana, Xalapa, Veracruz, Mexico.
[Ti] Título:Matrix metalloproteinase and heparin-stimulated serine proteinase activities in post-prostate massage urine of men with prostate cancer.
[So] Source:Exp Mol Pathol;103(3):300-305, 2017 12.
[Is] ISSN:1096-0945
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Proteinases secreted by the prostate gland have a reproductive function in cleaving proteins in the ejaculate and in the female reproductive tract, but some may have a fundamental role in disease and pathological processes including cancer. The purpose of this study was to determine if there were differences in proteinase activities in urine samples collected following prostate massage of men positive (CaP) or negative (no evidence of malignancy, NEM) for biopsy determined prostate cancer. Matrix metalloproteinase (MMP) and serine proteinase activities were detected using protein substrate zymography. There were no differences in activities of MMP-2, proMMP-9, and MMP-9/NGAL (neutrophil gelatinase associated lipocalin) complex (gelatin substrate) in men with detected prostate cancer, although the latter two were somewhat diminished. A caseinolytic activity of about 75kDa inhibited by calcium did not differ between the NEM and CaP groups. Heparin stimulated calcium sensitive gelatinolytic activities of approximately 22, 42, and 60kDa, but did not affect activities of MMP-2, MMP-9, or the 75kDa caseinolytic activity. The 22, 42, and 60kDa activities appear to be serine proteinases since they were inhibited by benzamidine. There was a significant decrease in the 22kDa heparin-stimulated serine proteinase activity in urines of men with cancer. Proteinase expression and activities, perhaps in combination with other potential markers, may prove useful in urine for detection and evaluation of prostate cancer.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/urina
Metaloproteinase 2 da Matriz/urina
Metaloproteinase 9 da Matriz/urina
Neoplasias da Próstata/urina
Serina Proteases/urina
[Mh] Termos MeSH secundário: Idoso
Benzamidinas/administração & dosagem
Cálcio/metabolismo
Heparina/química
Seres Humanos
Lipocalina-2/urina
Masculino
Meia-Idade
Neoplasias da Próstata/enzimologia
Neoplasias da Próstata/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzamidines); 0 (Biomarkers, Tumor); 0 (LCN2 protein, human); 0 (Lipocalin-2); 9005-49-6 (Heparin); EC 3.4.- (Serine Proteases); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9); KUE3ZY3J1F (benzamidine); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171214
[Lr] Data última revisão:
171214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  8 / 1389 MEDLINE  
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[PMID]:27770578
[Au] Autor:Perkin LC; Elpidina EN; Oppert B
[Ad] Endereço:USDA, Agricultural Research Service, Center for Grain and Animal Health Research, 1515 College Avenue, Manhattan, KS, USA.
[Ti] Título:RNA interference and dietary inhibitors induce a similar compensation response in Tribolium castaneum larvae.
[So] Source:Insect Mol Biol;26(1):35-45, 2017 02.
[Is] ISSN:1365-2583
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Tribolium castaneum is a major agriculture pest damaging stored grains and cereal products. The T. castaneum genome contains 26 cysteine peptidase genes, mostly cathepsins L and B, and seven have a major role in digestion. We targeted the expression of the most highly expressed cathepsin L gene on chromosome 10, TC011001, by RNA interference (RNAi), using double-stranded RNA (dsRNA) constructs of different regions of the gene (3', middle, 5' and entire coding regions). RNA sequencing and quantitation (RNA-seq) was used to evaluate knockdown and specificity amongst the treatments. Overall, target gene expression decreased in all treatment groups, but was more severe and specific in dsRNA targeting the 3' and entire coding regions, encoding the proteolytic active site in the enzyme. Additional cysteine cathepsin genes also were down-regulated (off-target effects), but some were up-regulated in response to RNAi treatment. Notably, some serine peptidase genes were increased in expression, especially in dsRNA targeting 5' and middle regions, and the response was similar to the effects of dietary cysteine protease inhibitors. We manually annotated these serine peptidase genes to gain insight into function and relevance to the RNAi study. The data indicate that T. castaneum larvae compensate for the loss of digestive peptidase activity in the larval gut, regardless of the mechanism of disruption.
[Mh] Termos MeSH primário: Catepsina L/genética
Interferência de RNA
Tribolium/genética
[Mh] Termos MeSH secundário: Animais
Catepsina L/metabolismo
Cisteína Proteases/metabolismo
Larva/metabolismo
RNA de Cadeia Dupla
Serina Proteases/metabolismo
Transcriptoma
Tribolium/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Double-Stranded); EC 3.4.- (Cysteine Proteases); EC 3.4.- (Serine Proteases); EC 3.4.22.15 (Cathepsin L)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1111/imb.12269


  9 / 1389 MEDLINE  
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[PMID]:28465236
[Au] Autor:Arya M; Srinivasan M; Rajasekharan R
[Ad] Endereço:Lipidomic Centre, Department of Lipid Science, CSIR-Central Food Technological Research Institute (CFTRI), Academy of Scientific & Innovative Research, Mysore 570020, Karnataka, India.
[Ti] Título:Human alpha beta hydrolase domain containing protein 11 and its yeast homolog are lipid hydrolases.
[So] Source:Biochem Biophys Res Commun;487(4):875-880, 2017 06 10.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian alpha/beta hydrolase domain (ABHD) family of proteins have emerged as key regulators of lipid metabolism and are found to be associated with human diseases. Human α/ß-hydrolase domain containing protein 11 (ABHD11) has recently been predicted as a potential biomarker for human lung adenocarcinoma. In silico analyses of the ABHD11 protein sequence revealed the presence of a conserved lipase motif GXSXG. However, the role of ABHD11 in lipid metabolism is not known. To understand the biological function of ABHD11, we heterologously expressed the human ABHD11 in budding yeast, Saccharomyces cerevisiae. In vivo [ C]acetate labeling of cellular lipids in yeast cells overexpressing ABHD11 showed a decrease in triacylglycerol content. Overexpression of ABHD11 also alters the molecular species of triacylglycerol in yeast. Similar activity was observed in its yeast homolog, Ygr031w. The role of the conserved lipase motif in the hydrolase activity was proven by the mutation of all conserved amino acid residues of GXSXG motif. Collectively, our results demonstrate that human ABHD11 and its yeast homolog YGR031W have a pivotal role in the lipid metabolism.
[Mh] Termos MeSH primário: Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/metabolismo
Serina Proteases/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
Metabolismo dos Lipídeos
Saccharomyces cerevisiae/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.- (ABHD11 protein, human); EC 3.4.- (Serine Proteases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


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[PMID]:29023605
[Au] Autor:Kobayashi H; Otsubo T; Teraoka F; Ikeda K; Seike S; Takahashi E; Okamoto K; Yoshida T; Tsuge H; Yamanaka H
[Ad] Endereço:Laboratory of Molecular Microbiological Science, Faculty of Pharmaceutical Sciences, Hiroshima International University, Hiroshima, Japan.
[Ti] Título:Involvement of the Arg566 residue of Aeromonas sobria serine protease in substrate specificity.
[So] Source:PLoS One;12(10):e0186392, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aeromonas sobria serine protease (ASP) is an extracellular serine protease secreted by the organism. Here, we identified the amino acid residue of ASP that contributes to substrate specificity by using both synthetic peptides and biological protein components. The results showed that the arginine residue at position 566 (Arg-566) of ASP, which is located in the extra occluding region of ASP close to an entrance of the catalytic cavity, is involved in the substrate specificity. A substitutional point mutation of the Arg-566 residue of ASP to Ala residue (ASP[R566A]) caused a decrease of the proteolytic efficiency for a certain substrate. In addition, ASP lost the ability to recognize the primary substrate by such a point mutation, and ASP[R566A] reacted to a wide range of synthetic substrates. It is likely that Arg-566 causes an interaction with the amino acid residue at position P3 of the substrate, which is the third amino acid residue upstream from the cleavage site. Another study using ORF2 protein, a chaperone protein of ASP, further suggested that Arg-566 could also play an important role in interaction with ORF2. We therefore conclude that the Arg-566 residue of ASP is likely responsible for the selection of substrates.
[Mh] Termos MeSH primário: Aeromonas/enzimologia
Arginina/metabolismo
Proteínas de Bactérias/metabolismo
Serina Proteases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arginina/química
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Fibrinogênio/metabolismo
Seres Humanos
Cininogênios/metabolismo
Chaperonas Moleculares/metabolismo
Mutagênese Sítio-Dirigida
Proteólise
Serina Proteases/química
Serina Proteases/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Kininogens); 0 (Molecular Chaperones); 9001-32-5 (Fibrinogen); 94ZLA3W45F (Arginine); EC 3.4.- (Serine Proteases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186392



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