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| Fernandes,B.L.; Anéas,M.A.F.; Juliano,L.; Palma,M.S.; Lebrun,I.; Portaro,F.C.V.. |
| The protease ZapA, secreted by Proteus mirabilis, has been considered to be a virulence factor of this opportunistic bacterium. The control of its expression requires the use of an appropriate methodology, which until now has not been developed. The present study focused on the replacement of azocasein with fluorogenic substrates, and on the definition of enzyme specificity. Eight fluorogenic substrates were tested, and the peptide Abz-Ala-Phe-Arg-Ser-Ala-Ala-Gln-EDDnp was found to be the most convenient for use as an operational substrate for ZapA. A single peptide bond (Arg-Ser) was cleaved with a Km of 4.6 µM, a k cat of 1.73 s-1, and a catalytic efficiency of 376 (mM s)-1. Another good substrate for ZapA was peptide 6... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Metalloprotease; Substrate specificity; Quenched fluorescence peptides; Proteus mirabilis. |
| Ano: 2000 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000700006 |
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| Laskoski,Luciane Maria; Valadão,Carlos Augusto Araújo; Vasconcelos,Rosemeri de Oliveira; Ferrucci,Danilo; Silva,Juliete Aparecida Francisco; Machado,Dagmar Ruth Stach; Doria,Renata Gebara Sampaio; Mendonça,Fabio de Sousa. |
| Twenty horses were used in the experiment, for composed control group, (Cg) instrumented group, (Ig;without intestinal obstruction), treated group (Tg;submitted to intestinal obstruction and hydrocortisone treatment) and non-treated group (Ntg;submitted to intestinal obstruction without treatment). Immunohistochemistry and zymography techniques were used for researches on MMPs 2 and 9 in horse hoof laminae. There was an increase in the expression of MMP-2 in animals of Tg and Ntg. MMP-9 increased on animals from groups Ntg and Ig, however there was no rise of this MMP on the Tg when compared to the other groups in the immunohistochemistry analysis. Based on the results, it was observed that the intestinal injury caused by enterotomy and intestinal... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Laminitis; Metalloprotease; Horse; Zymography; Immunohistochemistry. |
| Ano: 2013 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782013000100012 |
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| De Decker, Sophie; Reynaud, Yann; Saulnier, Denis. |
| The aim of that studywas to explore the hypothesis that a quorumsensingmechanismmodulatesmetalloprotease gene expression of two Vibrio species pathogenic for oyster, at intraspecific (Vibrio splendidus) and interspecific (V. splendidus affecting V. aestuarianus) levels. Metalloprotease activities (Vsm for V. splendidus LGP32 and Vam for V. aestuarianus 02/041) and growth curves obtained by real-time PCR assay revealed cell density-dependent metalloprotease inductions triggered between 12 h and 16 h of culture. A quorum sensing assay was then developed using a conditioned medium prepared from supernatant of a mutant strain of V. splendidus LGP32 unable to produce metalloprotease. Specific real-time qPCR assays targeting metalloprotease genes vsm and vam... |
| Tipo: Text |
Palavras-chave: Quorum sensing; Crassostrea gigas; Vibrio; Metalloprotease; Gene expression. |
| Ano: 2013 |
URL: http://archimer.ifremer.fr/doc/00124/23539/21381.pdf |
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| Chaves-Moreira,Daniele; Senff-Ribeiro,Andrea; Wille,Ana Carolina Martins; Gremski,Luiza Helena; Chaim,Olga Meiri; Veiga,Silvio Sanches. |
| Abstract Brown spiders are venomous arthropods that use their venom for predation and defense. In humans, bites of these animals provoke injuries including dermonecrosis with gravitational spread of lesions, hematological abnormalities and impaired renal function. The signs and symptoms observed following a brown spider bite are called loxoscelism. Brown spider venom is a complex mixture of toxins enriched in low molecular mass proteins (4–40 kDa). Characterization of the venom confirmed the presence of three highly expressed protein classes: phospholipases D, metalloproteases (astacins) and insecticidal peptides (knottins). Recently, toxins with low levels of expression have also been found in Loxosceles venom, such as serine proteases, protease... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Brown spider; Loxosceles; Venom; Toxins; Loxoscelism; Phospholipase-D; Metalloprotease; Insecticidal peptides; Serineprotease; Hyaluronidase. |
| Ano: 2017 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100201 |
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| Rádis-Baptista,G.. |
| Integrins encompass a family of transmembrane heterodimeric proteins of adhesion that maintain cells attached to other cells and to the extracellular matrix (ECM). Integrins work as bi-directional mechanotransducers, conveying mechanical signal from outside to inside the cell through a cascade of phosphorylation signals. On the other hand, the signal from inside to outside controls the strength and affinity of integrin adhesion. As proteins of focal contact, integrins are involved in diverse cell functions, such as cell activation, migration, growth, and survival. In the development of neoplastic disease and metastatic tumor, integrins can influence cancer invasiveness and progression, as well as mediate the formation of new blood vessels (angiogenesis).... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Integrin; Angiogenesis; Cancer; Apoptosis; Snake toxin; Snake venom C-type lectin; Metalloprotease; Disintegrin. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992005000300002 |
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| Cordeiro,Francielle Almeida; Coutinho,Bárbara Marques; Wiezel,Gisele Adriano; Bordon,Karla de Castro Figueiredo; Bregge-Silva,Cristiane; Rosa-Garzon,Nathalia Gonsales; Cabral,Hamilton; Ueberheide,Beatrix; Arantes,Eliane Candiani. |
| Abstract Background: Lachesis muta rhombeata (Lmr) is the largest venomous snake in Latin America and its venom contains mainly enzymatic components, such as serine and metalloproteases, L-amino acid oxidase and phospholipases A2. Metalloproteases comprise a large group of zinc-dependent proteases that cleave basement membrane components such as fibronectin, laminin and collagen type IV. These enzymes are responsible for local and systemic changes, including haemorrhage, myonecrosis and inflammation. This study aimed the isolation and enzymatic characterization of the first metalloprotease (Lmr-MP) from Lmr venom (LmrV). Methods and results: Lmr-MP was purified through two chromatographic steps and submitted to enzymatic characterization. It showed... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Lachesis muta rhombeata; Metalloprotease; Proteases; Snake venom. |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100323 |
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| Menaldo,Danilo L.; Jacob-Ferreira,Anna L.; Bernardes,Carolina P.; Cintra,Adélia C. O.; Sampaio,Suely V.. |
| Background Snake venoms are complex mixtures of inorganic and organic components, mainly proteins and peptides. Standardization of methods for isolating bioactive molecules from snake venoms is extremely difficult due to the complex and highly variable composition of venoms, which can be influenced by factors such as age and geographic location of the specimen. Therefore, this study aimed to standardize a simple purification methodology for obtaining a P-I class metalloprotease (MP) and an acidic phospholipase A2 (PLA 2 ) from Bothrops atroxvenom, and biochemically characterize these molecules to enable future functional studies.Methods To obtain the toxins of interest, a method has been standardized using consecutive isolation steps. The purity level of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Snake venoms; Bothrops atrox; Toxins; Metalloprotease; Phospholipase A2; Isolation; Characterization; Chromatography. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100337 |
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| Labreuche, Yannick; Le Roux, Frederique; Henry, Joel; Zatylny, Celine; Huvet, Arnaud; Lambert, Christophe; Soudant, Philippe; Mazel, Didier; Nicolas, Jean-louis. |
| Extracellular products (ECPs) of the pathogenic Vibrio aestuarianus 01/32 were previously reported to display lethality in Crassostrea gigas oysters and to cause morphological changes and immunosuppression in oyster hemocytes. To identify the source of this toxicity, biochemical and genetic approaches were developed. ECP protease activity and lethality were shown to be significantly reduced following incubation with metal chelators, suggesting the involvement of a zinc metalloprotease. An open reading frame of 1836 bp encoding a 611-aa metalloprotease (designated yam) was identified. The deduced protein sequence showed high homology to other Vibrio metalloproteases reported to be involved in pathogenicity. To further confirm the role of this enzyme in ECP... |
| Tipo: Text |
Palavras-chave: Vibrio aestuarianus; Metalloprotease; Crassostrea gigas; Oyster; Hemocytes; Extracellular products. |
| Ano: 2010 |
URL: http://archimer.ifremer.fr/doc/00015/12649/9588.pdf |
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| Anéas,M.A.F.; Portaro,F.C.V.; Lebrun,I.; Juliano,L.; Palma,M.S.; Fernandes,B.L.. |
| The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides derived from bioactive peptides and the oxidized ß-chain of insulin to determine the enzyme specificity. The bradykinin- and dynorphin-derived peptides were cleaved at the single bonds Phe-Ser and Phe-Leu, with catalytic efficiencies of 291 and 13 mM/s, respectively. Besides confirming already published cleavage sites, a novel cleavage site was determined for the ß-chain of insulin (Val-Asn). Both the natural and the recombinant enzyme displayed the same broad... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Proteus mirabilis; Metalloprotease; Substrate specificity; Fluorogenic peptides; IgA; Insulin ß-chain. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004 |
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| Registros recuperados: 10 | |
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