Base de dados : MEDLINE
Pesquisa : D06.472.910.800 [Categoria DeCS]
Referências encontradas : 670 [refinar]
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[PMID]:27756319
[Au] Autor:Zhang L; Wang G; Chen S; Ding J; Ju S; Cao H; Tian H
[Ad] Endereço:Department of Neurosurgery, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, School of Medicine, Shanghai Jiao Tong University, No. 600 Yishan Road, Xuhui District, Shanghai, 200233, China.
[Ti] Título:Depletion of thymopoietin inhibits proliferation and induces cell cycle arrest/apoptosis in glioblastoma cells.
[So] Source:World J Surg Oncol;14(1):267, 2016 Oct 19.
[Is] ISSN:1477-7819
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Glioblastoma (GBM) is the most malignant nervous system tumor with an almost 100 % recurrence rate. Thymopoietin (TMPO) has been demonstrated to be upregulated in various tumors, including lung cancer, breast cancer, and so on, but its role in GBM has not been reported. This study was aimed to determine the role of TMPO in GBM. METHODS: Publicly available Oncomine dataset analysis was used to explore the expression level of TMPO in GBM specimens. Then the expression of TMPO was knocked down in GBM cells using lentiviral system, and the knockdown efficacy was further validated by real-time quantitative PCR and western blot analysis. Furthermore, the effects of TMPO silencing on GBM cell proliferation and apoptosis were examined by MTT, colony formation, and flow cytometry analysis. Meanwhile, the expression of apoptotic markers caspase-3 and poly(ADP-ribose) polymerase (PARP) were investigated by western blot analysis. RESULTS: This study observed that the expression of TMPO in GBM specimens was remarkably higher than that in normal brain specimens. Moreover, knockdown of TMPO could significantly inhibit cell proliferation and arrest cell cycle progression at the G2/M phase. It also found that TMPO knockdown promoted cell apoptosis by upregulation of the cleavage of caspase-3 and PARP protein levels which are the markers of apoptosis. CONCLUSIONS: The results suggested TMPO might be a novel therapeutic target for GBM.
[Mh] Termos MeSH primário: Apoptose
Neoplasias Encefálicas/patologia
Pontos de Checagem do Ciclo Celular
Glioblastoma/patologia
Proteínas Nucleares/metabolismo
Timopoietinas/metabolismo
[Mh] Termos MeSH secundário: Apoptose/genética
Neoplasias Encefálicas/metabolismo
Caspase 3/metabolismo
Linhagem Celular Tumoral
Proliferação Celular
Técnicas de Silenciamento de Genes
Glioblastoma/metabolismo
Seres Humanos
Recidiva Local de Neoplasia
Proteínas Nucleares/genética
Poli(ADP-Ribose) Polimerase-1/metabolismo
Interferência de RNA
Timopoietinas/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Thymopoietins); 157298-12-9 (TMPO protein, human); EC 2.4.2.30 (PARP1 protein, human); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161021
[St] Status:MEDLINE


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[PMID]:26173563
[Au] Autor:Zhang Y; Feng J; Cui L; Zhang Y; Li W; Li C; Shi N; Chen Y; Kong W
[Ad] Endereço:National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun 130012, China; Key Laboratory for Molecular Enzymology and Engineering the Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China; State Key Laboratory of New Pha
[Ti] Título:Investigation Into Efficiency of a Novel Glycol Chitosan-Bestatin Conjugate to Protect Thymopoietin Oligopeptides From Enzymatic Degradation.
[So] Source:J Pharm Sci;105(2):828-837, 2016 Feb.
[Is] ISSN:1520-6017
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, a novel glycol chitosan (GCS)-bestatin conjugate was synthesized and evaluated to demonstrate its efficacy in protecting thymopoietin oligopeptides from aminopeptidase-mediated degradation. Moreover, the mechanism and relative susceptibility of three thymopoietin oligopeptides, thymocartin (TP4), thymopentin (TP5), and thymotrinan (TP3), to enzymatic degradation were investigated and compared at the molecular level. Initial investigations indicated that formation of the GCS-bestatin conjugate, with a substitution degree of 7.0% (moles of bestatin per mole of glycol glucosamine unit), could significantly protect all 3 peptides from aminopeptidase-mediated degradation in a concentration-dependent manner. The space hindrance and loss of one pair of hydrogen bonds, resulting from the covalent conjugation of chitosan with bestatin, did not affect the specific interaction between bestatin and aminopeptidase. Moreover, TP4 displayed a higher degradation clearance compared with those of TP5 and TP3 under the same experimental conditions. The varying levels of susceptibility of these 3 peptides to aminopeptidase (TP4 > TP5 > TP3) were closely related to differences in their binding energies to enzyme, which mainly involved Van der Waals forces and electrostatic interactions, as supported by the results of molecular dynamics simulations. These results suggest that GCS-bestatin conjugate might be useful in the delivery of thymopoietin oligopeptides by mucosal routes, and that TP3 and TP5 are better alternatives to TP4 for delivery because of their robust resistance against enzymatic degradation.
[Mh] Termos MeSH primário: Aminopeptidases/metabolismo
Quitosana/metabolismo
Leucina/análogos & derivados
Oligopeptídeos/metabolismo
Timopoietinas/metabolismo
[Mh] Termos MeSH secundário: Quitosana/química
Leucina/química
Leucina/metabolismo
Simulação de Acoplamento Molecular/métodos
Ressonância Magnética Nuclear Biomolecular/métodos
Oligopeptídeos/química
Substâncias Protetoras/química
Substâncias Protetoras/metabolismo
Espectroscopia de Infravermelho com Transformada de Fourier/métodos
Timopoietinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oligopeptides); 0 (Protective Agents); 0 (Thymopoietins); 0 (glycol-chitosan); 9012-76-4 (Chitosan); EC 3.4.11.- (Aminopeptidases); GMW67QNF9C (Leucine); I0J33N5627 (ubenimex)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170917
[Lr] Data última revisão:
170917
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150716
[St] Status:MEDLINE


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[PMID]:26002554
[Au] Autor:Narayana JL; Huang HN; Wu CJ; Chen JY
[Ad] Endereço:Doctoral Degree Program in Marine Biotechnology, Academia Sinica and National Sun Yat-sen University, Kaohsiung, Taiwan.
[Ti] Título:Efficacy of the antimicrobial peptide TP4 against Helicobacter pylori infection: in vitro membrane perturbation via micellization and in vivo suppression of host immune responses in a mouse model.
[So] Source:Oncotarget;6(15):12936-54, 2015 May 30.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Helicobacter pylori infection is marked by a strong association with various gastric diseases, including gastritis, ulcers, and gastric cancer. Antibiotic treatment regimens have low success rates due to the rapid occurrence of resistant H. pylori strains, necessitating the development of novel anti-H. pylori strategies. Here, we investigated the therapeutic potential of a novel peptide, Tilapia Piscidin 4 (TP4), against multidrug resistant gastric pathogen H. pylori, based on its in vitro and in vivo efficacy.TP4 inhibited the growth of both antibiotic-sensitive and -resistant H. pylori (CagA+, VacA+) via membrane micelle formation, which led to membrane depolarization and extravasation of cellular constituents. During colonization of gastric tissue, H. pylori infection maintains high T regulatory subsets and a low Th17/Treg ratio, and results in expression of both pro- and anti-inflammatory cytokines. Treatment with TP4 suppressed Treg subset populations and pro- and anti- inflammatory cytokines. TP4 restored the Th17/Treg balance, which resulted in early clearance of H. pylori density and recovery of gastric morphology. Toxicity studies demonstrated that TP4 treatment has no adverse effects in mice or rabbits. The results of this study indicate that TP4 may be an effective and safe monotherapeutic agent for the treatment of multidrug resistant H. pylori infections.
[Mh] Termos MeSH primário: Anti-Infecciosos/farmacologia
Infecções por Helicobacter/tratamento farmacológico
Helicobacter pylori/efeitos dos fármacos
Fragmentos de Peptídeos/farmacologia
Timopoietinas/farmacologia
[Mh] Termos MeSH secundário: Animais
Anti-Infecciosos/toxicidade
Modelos Animais de Doenças
Infecções por Helicobacter/imunologia
Infecções por Helicobacter/microbiologia
Helicobacter pylori/isolamento & purificação
Masculino
Camundongos
Camundongos Endogâmicos C3H
Testes de Sensibilidade Microbiana
Fragmentos de Peptídeos/toxicidade
Coelhos
Distribuição Aleatória
Timopoietinas/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Peptide Fragments); 0 (Thymopoietins); M0H0SK3AD5 (thymocartin)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150524
[St] Status:MEDLINE


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[PMID]:25992774
[Au] Autor:Huang HN; Chan YL; Hui CF; Wu JL; Wu CJ; Chen JY
[Ad] Endereço:Marine Research Station, Institute of Cellular and Organismic Biology, Academia Sinica, Jiaushi, Ilan, Taiwan.
[Ti] Título:Use of tilapia piscidin 3 (TP3) to protect against MRSA infection in mice with skin injuries.
[So] Source:Oncotarget;6(15):12955-69, 2015 May 30.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Antimicrobial peptides (AMPs), represent promising agents for new therapeutic approaches of infected wound treatment, on account of their antimicrobial and wound closure activities, and low potential for inducing resistance. However, therapeutic applications of these AMPs are limited by their toxicity and low stability in vivo. Previously, we reported that the 23 amino-acid designer peptide TP3 possessed antimicrobial activities. Here, we analyzed the wound closure activities of TP3 both and in vivo. TP3 at doses of up to 40 µg/ml did not affect the viability of baby hamster kidney cells. Furthermore, TP3 was found to be highly effective at combating peritonitis and wound infection caused by MRSA in mouse models, without inducing adverse behavioral effects or liver or kidney toxicity. TP3 treatment increased survival by 100% at 8 days after infection, and accelerated the progression of proliferation, remodeling, and maturation of infected wounds. Taken together, our results indicate that TP3 enhances the rate of survival of mice infected with the bacterial pathogen MRSA through both antimicrobial and immunomodulatory effects. Overall, these results suggest that TP3 may be suitable for development as a novel topical agent for treatment of infected wounds.
[Mh] Termos MeSH primário: Anti-Infecciosos/farmacologia
Staphylococcus aureus Resistente à Meticilina/efeitos dos fármacos
Fragmentos de Peptídeos/farmacologia
Infecções Estafilocócicas/prevenção & controle
Timopoietinas/farmacologia
Cicatrização/efeitos dos fármacos
Infecção dos Ferimentos/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Bacteriemia/tratamento farmacológico
Bacteriemia/imunologia
Bacteriemia/microbiologia
Bacteriemia/prevenção & controle
Cricetinae
Sinergismo Farmacológico
Feminino
Camundongos
Camundongos Endogâmicos BALB C
Pele/lesões
Pele/microbiologia
Infecções Estafilocócicas/tratamento farmacológico
Infecções Estafilocócicas/imunologia
Infecções Cutâneas Estafilocócicas/tratamento farmacológico
Infecções Cutâneas Estafilocócicas/imunologia
Infecções Cutâneas Estafilocócicas/prevenção & controle
Cicatrização/imunologia
Infecção dos Ferimentos/tratamento farmacológico
Infecção dos Ferimentos/imunologia
Infecção dos Ferimentos/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Peptide Fragments); 0 (Thymopoietins); 105803-00-7 (splenotritin)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150521
[St] Status:MEDLINE


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[PMID]:25837847
[Au] Autor:Marrero-Rodríguez D; Taniguchi-Ponciano K; Lopez-Sleman J; Romero-Morelos P; Mendoza-Rodríguez M; Garcia I; Huerta-Padilla V; Mantilla A; Duarte A; Piña P; Rodriguez-Esquivel M; Lopez-Romero R; Parrazal-Romero J; Tobias-Alonso S; Jimenez-Vega F; Alvarez-Blanco M; Salcedo M
[Ad] Endereço:Laboratorio de Oncología genómica, Unidad de Investigación Médica en Enfermedades Oncológicas, Hospital de Oncología, CMN-SXXI. IMSS, Av. Cuauhtémoc 330, Col. Doctores, México, DF, 06720, Mexico.
[Ti] Título:Thymopoietin Beta and Gamma Isoforms as a Potential Diagnostic Molecular Marker for Breast Cancer: Preliminary Data.
[So] Source:Pathol Oncol Res;21(4):1045-50, 2015 Sep.
[Is] ISSN:1532-2807
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Thymopoietin (TMPO) is an inner nuclear membrane protein, the coding gene named equally, can give arise to six isoforms by alternative splicing. This gene has been found up regulated in several types of cancer. At present work, we evaluated the TMPO isoforms generated by alternative splicing as well as the protein signal detection in breast cancer samples. TMPO expression was analyzed by immunohistochemistry in tissue microarray containing 46 breast tissue samples including normal (n = 6), benign lesions (n = 18) (fibroadenomas (n = 6), fibrocystic changes (n = 6), ductal hyperplasias (n = 6)) and breast carcinoma (n = 22). Isoforms -α, -ß and -γ of TMPO were evaluated using RT-PCR; clinical-pathological correlation analysis were done by mean of X(2). Neither the normal nor the benign lesions of the breast showed positive TMPO immunodetection, whilst 45 % of the breast carcinomas were immunopositive (p = 0.000), nine of ten positives carcinomas correspond to the Luminal A subtype. Further, alpha isoform was present in all breast samples analyzed; however, beta and gamma isoforms were only present in ten (p = 0.003) and 17 (p = 0.000), respectively, in the breast cancer samples. According with the present data, we suggest that TMPOß and -γ isoforms could provide a potential reliable diagnostic marker for breast cancer.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/genética
Neoplasias da Mama/genética
Proteínas Nucleares/genética
Timopoietinas/genética
[Mh] Termos MeSH secundário: Processamento Alternativo/genética
Neoplasias da Mama/diagnóstico
Neoplasias da Mama/patologia
Feminino
Seres Humanos
Meia-Idade
Isoformas de Proteínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Nuclear Proteins); 0 (Protein Isoforms); 0 (Thymopoietins); 157298-12-9 (TMPO protein, human)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150404
[St] Status:MEDLINE
[do] DOI:10.1007/s12253-015-9907-x


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[PMID]:25030574
[Au] Autor:Yuan J; Ando M; Higuchi I; Sakiyama Y; Matsuura E; Michizono K; Watanabe O; Nagano S; Inamori Y; Hashiguchi A; Higuchi Y; Yoshimura A; Takashima H
[Ad] Endereço:Department of Neurology and Geriatrics, Kagoshima University Graduate School of Medical and Dental Sciences, Japan.
[Ti] Título:Partial deficiency of emerin caused by a splice site mutation in EMD.
[So] Source:Intern Med;53(14):1563-8, 2014.
[Is] ISSN:1349-7235
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Emery-Dreifuss muscular dystrophy (EDMD) is caused by mutations in the EMD gene on the X chromosome, which codes for emerin, an inner nuclear membrane protein. Monoclonal antibodies against the N-terminus of emerin protein are used to screen for emerin deficiency in clinical practice. However, these tests may not accurately reflect the disease in some cases. We herein describe the identification of a splice site mutation in the EMD gene in a Japanese patient who suffered from complete atrioventricular conduction block, mild muscle weakness and joint contracture, and a persistently elevated serum creatine kinase level. We used multiple antibodies to confirm the presence of a novel truncating mutation in emerin without the transmembrane region and C-terminus in the skeletal muscle.
[Mh] Termos MeSH primário: DNA/genética
Proteínas de Membrana/deficiência
Músculo Esquelético/metabolismo
Distrofia Muscular de Emery-Dreifuss/genética
Mutação
Proteínas Nucleares/deficiência
[Mh] Termos MeSH secundário: Biópsia
Cromossomos Humanos X/genética
Análise Mutacional de DNA
Diagnóstico Diferencial
Seres Humanos
Imuno-Histoquímica
Masculino
Proteínas de Membrana/genética
Músculo Esquelético/diagnóstico por imagem
Músculo Esquelético/patologia
Distrofia Muscular de Emery-Dreifuss/diagnóstico
Distrofia Muscular de Emery-Dreifuss/metabolismo
Proteínas Nucleares/genética
Reação em Cadeia da Polimerase
Timopoietinas
Tomografia Computadorizada por Raios X
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Nuclear Proteins); 0 (Thymopoietins); 0 (emerin); 9007-49-2 (DNA)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140718
[St] Status:MEDLINE


  7 / 670 MEDLINE  
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[PMID]:24375709
[Au] Autor:Li P; Meinke P; Huong le TT; Wehnert M; Noegel AA
[Ad] Endereço:Institute for Biochemistry I, Center for Molecular Medicine Cologne (CMMC) and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Medical Faculty, University of Cologne, Cologne, Germany.
[Ti] Título:Contribution of SUN1 mutations to the pathomechanism in muscular dystrophies.
[So] Source:Hum Mutat;35(4):452-61, 2014 Apr.
[Is] ISSN:1098-1004
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in several genes encoding nuclear envelope (NE) associated proteins cause Emery-Dreifuss muscular dystrophy (EDMD). We analyzed fibroblasts from a patient who had a mutation in the EMD gene (p.L84Pfs*6) leading to loss of Emerin and a heterozygous mutation in SUN1 (p.A203V). The second patient harbored a heterozygous mutation in LAP2alpha (p.P426L) and a further mutation in SUN1 (p.A614V). p.A203V is located in the N-terminal domain of SUN1 facing the nucleoplasm and situated in the vicinity of the Nesprin-2 and Emerin binding site. p.A614V precedes the SUN domain, which interacts with the KASH domain of Nesprins in the periplasmic space and forms the center of the LINC complex. At the cellular level, we observed alterations in the amounts for several components of the NE in patient fibroblasts and further phenotypic characteristics generally attributed to laminopathies such as increased sensitivity to heat stress. The defects were more severe than observed in EDMD cells with mutations in a single gene. In particular, in patient fibroblasts carrying the p.A203V mutation in SUN1, the alterations were aggravated. Moreover, SUN1 of both patient fibroblasts exhibited reduced interaction with Lamin A/C and when expressed ectopically in wild-type fibroblasts, the SUN1 mutant proteins exhibited reduced interactions with Emerin as well.
[Mh] Termos MeSH primário: Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Distrofia Muscular de Emery-Dreifuss/genética
Distrofia Muscular de Emery-Dreifuss/patologia
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Timopoietinas/genética
[Mh] Termos MeSH secundário: Proteínas de Ligação a DNA/genética
Feminino
Fibroblastos/metabolismo
Seres Humanos
Lamina Tipo A/metabolismo
Masculino
Mutação
Membrana Nuclear/metabolismo
Timopoietinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (LMNA protein, human); 0 (Lamin Type A); 0 (Membrane Proteins); 0 (Microtubule-Associated Proteins); 0 (Nuclear Proteins); 0 (SUN1 protein, human); 0 (Thymopoietins); 0 (emerin); 0 (lamina-associated polypeptide 2); 157298-12-9 (TMPO protein, human)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:140318
[Lr] Data última revisão:
140318
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131231
[St] Status:MEDLINE
[do] DOI:10.1002/humu.22504


  8 / 670 MEDLINE  
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[PMID]:24024467
[Au] Autor:Kondratyev MS; Lunin SM; Kabanov AV; Samchenko AA; Komarov VM; Fesenko EE; Novoselova EG
[Ad] Endereço:a Institute of Cell Biophysics, Russian Academy of Sciences , Moscow region, Institutskaya street, 3, Pushchino , 142290 , Russia .
[Ti] Título:Structural and dynamic properties of thymopoietin mimetics.
[So] Source:J Biomol Struct Dyn;32(11):1793-801, 2014.
[Is] ISSN:1538-0254
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We propose a hypothesis that the T-cell receptor is a possible target of thymic hormones. We modelled the conformational dynamics of thymopentin and its structural variants in solution, as well as the interactions of these short peptides with the proposed molecular target. Thymopentin is a five-amino-acid fragment of the thymic hormone thymopoietin (residues 32 to 36) that reproduces the immunomodulatory activity of the complete hormone. Using molecular dynamics and flexible docking methods, we demonstrated high-affinity binding of thymopentin and its prospective mimetics with the T-cell receptor. The calculated biological activity spectra of thymopentin and its two promising modifications can be used in immunomodulatory activity screenings with live systems.
[Mh] Termos MeSH primário: Oligopeptídeos/química
Timopoietinas/química
[Mh] Termos MeSH secundário: Seres Humanos
Fatores Imunológicos/química
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Mimetismo Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunologic Factors); 0 (Oligopeptides); 0 (Thymopoietins)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:140805
[Lr] Data última revisão:
140805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130913
[St] Status:MEDLINE
[do] DOI:10.1080/07391102.2013.834851


  9 / 670 MEDLINE  
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[PMID]:22727332
[Au] Autor:Lunin SM; Glushkova OV; Khrenov MO; Novoselova TV; Parfenyuk SB; Fesenko EE; Novoselova EG
[Ad] Endereço:Institute of Cell Biophysics, Pushchino, Moscow region, Russia. lunin@pochta.ru
[Ti] Título:Thymic peptides restrain the inflammatory response in mice with experimental autoimmune encephalomyelitis.
[So] Source:Immunobiology;218(3):402-7, 2013 Mar.
[Is] ISSN:1878-3279
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Modulation of autoimmune inflammation by the thymic peptides thymulin and thymopentin was studied in mice with acute experimental autoimmune encephalomyelitis (EAE), which resembles multiple sclerosis in humans. EAE was induced in NZW mice by a single immunisation with myelin basic protein coupled with adjuvants. Visible signs of pathology appeared on days 12-14 after the immunisation, peaked on days 20-25, were retained up to day 45, and then reverted. A biphasic cytokine response was also detected. In the "early" phase, which started at day 35, increased levels of interferon-gamma and interleukin-6 in the blood were observed; during the "delayed" phase, which started at day 48, the levels of plasma interleukin-17 and tumour necrosis factor-alpha were also raised. In addition, the phosphorylation of NF-kappaB signalling proteins and the production of heat shock protein Hsp72 were significantly increased in splenic lymphocytes from EAE-bearing mice. When applied intraperitoneally every other day for 30 days, either thymulin or thymopentin (15 µg per 100g of body weight) significantly reduced the disease severity compared to untreated EAE mice. The effect of thymulin but not thymopentin remained after its withdrawal. Thymulin reduced the cytokine response in both the early and the delayed phases, whereas thymopentin only reduced the "early phase cytokines" (IL-6 and interferon-gamma). Both peptides significantly reduced the level of phosphorylation of the NF-kappaB signalling protein IKK and the production of Hsp72 protein. The data presented here indicate the presence of time-dependent immune responses in EAE-bearing mice, which may be associated with the Th1 and Th17 subpopulations of T-cells. Thymulin and thymopentin demonstrated different patterns of activity, most likely via mechanisms involved in NF-kappa B signalling and Hsp72 expression.
[Mh] Termos MeSH primário: Encefalomielite Autoimune Experimental/imunologia
Esclerose Múltipla/imunologia
Fator Tímico Circulante/administração & dosagem
Timopoietinas/administração & dosagem
Timo/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Citocinas/imunologia
Modelos Animais de Doenças
Proteínas de Choque Térmico HSP72/metabolismo
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos
Proteína Básica da Mielina/imunologia
NF-kappa B/metabolismo
Células Th1/imunologia
Células Th17/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytokines); 0 (HSP72 Heat-Shock Proteins); 0 (Myelin Basic Protein); 0 (NF-kappa B); 0 (Thymopoietins); 9H198D04WL (Thymic Factor, Circulating)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120626
[St] Status:MEDLINE


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[PMID]:21308741
[Au] Autor:Kuranda K; Berthon C; Leprêtre F; Polakowska R; Jouy N; Quesnel B
[Ad] Endereço:INSERM, Unité 837, Lille, France.
[Ti] Título:Expression of CD34 in hematopoietic cancer cell lines reflects tightly regulated stem/progenitor-like state.
[So] Source:J Cell Biochem;112(5):1277-85, 2011 May.
[Is] ISSN:1097-4644
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hematopoietic cancer stem cells preserve cellular hierarchy in a manner similar to normal stem cells, yet the underlying regulatory mechanisms are poorly understood. It is known that both normal and malignant stem/progenitor cells express CD34. Here, we demonstrate that several cell lines (HL-60, U266) derived from hematopoietic malignancies contain not only CD34(-) but also CD34(+) subpopulations. The CD34(+) cells displayed a stem/progenitor-like phenotype since, in contrast to CD34(-) cells, they frequently underwent cellular division and rapidly formed colonies in methylcellulose-based medium. Strikingly, a constant fraction of the CD34(+) and CD34(-) cell subpopulations, when separated, rapidly switched their phenotype. Consequently, both separated fractions could generate tumors in immunocompromised NOD/LtSz-scid/scid mice. Cultures in vitro showed that the proportion of CD34(+) stem/progenitor-like cells in the population was decreased by cell-cell contact and increased by soluble factors secreted by the cells. Using cytokine arrays, we identified some of these factors, notably thymopoietin that was able to increase the proportion of CD34(+) cells and overall colony-forming capacity in tested cell lines. This action of thymopoietin was conserved in mononuclear cells from bone marrow. Therefore, we propose that hematopoietic cancer cell lines containing subpopulations of CD34(+) cells can provide an in vitro model for studies of cancer stem/progenitor cells.
[Mh] Termos MeSH primário: Antígenos CD34/metabolismo
Células-Tronco Hematopoéticas/metabolismo
Células-Tronco Neoplásicas/metabolismo
Proteínas Nucleares/metabolismo
Timopoietinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Antígenos CD34/genética
Biomarcadores/metabolismo
Linhagem Celular Tumoral
Células Clonais
Células HL-60
Células-Tronco Hematopoéticas/efeitos dos fármacos
Seres Humanos
Camundongos
Camundongos Endogâmicos NOD
Camundongos SCID
Células-Tronco Neoplásicas/efeitos dos fármacos
Proteínas Nucleares/farmacologia
Timopentina/farmacologia
Timopoietinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD34); 0 (Biomarkers); 0 (Nuclear Proteins); 0 (Thymopoietins); 157298-12-9 (TMPO protein, human); O3Y80ZF13F (Thymopentin)
[Em] Mês de entrada:1107
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110211
[St] Status:MEDLINE
[do] DOI:10.1002/jcb.23026



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