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Pesquisa : D12.644.138 [Categoria DeCS]
Referências encontradas : 791 [refinar]
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[PMID]:29200855
[Au] Autor:Gerstenhaber JA; Barone FC; Marcinkiewicz C; Li J; Shiloh AO; Sternberg M; Lelkes PI; Feuerstein G
[Ad] Endereço:Department of Bioengineering, College of Engineering, Temple University, Philadelphia, PA.
[Ti] Título:Vascular thrombus imaging in vivo via near-infrared fluorescent nanodiamond particles bioengineered with the disintegrin bitistatin (Part II).
[So] Source:Int J Nanomedicine;12:8471-8482, 2017.
[Is] ISSN:1178-2013
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:The aim of this feasibility study was to test the ability of fluorescent nanodiamond particles (F-NDP) covalently conjugated with bitistatin (F-NDP-Bit) to detect vascular blood clots in vivo using extracorporeal near-infrared (NIR) imaging. Specifically, we compared NIR fluorescence properties of F-NDP with N-V (F-NDP ) and N-V-N color centers and sizes (100-10,000 nm). Optimal NIR fluorescence and tissue penetration across biological tissues (rat skin, porcine axillary veins, and skin) was obtained for F-NDP with a mean diameter of 700 nm. Intravital imaging (using in vivo imaging system [IVIS]) in vitro revealed that F-NDP -loaded glass capillaries could be detected across 6 mm of rat red-muscle barrier and 12 mm of porcine skin, which equals the average vertical distance of a human carotid artery bifurcation from the surface of the adjacent skin (14 mm). In vivo, feasibility was demonstrated in a rat model of occlusive blood clots generated using FeCl in the carotid artery bifurcation. Following systemic infusions of F-NDP -Bit (3 or 15 mg/kg) via the external carotid artery or femoral vein (N=3), presence of the particles in the thrombi was confirmed both in situ via IVIS, and ex vivo via confocal imaging. The presence of F-NDP in the vascular clots was further confirmed by direct counting of fluorescent particles extracted from clots following tissue solubilization. Our data suggest that F-NDP -Bit associate with vascular blood clots, presumably by binding of F-NDP -Bit to activated platelets within the blood clot. We posit that F-NDP -Bit could serve as a noninvasive platform for identification of vascular thrombi using NIR energy monitored by an extracorporeal device.
[Mh] Termos MeSH primário: Bioengenharia/métodos
Diagnóstico por Imagem
Desintegrinas/química
Raios Infravermelhos
Nanodiamantes/química
Peptídeos/química
Trombose/diagnóstico
[Mh] Termos MeSH secundário: Animais
Artérias Carótidas/patologia
Modelos Animais de Doenças
Desintegrinas/administração & dosagem
Fluorescência
Seres Humanos
Infusões Intravenosas
Masculino
Peptídeos/administração & dosagem
Ratos Sprague-Dawley
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disintegrins); 0 (Nanodiamonds); 0 (Peptides); 124123-27-9 (bitistatin)
[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:171205
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S146946


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[PMID]:28823917
[Au] Autor:Shih CH; Chiang TB; Wang WJ
[Ad] Endereço:Chang Gung University of Science and Technology, Guishan Dist., Taoyuan City, Taiwan.
[Ti] Título:Synergistic suppression of a disintegrin acurhagin-C in combination with AZD4547 and reparixin on terminating development for human osteosarcoma MG-63 cell.
[So] Source:Biochem Biophys Res Commun;492(3):513-519, 2017 Oct 21.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Current therapies available for the treatment of human osteosarcoma, an aggressive bone tumor, are insufficient. To examine an alternative approach of integrin-based anti-osteosacoma strategy, acurhagin-C, a Glu-Cys-Asp (ECD)-disintegrin, was isolated and evaluated for its application in combination with two potent inhibitors of basic fibroblast growth factor (bFGF) and interleukin-8 (IL-8). The investigation of human osteosarcoma MG-63 cells pre-incubated with a FGF receptor-1 (FGFR-1) blocker AZD4547, a CXC-chemokine receptor-1/-2 (CXCR1/2) antagonist reparixin, and acurhagin-C via two given modes of separation and combination was executed. Detected by flow cytometry, integrins-α2/-α5/-αv/-ß1, FGFR-1, CXCR1 and CXCR2 constitutively express on the resting membrane. However, bFGF/IL-8-activated MG-63 cells only statistically enhanced the surface exposure of integrins-α5/-ß1, FGFR-1 and CXCR2. In activated MG-63 cells, acurhagin-C targeting integrin-α5 not only might potentiate the inhibitory effect of AZD4547 and reparixin on the surface expression of integrin-α5, FGFR-1 and CXCR2, but also acurhagin-C used alone remained effectively to diminish the surface exposure of those targeted receptors. Hence, a complicated crosstalk mechanism should be involved in the membrane interactions. Furthermore, co-administration of acurhagin-C with AZD4547 and reparixin also showed to have the synergistic suppression toward cell proliferation and the gene expression of matrix metalloproteinase-2. Also, the administration of three-in-one mode could nearly abrogate the cellular attachment onto collagen-IV- and fibronectin-coated wells, as well as penetration into Matrigel-barrier. These data supported an ECD-disintegrin acurhagin-C targeting integrin-α5 upon combined used with AZD4547 and reparixin may become a promising therapeutic approach for attenuating osteosarcoma development.
[Mh] Termos MeSH primário: Benzamidas/farmacologia
Desintegrinas/farmacologia
Osteossarcoma/tratamento farmacológico
Osteossarcoma/patologia
Piperazinas/farmacologia
Pirazóis/farmacologia
Sulfonamidas/farmacologia
[Mh] Termos MeSH secundário: Benzamidas/química
Proliferação Celular/efeitos dos fármacos
Desintegrinas/química
Desintegrinas/isolamento & purificação
Seres Humanos
Piperazinas/química
Pirazóis/química
Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/antagonistas & inibidores
Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/metabolismo
Receptores de Interleucina-8B/antagonistas & inibidores
Receptores de Interleucina-8B/metabolismo
Sulfonamidas/química
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-(4-isobutylphenyl)propionylmethanesulfonamide); 0 (AZD4547); 0 (Benzamides); 0 (Disintegrins); 0 (Piperazines); 0 (Pyrazoles); 0 (Receptors, Interleukin-8B); 0 (Sulfonamides); EC 2.7.10.1 (Receptor, Fibroblast Growth Factor, Type 1)
[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:170822
[St] Status:MEDLINE


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[PMID]:28437464
[Au] Autor:Montenegro CF; Casali BC; Lino RLB; Pachane BC; Santos PK; Horwitz AR; Selistre-de-Araujo HS; Lamers ML
[Ad] Endereço:Department of Physiological Sciences, Center of Biological and Health Science, Federal University of São Carlos, Rod. Washington Luis, São Carlos, São Paulo, Brazil, CEP.
[Ti] Título:Inhibition of αvß3 integrin induces loss of cell directionality of oral squamous carcinoma cells (OSCC).
[So] Source:PLoS One;12(4):e0176226, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The connective tissue formed by extracellular matrix (ECM) rich in fibronectin and collagen consists a barrier that cancer cells have to overpass to reach blood vessels and then a metastatic site. Cell adhesion to fibronectin is mediated by αvß3 and α5ß1 integrins through an RGD motif present in this ECM protein, thus making these receptors key targets for cell migration studies. Here we investigated the effect of an RGD disintegrin, DisBa-01, on the migration of human fibroblasts (BJ) and oral squamous cancer cells (OSCC, SCC25) on a fibronectin-rich environment. Time-lapse images were acquired on fibronectin-coated glass-bottomed dishes. Migration speed and directionality analysis indicated that OSCC cells, but not fibroblasts, showed significant decrease in both parameters in the presence of DisBa-01 (1µM and 2µM). Integrin expression levels of the α5, αv and ß3 subunits were similar in both cell lines, while ß1 subunit is present in lower levels on the cancer cells. Next, we examined whether the effects of DisBa-01 were related to changes in adhesion properties by using paxillin immunostaining and total internal reflection fluorescence TIRF microscopy. OSCCs in the presence of DisBa-01 showed increased adhesion sizes and number of maturing adhesion. The same parameters were analyzed usingß3-GFP overexpressing cells and showed that ß3 overexpression restored cell migration velocity and the number of maturing adhesion that were altered by DisBa-01. Surface plasmon resonance analysis showed that DisBa-01 has 100x higher affinity for αvß3 integrin than forα5ß1 integrin. In conclusion, our results suggest that the αvß3 integrin is the main receptor involved in cell directionality and its blockage may be an interesting alternative against metastasis.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/metabolismo
Adesão Celular/efeitos dos fármacos
Movimento Celular/efeitos dos fármacos
Integrina alfaVbeta3/metabolismo
Neoplasias Bucais/metabolismo
[Mh] Termos MeSH secundário: Carcinoma de Células Escamosas/patologia
Linhagem Celular Tumoral
Venenos de Crotalídeos/farmacologia
Desintegrinas/farmacologia
Matriz Extracelular/metabolismo
Fibroblastos/metabolismo
Fibronectinas/metabolismo
Seres Humanos
Neoplasias Bucais/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crotalid Venoms); 0 (DisBa-01, Bothrops alternatus); 0 (Disintegrins); 0 (Fibronectins); 0 (Integrin alphaVbeta3)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0176226


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[PMID]:28373586
[Au] Autor:Wang X; Chen W; Zhang J; Khan A; Li L; Huang F; Qiu Z; Wang L; Chen X
[Ad] Endereço:From the Department of Thoracic and Cardiovascular Surgery, Nanjing First Hospital, Nanjing Medical University, Jiangsu, People's Republic of China.
[Ti] Título:Critical Role of ADAMTS2 (A Disintegrin and Metalloproteinase With Thrombospondin Motifs 2) in Cardiac Hypertrophy Induced by Pressure Overload.
[So] Source:Hypertension;69(6):1060-1069, 2017 Jun.
[Is] ISSN:1524-4563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ADAMTS2 (A Disintegrin and Metalloproteinase With Thrombospondin Motifs 2) is recognized as a metalloproteinase that promotes the cleavage of amino propeptides of types I, II, III, and V procollagens. However, the role of ADAMTS2 in the heart has not yet been defined. Herein, we observed the upregulated expression of ADAMTS2 in failing human hearts and hypertrophic murine hearts. Mice lacking ADAMTS2 display exacerbated cardiac hypertrophy on pressure overload-induced hypertrophic response, whereas mice with cardiac-specific overexpression of ADAMTS2 display alleviation of this detrimental phenotype. Consistent with these results, in vitro loss or gain of function experiments in neonatal rat cardiomyocytes confirmed that ADAMTS2 negatively regulates cardiomyocyte hypertrophy in response to Ang II. Mechanistically, blockage of the PI3K (phosphoinositide 3-kinase)/AKT (protein kinase B)-dependent signaling pathway with specific inhibitors both in vivo and in vitro could rescue the aggravated hypertrophic response to the loss of ADAMTS2. Collectively, we propose that ADAMTS2 regulates the hypertrophic response through inhibiting the activation of the PI3K/AKT-dependent signaling pathway. Because ADAMTS2 is an extracellular protein, it could be effectively manipulated using pharmacological means to modulate cardiac hypertrophy.
[Mh] Termos MeSH primário: Proteínas ADAMTS/genética
Cardiomegalia/genética
Transdução de Sinais/genética
Trombospondinas/genética
Regulação para Cima
[Mh] Termos MeSH secundário: Angiotensina II/farmacologia
Animais
Biópsia por Agulha
Cardiomegalia/patologia
Modelos Animais de Doenças
Desintegrinas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Metaloproteases/metabolismo
Camundongos
Camundongos Transgênicos
Miócitos Cardíacos/metabolismo
Miócitos Cardíacos/patologia
Fosfatidilinositol 3-Quinases/metabolismo
Fosforilação/genética
Proteínas Proto-Oncogênicas c-akt/metabolismo
Distribuição Aleatória
Técnicas de Cultura de Tecidos
Disfunção Ventricular Esquerda/genética
Disfunção Ventricular Esquerda/patologia
Remodelação Ventricular/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disintegrins); 0 (Thrombospondins); 0 (thrombospondin 2); 11128-99-7 (Angiotensin II); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.4.- (Metalloproteases); EC 3.4.24.- (ADAMTS Proteins); EC 3.4.24.14 (ADAMTS2 protein, human); EC 3.4.24.14 (Adamts2 protein, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1161/HYPERTENSIONAHA.116.08581


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[PMID]:28315346
[Au] Autor:Lin TH; Yang RS; Tu HJ; Liou HC; Lin YM; Chuang WJ; Fu WM
[Ad] Endereço:Department of Pharmacology, College of Medicine, National Taiwan University, No.1, Section 1, Jen-Ai Rd., Taipei 10051, Taiwan; Material and Chemical Research Laboratories, Industrial Technology Research Institute, No.195, Section 4, Chung Hsing Rd., Hsinchu 31040, Taiwan.
[Ti] Título:Inhibition of osteoporosis by the αvß3 integrin antagonist of rhodostomin variants.
[So] Source:Eur J Pharmacol;804:94-101, 2017 Jun 05.
[Is] ISSN:1879-0712
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Integrins are heterodimeric cell surface receptors that mediate cell-cell and cell-matrix interaction. The vitronectin and osteopontin receptor αvß3 integrin has increased expression levels and is implicated in the adhesion, activation, and migration of osteoclasts on the bone surface as well as osteoclast polarization. αvß3 integrin plays an important role in osteoclast differentiation and resorption. In addition, Arg-Gly-Asp (RGD)-containing peptides, small molecular inhibitors, and antibodies to αvß3 integrin have been shown to inhibit bone resorption in vitro and in vivo. Here we examined the effects of a disintegrin HSA-ARLDDL a genetically modified mutant of rhodostomin conjugated with human serum albumin, which is highly selective of αvß3, on RANKL-induced osteoclastogenesis and ovariectomy (OVX)-induced osteoporosis. In RANKL-induced osteoclastogenesis, HSA-ARLDDL significantly inhibited osteoclast formation, and IC was at nM range. Post-treatment HSA-ARLDDL also inhibits osteoclast formation. Furthermore, weekly administration of HSA-ARLDDL significantly inhibits the increase in serum bone resorption marker levels and decrease in cancellous bone loss in tibia and femur induced by OVX. On the other hand, HSA-ARLDDL did not affect the differentiation and calcium deposition of osteoblasts. These results indicate that the highly selective and long-acting αvß3 integrin antagonists could be developed as effective drugs for postmenopausal osteoporosis.
[Mh] Termos MeSH primário: Desintegrinas/farmacologia
Integrina alfaVbeta3/antagonistas & inibidores
Mutação
Osteoporose/tratamento farmacológico
Peptídeos/genética
[Mh] Termos MeSH secundário: Animais
Desintegrinas/química
Desintegrinas/metabolismo
Desintegrinas/uso terapêutico
Feminino
Seres Humanos
Masculino
Camundongos
Oligopeptídeos/química
Peptídeos/metabolismo
Domínios Proteicos
Ratos
Albumina Sérica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disintegrins); 0 (Integrin alphaVbeta3); 0 (Oligopeptides); 0 (Peptides); 0 (Serum Albumin); 127829-86-1 (rhodostomin); 78VO7F77PN (arginyl-glycyl-aspartic acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170319
[St] Status:MEDLINE


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[PMID]:28282546
[Au] Autor:Burdelski C; Fitzner M; Hube-Magg C; Kluth M; Heumann A; Simon R; Krech T; Clauditz T; Büscheck F; Steurer S; Wittmer C; Hinsch A; Luebke AM; Jacobsen F; Minner S; Tsourlakis MC; Beyer B; Steuber T; Thederan I; Sauter G; Izbicki J; Schlomm T; Wilczak W
[Ad] Endereço:Institute of Pathology, University Medical Center Hamburg-Eppendorf, Germany; General, Visceral and Thoracic Surgery Department and Clinic, University Medical Center Hamburg-Eppendorf, Germany.
[Ti] Título:Overexpression of the A Disintegrin and Metalloproteinase ADAM15 is linked to a Small but Highly Aggressive Subset of Prostate Cancers.
[So] Source:Neoplasia;19(4):279-287, 2017 Apr.
[Is] ISSN:1476-5586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The A Disintegrin and Metalloproteinase (ADAM) family of endopeptidases plays a role in many solid cancers and includes promising targets for anticancer therapies. Deregulation of ADAM15 has been linked to tumor aggressiveness and cell line studies suggest that ADAM15 overexpression may also be implicated in prostate cancer. To evaluate the impact of ADAM15 expression and its relationship with key genomic alterations, a tissue microarray containing 12,427 prostate cancers was analyzed by immunohistochemistry. ADAM15 expression was compared to phenotype, prognosis and molecular features including TMPRSS2:ERG fusion and frequent deletions involving PTEN, 3p, 5q and 6q. Normal prostate epithelium did not show ADAM15 staining. In prostate cancers, negative, weak, moderate, and strong ADAM15 staining was found in 87.7%, 3.7%, 5.6%, and 3.0% of 9826 interpretable tumors. Strong ADAM15 staining was linked to high Gleason grade, advanced pathological tumor stage, positive nodal stage and resection margin. ADAM15 overexpression was also associated with TMPRSS2:ERG fusions and PTEN deletions (P<.0001) but unrelated to deletions of 3p, 5q and 6q. In univariate analysis, high ADAM15 expression was strongly linked to PSA recurrence (P<.0001). However, in multivariate analyses this association was only maintained if the analysis was limited to preoperatively available parameters in ERG-negative cancers. The results of our study demonstrate that ADAM15 is strongly up regulated in a small but highly aggressive fraction of prostate cancers. In these tumors, ADAM15 may represent a suitable drug target. In a preoperative scenario, ADAM15 expression measurement may assist prognosis assessment, either alone or in combination with other markers.
[Mh] Termos MeSH primário: Proteínas ADAM/metabolismo
Biomarcadores Tumorais
Desintegrinas/genética
Proteínas de Membrana/metabolismo
Neoplasias da Próstata/metabolismo
Neoplasias da Próstata/patologia
[Mh] Termos MeSH secundário: Proteínas ADAM/genética
Adulto
Idoso
Idoso de 80 Anos ou mais
Progressão da Doença
Desintegrinas/metabolismo
Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Hibridização in Situ Fluorescente
Masculino
Proteínas de Membrana/genética
Meia-Idade
Gradação de Tumores
Recidiva Local de Neoplasia
Estadiamento de Neoplasias
Proteínas de Fusão Oncogênicas/genética
Proteínas de Fusão Oncogênicas/metabolismo
Prognóstico
Antígeno Prostático Específico
Neoplasias da Próstata/genética
Neoplasias da Próstata/mortalidade
Deleção de Sequência
Serina Endopeptidases/genética
Serina Endopeptidases/metabolismo
Análise de Sobrevida
Regulador Transcricional ERG/genética
Regulador Transcricional ERG/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Disintegrins); 0 (Membrane Proteins); 0 (Oncogene Proteins, Fusion); 0 (Transcriptional Regulator ERG); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (TMPRSS2 protein, human); EC 3.4.21.77 (Prostate-Specific Antigen); EC 3.4.24.- (ADAM Proteins); EC 3.4.24.- (ADAM15 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170311
[St] Status:MEDLINE


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[PMID]:28264436
[Au] Autor:Shimokawa-Falcão LH; Caporrino MC; Barbaro KC; Della-Casa MS; Magalhães GS
[Ad] Endereço:Laboratory of Immunopathology, Butantan Institute, Av. Vital Brazil 1500, 05503-900 São Paulo, SP, Brazil. lhiri.hanna@gmail.com.
[Ti] Título:Toxin Fused with SUMO Tag: A New Expression Vector Strategy to Obtain Recombinant Venom Toxins with Easy Tag Removal inside the Bacteria.
[So] Source:Toxins (Basel);9(3), 2017 Feb 27.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Many animal toxins may target the same molecules that need to be controlled in certain pathologies; therefore, some toxins have led to the formulation of drugs that are presently used, and many other drugs are still under development. Nevertheless, collecting sufficient toxins from the original source might be a limiting factor in studying their biological activities. Thus, molecular biology techniques have been applied in order to obtain large amounts of recombinant toxins into . However, most animal toxins are difficult to express in this system, which results in insoluble, misfolded, or unstable proteins. To solve these issues, toxins have been fused with tags that may improve protein expression, solubility, and stability. Among these tags, the SUMO (small ubiquitin-related modifier) has been shown to be very efficient and can be removed by the Ulp1 protease. However, removing SUMO is a labor- and time-consuming process. To enhance this system, here we show the construction of a bicistronic vector that allows the expression of any protein fused to both the SUMO and Ulp1 protease. In this way, after expression, Ulp1 is able to cleave SUMO and leave the protein interest-free and ready for purification. This strategy was validated through the expression of a new phospholipase D from the spider and a disintegrin from the snake. Both recombinant toxins showed good yield and preserved biological activities, indicating that the bicistronic vector may be a viable method to produce proteins that are difficult to express.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/genética
Proteína SUMO-1/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Artrópodes/genética
Proteínas de Artrópodes/toxicidade
Plaquetas/efeitos dos fármacos
Bothrops
Venenos de Crotalídeos/genética
Venenos de Crotalídeos/toxicidade
Cisteína Endopeptidases/metabolismo
Desintegrinas/genética
Desintegrinas/toxicidade
Escherichia coli/genética
Seres Humanos
Fosfolipase D/genética
Fosfolipase D/toxicidade
Agregação Plaquetária/efeitos dos fármacos
Inibidores da Agregação de Plaquetas/toxicidade
Proteínas Recombinantes de Fusão/toxicidade
Proteína SUMO-1/metabolismo
Venenos de Aranha
Aranhas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Crotalid Venoms); 0 (Disintegrins); 0 (Platelet Aggregation Inhibitors); 0 (Recombinant Fusion Proteins); 0 (SUMO-1 Protein); 0 (Spider Venoms); 0 (insularin, Bothrops insularis); EC 3.1.4.4 (Phospholipase D); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.- (Ulp1 protease)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE


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[PMID]:28260841
[Au] Autor:Dreymueller D; Theodorou K; Donners M; Ludwig A
[Ad] Endereço:Institute of Pharmacology and Toxicology, Uniklinik RWTH Aachen, Aachen, Germany.
[Ti] Título:Fine Tuning Cell Migration by a Disintegrin and Metalloproteinases.
[So] Source:Mediators Inflamm;2017:9621724, 2017.
[Is] ISSN:1466-1861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell migration is an instrumental process involved in organ development, tissue homeostasis, and various physiological processes and also in numerous pathologies. Both basic cell migration and migration towards chemotactic stimulus consist of changes in cell polarity and cytoskeletal rearrangement, cell detachment from, invasion through, and reattachment to their neighboring cells, and numerous interactions with the extracellular matrix. The different steps of immune cell, tissue cell, or cancer cell migration are tightly coordinated in time and place by growth factors, cytokines/chemokines, adhesion molecules, and receptors for these ligands. This review describes how a disintegrin and metalloproteinases interfere with several steps of cell migration, either by proteolytic cleavage of such molecules or by functions independent of proteolytic activity.
[Mh] Termos MeSH primário: Movimento Celular
Desintegrinas/metabolismo
Metaloproteases/metabolismo
[Mh] Termos MeSH secundário: Animais
Catálise
Adesão Celular
Quimiocinas/metabolismo
Quimiotaxia
Citoesqueleto/metabolismo
Homeostase
Seres Humanos
Inflamação/metabolismo
Leucócitos/metabolismo
Ligantes
Invasividade Neoplásica
Neoplasias/patologia
Neovascularização Fisiológica
Cicatrização
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chemokines); 0 (Disintegrins); 0 (Ligands); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170307
[St] Status:MEDLINE
[do] DOI:10.1155/2017/9621724


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[PMID]:27993561
[Au] Autor:Shen M; Morton J; Davidge ST; Kassiri Z
[Ad] Endereço:Department of Physiology, University of Alberta, Edmonton, Alberta, Canada; Cardiovascular Research Centre, Mazankowski Alberta Heart Institute, University of Alberta, Edmonton, Alberta, Canada.
[Ti] Título:Loss of smooth muscle cell disintegrin and metalloproteinase 17 transiently suppresses angiotensin II-induced hypertension and end-organ damage.
[So] Source:J Mol Cell Cardiol;103:11-21, 2017 Feb.
[Is] ISSN:1095-8584
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Hypertension is associated with hypertrophy and hyperplasia of smooth muscle cells (SMCs). Disintegrin and metalloproteinase 17 (ADAM17) is a membrane-bound enzyme reported to mediate SMC hypertrophy through activation of epidermal growth factor receptor (EGFR). We investigated the role of ADAM17 in Ang II-induced hypertension and end-organ damage. VSMC was isolated from mice with intact ADAM17 expression (Adam17 ) or lacking ADAM17 in the SMC (Adam17 /Cre ). Human VSMCs were isolated from the aorta of donors, and ADAM17 deletion was achieved by siRNA transfection. Ang II suppressed proliferation and migration of Adam17-deficient SMCs, but did not affect apoptosis (mouse and human), this was associated with reduced activation of EGFR and Erk1/2 signaling. Adam17 /Cre and littermate Adam17 mice received saline or Ang II (Alzet pumps, 1.5mg/kg/d; 2 or 4weeks). Daily blood pressure measurement in conscious mice (telemetry) showed suppressed hypertension in Adam17 /Cre mice during the first week of Ang II infusion, but by the second week, it become comparable to that in Adam17 mice. EGFR activation remained suppressed in Adam17 /Cre -Ang II arteries. Ex vivo vascular function and compliance assessed in mesenteric arteries were comparable between genotypes. Consistent with the transient protection against Ang II-induced hypertension, Adam17 /Cre mice exhibited significantly lower cardiac hypertrophy and fibrosis, and renal fibrosis at 2weeks post-Ang II, however this protection was abolished by the fourth week of Ang II infusion. In conclusion, while Adam17-deficiency suppresses Ang II-induced SMC remodeling in vitro, in vivo Adam17-deficiency provides only a transient protective effect against Ang II-mediated hypertension and end-organ damage.
[Mh] Termos MeSH primário: Angiotensina II/metabolismo
Desintegrinas/metabolismo
Hipertensão/etiologia
Hipertensão/metabolismo
Metaloproteinase 17 da Matriz/metabolismo
Miócitos de Músculo Liso/metabolismo
[Mh] Termos MeSH secundário: Angiotensina II/efeitos adversos
Animais
Apoptose
Modelos Animais de Doenças
Seres Humanos
Hipertensão/patologia
Masculino
Metaloproteinase 17 da Matriz/deficiência
Metaloproteinase 17 da Matriz/genética
Camundongos
Camundongos Knockout
Músculo Liso Vascular/metabolismo
Receptor do Fator de Crescimento Epidérmico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disintegrins); 11128-99-7 (Angiotensin II); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 3.4.24.- (Matrix Metalloproteinase 17)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE


  10 / 791 MEDLINE  
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[PMID]:27989783
[Au] Autor:Cantú E; Mallela S; Nyguen M; Báez R; Parra V; Johnson R; Wilson K; Suntravat M; Lucena S; Rodríguez-Acosta A; Sánchez EE
[Ad] Endereço:National Natural Toxins Research Center (NNTRC), Texas A&M University-Kingsville, MSC 224, 975 West Avenue B, Kingsville, TX 78363, USA.
[Ti] Título:The binding effectiveness of anti-r-disintegrin polyclonal antibodies against disintegrins and PII and PIII metalloproteases: An immunological survey of type A, B and A+B venoms from Mohave rattlesnakes.
[So] Source:Comp Biochem Physiol C Toxicol Pharmacol;191:168-176, 2017 Jan.
[Is] ISSN:1532-0456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Snake venoms are known to have different venom compositions and toxicity, but differences can also be found within populations of the same species contributing to the complexity of treatment of envenomated victims. One of the first well-documented intraspecies venom variations comes from the Mohave rattlesnake (Crotalus scutulatus scutulatus). Initially, three types of venoms were described; type A venom is the most toxic as a result of ~45% Mojave toxin in the venom composition, type B lacks the Mojave toxin but contains over 50% of snake venom metalloproteases (SVMPs). Also, type A+B venom contains a combination of Mojave toxin and SVMP. The use of an anti-disintegrin antibody in a simple Enzyme-Linked Immunosorbent Assay (ELISA) can be used to identify the difference between the venoms of the type A, B, and A+B Mohave rattlesnakes. This study implements the use of an anti-recombinant disintegrin polyclonal antibody (ARDPA) for the detection of disintegrins and ADAMs (a disintegrin and metalloproteases) in individual crude snake venoms of Mohave rattlesnakes (Crotalus scutulatus scutulatus) of varying geographical locations. After correlation with Western blots, coagulation activity and LD data, it was determined that the antibody allows for a quick and cost-efficient identification of venom types.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/imunologia
Venenos de Crotalídeos/imunologia
Crotalus/imunologia
Desintegrinas/imunologia
Metaloproteases/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/metabolismo
Arizona
Coagulação Sanguínea/efeitos dos fármacos
Western Blotting
California
Venenos de Crotalídeos/classificação
Venenos de Crotalídeos/metabolismo
Crotalus/metabolismo
Desintegrinas/metabolismo
Ensaio de Imunoadsorção Enzimática
Geografia
Seres Humanos
Dose Letal Mediana
Metaloproteases/metabolismo
Camundongos Endogâmicos BALB C
Neurotoxinas/imunologia
Neurotoxinas/metabolismo
Neurotoxinas/toxicidade
Ligação Proteica/imunologia
Texas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Crotalid Venoms); 0 (Disintegrins); 0 (Neurotoxins); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161220
[St] Status:MEDLINE



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