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  1 / 7524 MEDLINE  
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[PMID]:29367526
[Au] Autor:Ishitsuka Y
[Ad] Endereço:Department of Dermatology, Faculty of Medicine, University of Tsukuba.
[Ti] Título:[The formation of skin barrier and defective barrier-associated skin diseases].
[So] Source:Nihon Rinsho Meneki Gakkai Kaishi;40(6):416-427, 2017.
[Is] ISSN:1349-7413
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:  Since the discovery of loss-of-function mutations in filaggrin (FLG) gene in atopic dermatitis (AD) individuals, significant attention has been paid against the skin barrier as an initial starting point of atopic march. Although FLG is a significant cornification-associated gene, skin barrier formation is a complex process mediated by an array of genes with specific functions. In this article, the mechanism of physical skin barrier formation is reviewed in detail, focusing on specific gene functions and inherited disorders caused by genetic aberrations. Additionally, the mechanism of percutaneous sensitization with environmental allergens in association with FLG-deficiency is reviewed in order to clarify the link between defective skin barrier and atopic march. Finally, updated knowledge of psoriasis pathophysiology in connection with genetic defect in skin barrier is reviewed. This article would provide a novel opportunity to understand the allergic/autoimmune disorders from the viewpoint of non-classical immune cells.
[Mh] Termos MeSH primário: Dermatopatias/genética
Dermatopatias/imunologia
Pele/imunologia
[Mh] Termos MeSH secundário: Dermatite Atópica/genética
Dermatite Atópica/imunologia
Seres Humanos
Proteínas de Filamentos Intermediários/genética
Mutação com Perda de Função
Psoríase/genética
Psoríase/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Intermediate Filament Proteins); 0 (filaggrin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE
[do] DOI:10.2177/jsci.40.416


  2 / 7524 MEDLINE  
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[PMID]:29339073
[Au] Autor:Roginski RS; Lau CW; Santoiemma PP; Weaver SJ; Du P; Soteropoulos P; Yang J
[Ad] Endereço:Department of Anesthesiology, CMC VA Medical Center, Philadelphia, PA 19104, United States; Department of Anesthesiology and Critical Care, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States. Electronic address: raymond.roginski@va.gov.
[Ti] Título:The human GCOM1 complex gene interacts with the NMDA receptor and internexin-alpha.
[So] Source:Gene;648:42-53, 2018 Mar 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The known functions of the human GCOM1 complex hub gene include transcription elongation and the intercalated disk of cardiac myocytes. However, in all likelihood, the gene's most interesting, and thus far least understood, roles will be found in the central nervous system. To investigate the functions of the GCOM1 gene in the CNS, we have cloned human and rat brain cDNAs encoding novel, 105 kDa GCOM1 combined (Gcom) proteins, designated Gcom15, and identified a new group of GCOM1 interacting genes, termed Gints, from yeast two-hybrid (Y2H) screens. We showed that Gcom15 interacts with the NR1 subunit of the NMDA receptor by co-expression in heterologous cells, in which we observed bi-directional co-immunoprecipitation of human Gcom15 and murine NR1. Our Y2H screens revealed 27 novel GCOM1 interacting genes, many of which are synaptic proteins and/or play roles in neurologic diseases. Finally, we showed, using rat brain protein preparations, that the Gint internexin-alpha (INA), a known interactor of the NMDAR, co-IPs with GCOM1 proteins, suggesting a GCOM1-GRIN1-INA interaction and a novel pathway that may be relevant to neuroprotection.
[Mh] Termos MeSH primário: Proteínas de Filamentos Intermediários/metabolismo
RNA Polimerase II/metabolismo
Receptores de N-Metil-D-Aspartato/metabolismo
[Mh] Termos MeSH secundário: Adulto
Animais
Encéfalo/metabolismo
Células HEK293
Seres Humanos
Imunoprecipitação
Proteínas de Filamentos Intermediários/genética
Masculino
Camundongos
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Ligação Proteica
Mapas de Interação de Proteínas
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
RNA Polimerase II/genética
Ratos Wistar
Receptores de N-Metil-D-Aspartato/genética
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GRIN1 protein, human); 0 (Intermediate Filament Proteins); 0 (NR1 NMDA receptor); 0 (Nerve Tissue Proteins); 0 (POLR2M protein, human); 0 (Protein Subunits); 0 (Receptors, N-Methyl-D-Aspartate); 0 (alpha-internexin); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  3 / 7524 MEDLINE  
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[PMID]:29353040
[Au] Autor:Jung Y; Kim JC; Park NJ; Bong SK; Lee S; Jegal H; Jin LT; Kim SM; Kim YK; Kim SN
[Ad] Endereço:Natural Products Research Institute, Korea Institute of Science and Technology, Gangneung, Gangwon-do 25451, Republic of Korea.
[Ti] Título:Eupatilin, an activator of PPARα, inhibits the development of oxazolone-induced atopic dermatitis symptoms in Balb/c mice.
[So] Source:Biochem Biophys Res Commun;496(2):508-514, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eupatilin (5,7-dihydroxy-3',4',6-trimethoxyflavone) is the main lipophilic flavonoid obtained from the Artemisia species. Eupatilin has been reported to have anti-apoptotic, anti-oxidative and anti-inflammatory activities. Previously, we found that eupatilin increases transcriptional activity and expression of peroxisome proliferator-activated receptor α (PPARα) in a keratinocyte cell line and acts as an agonist of PPARα. PPARα agonists ameliorate atopic dermatitis (AD) and restore the skin barrier function. In this study, we confirmed that the effects of eupatilin improved AD-like symptoms in an oxazolone-induced AD-like mouse model. Furthermore, we found that eupatilin suppressed the levels of serum immunoglobulin E (IgE), interleukin-4 (IL-4), and AD involved cytokines, such as tumor necrosis factor α (TNFα), interferon-γ (IFN-γ), IL-1ß, and thymic stromal lymphopoietin (TSLP), IL-33, IL-25 and increased the levels of filaggrin and loricrin in the oxazolone-induced AD-like mouse model. Taken together, our data suggest that eupatilin is a potential candidate for the treatment of AD.
[Mh] Termos MeSH primário: Dermatite Atópica/tratamento farmacológico
Fármacos Dermatológicos/farmacologia
Medicamentos de Ervas Chinesas/farmacologia
Flavonoides/farmacologia
PPAR alfa/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Citocinas/genética
Citocinas/imunologia
Dermatite Atópica/induzido quimicamente
Dermatite Atópica/imunologia
Dermatite Atópica/patologia
Relação Dose-Resposta a Droga
Feminino
Regulação da Expressão Gênica
Imunoglobulina E/sangue
Imunoglobulina E/genética
Interferon gama/genética
Interferon gama/imunologia
Interleucina-1beta/genética
Interleucina-1beta/imunologia
Interleucina-33/genética
Interleucina-33/imunologia
Interleucina-4/genética
Interleucina-4/imunologia
Interleucinas/genética
Interleucinas/imunologia
Proteínas de Filamentos Intermediários/genética
Proteínas de Filamentos Intermediários/imunologia
Proteínas de Membrana/genética
Proteínas de Membrana/imunologia
Camundongos
Camundongos Endogâmicos BALB C
Oxazolona
PPAR alfa/imunologia
Ratos
Transdução de Sinais
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytokines); 0 (D17Wsu104e protein, mouse); 0 (Dermatologic Agents); 0 (Drugs, Chinese Herbal); 0 (Flavonoids); 0 (IL1B protein, mouse); 0 (Il33 protein, mouse); 0 (Interleukin-1beta); 0 (Interleukin-33); 0 (Interleukins); 0 (Intermediate Filament Proteins); 0 (Membrane Proteins); 0 (PPAR alpha); 0 (Tumor Necrosis Factor-alpha); 0 (filaggrin); 0 (loricrin); 0 (thymic stromal lymphopoietin); 15646-46-5 (Oxazolone); 207137-56-2 (Interleukin-4); 37341-29-0 (Immunoglobulin E); 4D58O05490 (eupatilin); 82115-62-6 (Interferon-gamma)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180122
[St] Status:MEDLINE


  4 / 7524 MEDLINE  
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[PMID]:28455573
[Au] Autor:Yang Y; Liu W; Zhao Z; Zhang Y; Xiao H; Luo B
[Ad] Endereço:Department of Medical Microbiology, Qingdao University Medical College, 38 Dengzhou Road, Qingdao, 266021, China.
[Ti] Título:Filaggrin gene polymorphism associated with Epstein-Barr virus-associated tumors in China.
[So] Source:Virus Genes;53(4):532-537, 2017 Aug.
[Is] ISSN:1572-994X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations of filaggrin gene (FLG) have been identified as the cause of ichthyosis vulgaris, while recently FLG mutations were found to be associated with gastric cancer. This study aimed to investigate the association of filaggrin polymorphism with Epstein-Barr virus-associated tumors in China. A total of 200 patients with three types of tumors and 117 normal control samples were genotyped at three common FLG mutation loci (rs3126085, K4671X, R501X) by using Sequenom MassARRAY technique. The χ test was used to evaluate the relationship between the mutation and the three kinds of tumors. A two-sided P value of <0.05 was considered statistically significant. The results showed that two single-nucleotide polymorphism (SNP) loci (rs3126085, K4671X) were significantly associated with nasopharyngeal carcinoma in genetic model. In addition, the two SNPs K4671X and rs3126085 were related to Epstein-Barr virus (EBV)-associated gastric carcinoma (EBVaGC) and EBV-negative gastric carcinoma (EBVnGC), respectively. Furthermore, allele distributions in EBVaGC and EBVnGC were verified to be different in both SNP loci.
[Mh] Termos MeSH primário: Infecções por Vírus Epstein-Barr/genética
Herpesvirus Humano 4/fisiologia
Proteínas de Filamentos Intermediários/genética
Polimorfismo de Nucleotídeo Único
Neoplasias Gástricas/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
China
Infecções por Vírus Epstein-Barr/metabolismo
Infecções por Vírus Epstein-Barr/virologia
Feminino
Genótipo
Herpesvirus Humano 4/genética
Seres Humanos
Proteínas de Filamentos Intermediários/metabolismo
Masculino
Meia-Idade
Mutação
Neoplasias Gástricas/metabolismo
Neoplasias Gástricas/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intermediate Filament Proteins); 0 (filaggrin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180126
[Lr] Data última revisão:
180126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s11262-017-1463-x


  5 / 7524 MEDLINE  
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[PMID]:28456621
[Au] Autor:Johansson EK; Bergström A; Kull I; Lind T; Söderhäll C; van Hage M; Wickman M; Ballardini N; Wahlgren CF
[Ad] Endereço:Dermatology and Venereology Unit, Department of Medicine Solna, Karolinska Institutet, Stockholm, Sweden; Dermatological and Venereal Clinic, Södersjukhuset, Stockholm, Sweden. Electronic address: emma.k.johansson@sll.se.
[Ti] Título:IgE sensitization in relation to preschool eczema and filaggrin mutation.
[So] Source:J Allergy Clin Immunol;140(6):1572-1579.e5, 2017 Dec.
[Is] ISSN:1097-6825
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Eczema (atopic dermatitis) is associated with an increased risk of having IgE antibodies. IgE sensitization can occur through an impaired skin barrier. Filaggrin gene (FLG) mutation is associated with eczema and possibly also with IgE sensitization. OBJECTIVE: We sought to explore the longitudinal relation between preschool eczema (PSE), FLG mutation, or both and IgE sensitization in childhood. METHODS: A total of 3201 children from the BAMSE (Children Allergy Milieu Stockholm Epidemiology) birth cohort recruited from the general population were included. Regular parental questionnaires identified children with eczema. Blood samples were collected at 4, 8, and 16 years of age for analysis of specific IgE. FLG mutation analysis was performed on 1890 of the children. RESULTS: PSE was associated with IgE sensitization to both food allergens and aeroallergens up to age 16 years (overall adjusted odds ratio, 2.30; 95% CI, 2.00-2.66). This association was even stronger among children with persistent PSE. FLG mutation was associated with IgE sensitization to peanut at age 4 years (adjusted odds ratio, 1.88; 95% CI, 1.03-3.44) but not to other allergens up to age 16 years. FLG mutation and PSE were not effect modifiers for the association between IgE sensitization and PSE or FLG mutation, respectively. Sensitized children with PSE were characterized by means of polysensitization, but no other specific IgE sensitization patterns were found. CONCLUSIONS: PSE is associated with IgE sensitization to both food allergens and aeroallergens up to 16 years of age. FLG mutation is associated with IgE sensitization to peanut but not to other allergens. Sensitized children with preceding PSE are more often polysensitized.
[Mh] Termos MeSH primário: Eczema/imunologia
Hipersensibilidade Alimentar/imunologia
Proteínas de Filamentos Intermediários/genética
Mutação/genética
Pele/imunologia
[Mh] Termos MeSH secundário: Adolescente
Alérgenos/imunologia
Arachis/imunologia
Criança
Pré-Escolar
Estudos de Coortes
Análise Mutacional de DNA
Eczema/epidemiologia
Eczema/genética
Feminino
Hipersensibilidade Alimentar/epidemiologia
Hipersensibilidade Alimentar/genética
Estudos de Associação Genética
Genótipo
Seres Humanos
Imunização
Imunoglobulina E/metabolismo
Masculino
Pele/patologia
Suécia/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Intermediate Filament Proteins); 0 (filaggrin); 37341-29-0 (Immunoglobulin E)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


  6 / 7524 MEDLINE  
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[PMID]:29196765
[Au] Autor:Kumari S; Gao J; Mathias RT; Sun X; Eswaramoorthy A; Browne N; Zhang N; Varadaraj K
[Ad] Endereço:Department of Physiology and Biophysics, Stony Brook University, Stony Brook, New York, United States.
[Ti] Título:Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.
[So] Source:Invest Ophthalmol Vis Sci;58(14):6006-6019, 2017 Dec 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: The objective of this study was to understand the molecular and physiologic mechanisms behind the lens cataract differences in Aquaporin 0-knockout-Heterozygous (AQP0-Htz) mice developed in C57 and FVB (lacks beaded filaments [BFs]) strains. Methods: Lens transparency was studied using dark field light microscopy. Water permeability (Pf) was measured in fiber cell membrane vesicles. Western blotting/immunostaining was performed to verify expression of BF proteins and connexins. Microelectrode-based intact lens intracellular impedance was measured to determine gap junction (GJ) coupling resistance. Lens intracellular hydrostatic pressure (HP) was determined using a microelectrode/manometer system. Results: Lens opacity and spherical aberration were more distinct in AQP0-Htz lenses from FVB than C57 strains. In either background, compared to wild type (WT), AQP0-Htz lenses showed decreased Pf (approximately 50%), which was restored by transgenic expression of AQP1 (TgAQP1/AQP0-Htz), but the opacities and differences between FVB and C57 persisted. Western blotting revealed no change in connexin expression levels. However, in C57 AQP0-Htz and TgAQP1/AQP0-Htz lenses, GJ coupling resistance decreased approximately 2.8-fold and the HP gradient decreased approximately 1.9-fold. Increased Pf in TgAQP1/AQP0-Htz did not alter GJ coupling resistance or HP. Conclusions: In C57 AQP0-Htz lenses, GJ coupling resistance decreased. HP reduction was smaller than the coupling resistance reduction, a reflection of an increase in fluid circulation, which is one reason for the less severe cataract in C57 than FVB. Overall, our results suggest that AQP0 modulates GJs in the presence of BF proteins to maintain lens transparency and homeostasis.
[Mh] Termos MeSH primário: Aquaporina 1/genética
Catarata/genética
Proteínas do Olho/genética
Regulação da Expressão Gênica
Proteínas de Filamentos Intermediários/genética
Cristalino/metabolismo
RNA/genética
[Mh] Termos MeSH secundário: Animais
Aquaporina 1/biossíntese
Western Blotting
Catarata/metabolismo
Catarata/patologia
Modelos Animais de Doenças
Impedância Elétrica
Proteínas do Olho/biossíntese
Junções Comunicantes/genética
Junções Comunicantes/metabolismo
Genótipo
Heterozigoto
Proteínas de Filamentos Intermediários/biossíntese
Cristalino/patologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microeletrodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp1 protein, mouse); 0 (Eye Proteins); 0 (Intermediate Filament Proteins); 0 (filensin); 146410-94-8 (Aquaporin 1); 63231-63-0 (RNA)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22153


  7 / 7524 MEDLINE  
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[PMID]:29183042
[Au] Autor:Garreis F; Jahn J; Wild K; Abrar DB; Schicht M; Schröder JM; Paulsen F
[Ad] Endereço:Department of Anatomy II, Friedrich Alexander University Erlangen-Nürnberg (FAU), Erlangen, Germany.
[Ti] Título:Expression and Regulation of S100 Fused-Type Protein Hornerin at the Ocular Surface and Lacrimal Apparatus.
[So] Source:Invest Ophthalmol Vis Sci;58(13):5968-5977, 2017 Nov 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: The S100 fused-type proteins hornerin (HRNR) and filaggrin-2 (FLG2) are members of the epidermal differentiation complex, which is involved in terminal differentiation of keratinocytes via cornification as well as maintenance of the epidermal antimicrobial barrier. We investigated the expression and possible regulation of HRNR and FLG2 at the ocular surface and in the lacrimal apparatus. Methods: Tissues of the lacrimal apparatus and ocular surface were analyzed systematically by means of RT-PCR, immunohistochemistry, and immuntransmission electron microscopy (iTEM) for their ability to express and produce HRNR and FLG2. In addition, inducibility and regulation of HRNR were studied in cultivated human corneal (HCE), conjunctival (HCjE), as well as meibomian gland (HMGEC) epithelial cell line by real-time RT-PCR. Results: RT-PCR, immunohistochemistry, and iTEM revealed constitutive expression of HRNR in the epithelium of cornea, conjunctiva, nasolacrimal ducts, and acinus cells of lacrimal and meibomian glands. HRNR also was detected in tears of healthy volunteers. No expression of FLG2 could be detected in tissue samples of the ocular surface and lacrimal apparatus. Real-time RT-PCR revealed a decreased HRNR gene expression after challenge with proinflammatory cytokines and supernatants of Escherichia coli and Pseudomonas aeroginosa in HCE cells, whereas HCjE cells revealed no changes. In HMGECs serum-induced differentiation and application of all-trans retinoic acid significantly increased HRNR gene expression. Conclusions: The data suggest that HRNR, but not FLG2, is a component of the ocular surface and lacrimal apparatus, including meibomian glands. HRNR seems to contribute to the maintenance of the epithelial barrier at the ocular surface and, thus, also may be involved in ocular surface diseases.
[Mh] Termos MeSH primário: Túnica Conjuntiva/metabolismo
Córnea/metabolismo
Aparelho Lacrimal/metabolismo
Glândulas Tarsais/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Cadáver
Proteínas de Ligação ao Cálcio
Feminino
Regulação da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Proteínas de Filamentos Intermediários
Masculino
Microscopia Eletrônica
Meia-Idade
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Proteínas S100/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (HRNR protein, human); 0 (Intermediate Filament Proteins); 0 (S100 Proteins); 0 (filaggrin-2 protein, human)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171201
[Lr] Data última revisão:
171201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22637


  8 / 7524 MEDLINE  
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[PMID]:28935373
[Au] Autor:Chaves JM; Gupta R; Srivastava K; Srivastava O
[Ad] Endereço:Department of Optometry and Vision Science, University of Alabama at Birmingham, Birmingham, AL 35294, United States.
[Ti] Título:Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin.
[So] Source:Biochem Biophys Res Commun;494(1-2):402-408, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aim of this study was to determine relative importance of N-terminal domain and C-terminal extension of αA-crystallin during their in vitro complex formation with phakinin and filensin (the two lens-specific intermediate filament [IF] proteins). Cloned phakinin, filensin and vimentin were purified under a denaturing conditions by consecutive DEAE-cellulose-, hydroxyapatite- and Sephadex G-75-column chromatographic methods. WTαA-crystallin, αA-NT (N-terminal domain [residue number 1-63])-deleted and αA-CT (C-terminal terminal extension [residue number 140-173]-deleted), were cloned in pET 100 TOPO vector, expressed in BL-21 (DE3) cells using 1% IPTG, and purified using a Ni -affinity column. The following two in vitro methods were used to determine complex formation of WT-αA, αA-NT, or αA-CT with phakinin, filensin or both phakinin plus filensin together: an ultracentrifugation sedimentation (centrifugation at 80,000 × g for 30 min at 20 °C) followed by SDS-PAGE analysis, and an electron microscopic analysis. In the first method, the individual control proteins (WT-αA, αA-NT and αA-CT crystallin species) remained in the supernatant fractions whereas phakinin, filensin, and vimentin were recovered in the pellet fractions. On complex formation by individual WT-αA-, αA-NT or αA-CT-species with filensin, phakinin or both phakinin and filensin, WT-αA and αA-CT were recovered in the pellet fraction with phakinin, filensin or both filensin and phakinin, whereas αA-NT remained mostly in the supernatant, suggesting its poor complex formation property. EM-studies showed filamentous structure formation between WT-αA and αA-CT with phakinin or filensin, or with both filensin and phakinin together but relatively poor filamentous structures with αA-NT. Together, the results suggest that the N-terminal domain of αA-crystallin is required during in vitro complex formation with filensin and phakinin.
[Mh] Termos MeSH primário: Proteínas do Olho/metabolismo
Vetores Genéticos/química
Proteínas de Filamentos Intermediários/metabolismo
Cadeia A de alfa-Cristalina/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas do Olho/genética
Proteínas do Olho/ultraestrutura
Expressão Gênica
Vetores Genéticos/metabolismo
Seres Humanos
Proteínas de Filamentos Intermediários/genética
Proteínas de Filamentos Intermediários/ultraestrutura
Filamentos Intermediários/metabolismo
Filamentos Intermediários/ultraestrutura
Cristalino/metabolismo
Cristalino/ultraestrutura
Microscopia Eletrônica
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/ultraestrutura
Cadeia A de alfa-Cristalina/genética
Cadeia A de alfa-Cristalina/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eye Proteins); 0 (Intermediate Filament Proteins); 0 (Recombinant Proteins); 0 (alpha-Crystallin A Chain); 0 (filensin); 0 (phakinin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE


  9 / 7524 MEDLINE  
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[PMID]:28890293
[Au] Autor:Donetti E; Cornaghi L; Arnaboldi F; Ricceri F; Pescitelli L; Maiocchi M; Carriero F; Baruffaldi Preis F; Prignano F
[Ad] Endereço:Department of Biomedical Sciences for Health, Università degli Studi di Milano, Via Mangiagalli, 31, 20133 Milan, Italy. Electronic address: elena.donetti@unimi.it.
[Ti] Título:Epidermal barrier reaction to an in vitro psoriatic microenvironment.
[So] Source:Exp Cell Res;360(2):180-188, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Keratinocytes (KCs) and Langerhans cells (LCs) contribute to create the epidermal barrier. To form a functional epidermis, KCs express filaggrin and Toll-like Receptors (TLRs). LCs are the first line of epidermal defence and can be activated by interleukin (IL)-17 and Tumor Necrosis Factor (TNF)-alpha. In psoriasis, an alteration of TLR expression, a defective expression of filaggrin, and LC activation occur. In organotypic cultures of human skin we investigated the interplay between IL-17 and TNF-alpha on i) expression of filaggrin, TLR2, 7 and 9, and Nuclear Factor (NF)-kB localization by immunofluorescence and ii) LC ultrastructural features by transmission electron microscopy. Normal human skin was obtained after aesthetic surgery (n=7), overnight incubated in a Transwell system, and exposed to TNF-alpha and/or IL-17 for 24 (T24), 48 (T48), and 72 (T72) hours. Cytokines always influenced the expression of filaggrin. TNF-alpha alone activated LCs only starting from T48. TLR2 and TLR7 expressions were affected at T24 by IL-17 and the combination of cytokines, but not by TNF-alpha. TLR9-positive cells were detectable in the granular layer after cytokine exposure. A nuclear localization of NF-kB was always observed after cytokine incubation. In conclusion, each cytokine possess an intrinsic activity on the different components of the epidermal barrier.
[Mh] Termos MeSH primário: Técnicas de Cultura de Células/métodos
Microambiente Celular/fisiologia
Epiderme/fisiologia
Queratinócitos/fisiologia
Psoríase/patologia
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Células Cultivadas
Epiderme/ultraestrutura
Feminino
Regulação da Expressão Gênica
Seres Humanos
Proteínas de Filamentos Intermediários/genética
Proteínas de Filamentos Intermediários/metabolismo
Queratinócitos/ultraestrutura
Psoríase/genética
Receptores Toll-Like/genética
Receptores Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intermediate Filament Proteins); 0 (Toll-Like Receptors); 0 (filaggrin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE


  10 / 7524 MEDLINE  
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[PMID]:28710038
[Au] Autor:Zhang Q; Si N; Liu Y; Zhang D; Wang R; Zhang Y; Wang S; Liu X; Deng X; Ma Y; Ge P; Zhao J; Zhang X
[Ad] Endereço:Department of Neurosurgery, Beijing Tiantan Hospital, Capital Medical University, China 6 Tiantanxili, DongCheng District, Beijing 100050, China; China National Clinical Research Center for Neurological Diseases, Beijing, China; Center of Stroke, Beijing Institute for Brain Disorders, Beijing, China
[Ti] Título:Steroid sulfatase and filaggrin mutations in a boy with severe ichthyosis, elevated serum IgE level and moyamoya syndrome.
[So] Source:Gene;628:103-108, 2017 Sep 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:X-linked ichthyosis (XLI) is a relatively common, recessive condition caused by mutations in the steroid sulfatase (STS) gene. Common loss-of-function mutations in the filaggrin gene (FLG) cause ichthyosis vulgaris and predispose individuals to atopic eczema. We report a case of a 6-year-old boy who presented with unusually severe XLI, an increased serum immunoglobulin E level (2120IU/ml) and moyamoya angiopathy. Whole-exome sequencing identified a gross deletion encompassing the STS in Xp22.31 and the p.K4022X FLG mutation. The deletion is at least 1.6Mb in size in the proband, based on real-time quantitative polymerase chain reaction results. No other genetic mutations related to ichthyosis, moyamoya or hyper-immunoglobulin E syndrome were detected. Furthermore, his mother's brothers suffered from mild XLI and only had a deletion encompassing the STS. Additionally, his father and older sister suffered from mild ichthyosis vulgaris and had the p.K4022X FLG mutation. We report the first case of XLI with concurrent moyamoya syndrome. Moreover, an IgE-mediated immune response may have triggered the moyamoya signaling cascade in this patient with ichthyosis. Furthermore, our study strengthens the hypothesis that filaggrin defects can synergize with an STS deficiency to exacerbate the ichthyosis phenotype in an ethnically diverse population.
[Mh] Termos MeSH primário: Ictiose Ligada ao Cromossomo X/genética
Imunoglobulina E/sangue
Proteínas de Filamentos Intermediários/genética
Doença de Moyamoya/genética
Esteril-Sulfatase/genética
[Mh] Termos MeSH secundário: Criança
Saúde da Família
Feminino
Seres Humanos
Ictiose Ligada ao Cromossomo X/complicações
Ictiose Ligada ao Cromossomo X/imunologia
Masculino
Doença de Moyamoya/complicações
Doença de Moyamoya/imunologia
Mutação
Linhagem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intermediate Filament Proteins); 0 (filaggrin); 37341-29-0 (Immunoglobulin E); EC 3.1.6.2 (Steryl-Sulfatase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE



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