Base de dados : MEDLINE
Pesquisa : A11.284.149.165.420.297 [Categoria DeCS]
Referências encontradas : 3317 [refinar]
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  1 / 3317 MEDLINE  
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[PMID]:29253567
[Au] Autor:Vishal SS; Tilwani S; Dalal SN
[Ad] Endereço:KS215, Advanced Centre for Treatment Research and Education in Cancer (ACTREC), Tata Memorial Centre, Kharghar Node, Navi Mumbai 410210, India; Homi Bhabha National Institute, Training School Complex, Anushakti Nagar, Mumbai 400085, India.
[Ti] Título:Plakoglobin localization to the cell border restores desmosome function in cells lacking 14-3-3γ.
[So] Source:Biochem Biophys Res Commun;495(2):1998-2003, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Desmosomes are cell-cell adhesion junctions that anchor intermediate filaments. Loss of 14-3-3γ in HCT116 cells led to defects in desmosome assembly due to a decrease in the transport of Plakoglobin (PG) to the cell border thus disrupting desmosome formation. Desmosome formation in cells lacking 14-3-3γ was restored by artificially localizing PG to the cell border by fusing it to EGFP-f (PG-EGFP-f). These results suggest that a major role of 14-3-3γ in desmosome assembly is to transport PG to the cell border leading to the initiation of desmosome formation.
[Mh] Termos MeSH primário: Proteínas 14-3-3/metabolismo
Membrana Celular/metabolismo
Neoplasias Colorretais/metabolismo
Desmossomos/metabolismo
Frações Subcelulares/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Seres Humanos
gama Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (14-3-3 Proteins); 0 (JUP protein, human); 0 (gamma Catenin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE


  2 / 3317 MEDLINE  
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[PMID]:29212005
[Au] Autor:Bartle EI; Urner TM; Raju SS; Mattheyses AL
[Ad] Endereço:Department of Cell Biology, Emory University, Atlanta, Georgia.
[Ti] Título:Desmoglein 3 Order and Dynamics in Desmosomes Determined by Fluorescence Polarization Microscopy.
[So] Source:Biophys J;113(11):2519-2529, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Desmosomes are macromolecular cell-cell junctions that provide adhesive strength in epithelial tissue. Desmosome function is inseparably linked to structure, and it is hypothesized that the arrangement, or order, of desmosomal cadherins in the intercellular space is critical for adhesive strength. However, due to desmosome size, molecular complexity, and dynamics, the role that order plays in adhesion is challenging to study. Herein, we present an excitation resolved fluorescence polarization microscopy approach to measure the spatiotemporal dynamics of order and disorder of the desmosomal cadherin desmoglein 3 (Dsg3) in living cells. Simulations were used to establish order factor as a robust metric for quantifying the spatiotemporal dynamics of order and disorder. Order factor measurements in keratinocytes showed the Dsg3 extracellular domain is ordered at the individual desmosome, single cell, and cell population levels compared to a series of disordered controls. Desmosomal adhesion is Ca dependent, and reduction of extracellular Ca leads to a loss of adhesion measured by dispase fragmentation assay (λ = 15.1 min). Live cell imaging revealed Dsg3 order decreased more rapidly (λ = 5.5 min), indicating that cadherin order is not required for adhesion. Our results suggest that rapid disordering of cadherins can communicate a change in extracellular Ca concentration to the cell, leading to a downstream loss of adhesion. Fluorescence polarization is an effective bridge between protein structure and complex dynamics and the approach presented here is broadly applicable to studying order in macromolecular structures.
[Mh] Termos MeSH primário: Desmogleína 3/metabolismo
Desmossomos/metabolismo
[Mh] Termos MeSH secundário: Sobrevivência Celular
Desmogleína 3/química
Seres Humanos
Queratinócitos/citologia
Microscopia de Fluorescência
Microscopia de Polarização
Modelos Moleculares
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Desmoglein 3)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


  3 / 3317 MEDLINE  
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[PMID]:29038103
[Au] Autor:Pilichou K; Lazzarini E; Rigato I; Celeghin R; De Bortoli M; Perazzolo Marra M; Cason M; Jongbloed J; Calore M; Rizzo S; Regazzo D; Poloni G; Iliceto S; Daliento L; Delise P; Corrado D; Van Tintelen JP; Thiene G; Rampazzo A; Basso C; Bauce B; Lorenzon A; Occhi G
[Ad] Endereço:From the Departments of Cardiac, Thoracic, and Vascular Sciences (K.P., E.L., I.R., R.C., M.P.M., M.C., S.R., S.I., L.D., D.C., G. T., C.B., B.B.) and Medicine (D.R.), University of Padua, Italy; Department of Biology, University of Padua, Italy (M.D.B., M.C., G.P., A.R., A.L., G.O.); University Med
[Ti] Título:Large Genomic Rearrangements of Desmosomal Genes in Italian Arrhythmogenic Cardiomyopathy Patients.
[So] Source:Circ Arrhythm Electrophysiol;10(10), 2017 Oct.
[Is] ISSN:1941-3084
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Arrhythmogenic cardiomyopathy (AC) is an inherited heart muscle disease associated with point mutations in genes encoding for cardiac desmosome proteins. Conventional mutation screening is positive in ≈50% of probands. Copy number variations (CNVs) have recently been linked to AC pointing to the need to determine the prevalence of CNVs in desmosomal genes and to evaluate disease penetrance by cosegregation analysis in family members. METHODS AND RESULTS: A total of 160 AC genotype-negative probands for 5 AC desmosomal genes by conventional mutation screening underwent multiplex ligation-dependent probe amplification. Nine heterozygous CNVs were identified in 11 (6.9%) of the 160 probands. Five carried a deletion of the entire plakophilin-2 ( ) gene, 2 a deletion of only exon 4, 1 a deletion of the exons 6 to 11, 1 a duplication of 5' untranslated region till exon 1, 1 the desmocollin-2 ( ) duplication of exons 7 to 9, and 1 a large deletion of chromosome 18 comprising both and genes. All probands were affected by moderate-severe forms of the disease, whereas 10 (32%) of the 31 family members carrying one of these deletions fulfilled the diagnostic criteria. CONCLUSIONS: Genomic rearrangements were detected in ≈7% of AC probands negative for pathogenic point mutations in desmosomal genes, highlighting the potential of CNVs analysis to substantially increase the diagnostic yield of genetic testing. Genotype-phenotype correlation demonstrated the presence of the disease in about one third of family members carrying the CNV, underlying the role of other factors in the development and progression of the disease.
[Mh] Termos MeSH primário: Displasia Arritmogênica Ventricular Direita/genética
Desmossomos/genética
Rearranjo Gênico
[Mh] Termos MeSH secundário: Potenciais de Ação
Adolescente
Adulto
Idoso
Displasia Arritmogênica Ventricular Direita/diagnóstico
Displasia Arritmogênica Ventricular Direita/fisiopatologia
Variações do Número de Cópias de DNA
Análise Mutacional de DNA
Desmocolinas/genética
Desmogleína 2/genética
Desmoplaquinas/genética
Eletrocardiografia
Técnicas Eletrofisiológicas Cardíacas
Feminino
Deleção de Genes
Dosagem de Genes
Duplicação Gênica
Estudos de Associação Genética
Marcadores Genéticos
Predisposição Genética para Doença
Frequência Cardíaca
Hereditariedade
Seres Humanos
Itália
Masculino
Meia-Idade
Reação em Cadeia da Polimerase Multiplex
Linhagem
Fenótipo
Placofilinas/genética
Mutação Puntual
Fatores de Risco
Adulto Jovem
gama Catenina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DSC2 protein, human); 0 (DSG2 protein, human); 0 (DSP protein, human); 0 (Desmocollins); 0 (Desmoglein 2); 0 (Desmoplakins); 0 (Genetic Markers); 0 (JUP protein, human); 0 (PKP2 protein, human); 0 (Plakophilins); 0 (gamma Catenin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE


  4 / 3317 MEDLINE  
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[PMID]:28764973
[Au] Autor:Kessler EL; Nikkels PG; van Veen TA
[Ad] Endereço:Department of Medical Physiology, University Medical Center Utrecht, 3584CM Utrecht, The Netherlands.
[Ti] Título:Disturbed Desmoglein-2 in the intercalated disc of pediatric patients with dilated cardiomyopathy.
[So] Source:Hum Pathol;67:101-108, 2017 Sep.
[Is] ISSN:1532-8392
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dilated cardiomyopathy (DCM) leads to disturbed contraction and force transduction, and is associated with substantial mortality in all age groups. Involvement of a disrupted composition of the intercalated disc (ID) has been reported. However, in children, little is established about such subcellular changes during disease, because of the pathological mix-up with the ongoing cardiac maturation. This leaves maladaptive remodeling often undetected. We aimed at illustrating subcellular alterations in children diagnosed with DCM compared to age-matched controls, focusing on ID proteins known to be crucially stable under healthy conditions and destabilized during cardiac injury in adults. Left ventricular or septal pediatric specimens were collected from 7 individuals diagnosed with DCM (age: 23 weeks in utero to 8 weeks postnatal) and age-matched controls that died of non-cardiovascular cause. We determined the amount of fibrosis and localization of ID proteins by immunohistochemistry. In pediatric DCM, most ID proteins follow similar spatiotemporal changes in localization as in controls. However, although no mutations were found, the signal of the desmosomal protein Desmoglein-2 was reduced in all pediatric DCM specimens, but not in controls or adult DCM patients. Endocardial and transmural fibrosis was increased in all pediatric DCM patients compared to age-matched controls. Composition of the ID in pediatric DCM patients is similar to controls, except for the localization of Desmoglein-2 and presence of severe fibrosis. This suggests that the architecture of desmosomes is already disturbed in the early stages of DCM. These findings contribute to the understanding of pediatric DCM.
[Mh] Termos MeSH primário: Cardiomiopatia Dilatada/metabolismo
Desmogleína 2/análise
Desmossomos/química
Miócitos Cardíacos/química
[Mh] Termos MeSH secundário: Fatores Etários
Autopsia
Biópsia
Cardiomiopatia Dilatada/diagnóstico
Cardiomiopatia Dilatada/genética
Cardiomiopatia Dilatada/mortalidade
Estudos de Casos e Controles
Desmossomos/patologia
Regulação para Baixo
Feminino
Fibrose
Imunofluorescência
Predisposição Genética para Doença
Seres Humanos
Lactente
Recém-Nascido
Masculino
Mutação
Miócitos Cardíacos/patologia
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DSG2 protein, human); 0 (Desmoglein 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE


  5 / 3317 MEDLINE  
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[PMID]:28684609
[Au] Autor:De Pascalis C; Etienne-Manneville S
[Ad] Endereço:Cell Polarity, Migration and Cancer Unit, Institut Pasteur Paris, CNRS UMR3691, 75724 Paris Cedex 15, France.
[Ti] Título:Single and collective cell migration: the mechanics of adhesions.
[So] Source:Mol Biol Cell;28(14):1833-1846, 2017 Jul 07.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chemical and physical properties of the environment control cell proliferation, differentiation, or apoptosis in the long term. However, to be able to move and migrate through a complex three-dimensional environment, cells must quickly adapt in the short term to the physical properties of their surroundings. Interactions with the extracellular matrix (ECM) occur through focal adhesions or hemidesmosomes via the engagement of integrins with fibrillar ECM proteins. Cells also interact with their neighbors, and this involves various types of intercellular adhesive structures such as tight junctions, cadherin-based adherens junctions, and desmosomes. Mechanobiology studies have shown that cell-ECM and cell-cell adhesions participate in mechanosensing to transduce mechanical cues into biochemical signals and conversely are responsible for the transmission of intracellular forces to the extracellular environment. As they migrate, cells use these adhesive structures to probe their surroundings, adapt their mechanical properties, and exert the appropriate forces required for their movements. The focus of this review is to give an overview of recent developments showing the bidirectional relationship between the physical properties of the environment and the cell mechanical responses during single and collective cell migration.
[Mh] Termos MeSH primário: Adesão Celular/fisiologia
Movimento Celular/fisiologia
Mecanotransdução Celular/fisiologia
[Mh] Termos MeSH secundário: Junções Aderentes/metabolismo
Animais
Fenômenos Biomecânicos/fisiologia
Caderinas/metabolismo
Desmossomos/metabolismo
Matriz Extracelular/fisiologia
Adesões Focais/metabolismo
Seres Humanos
Integrinas/metabolismo
Junções Íntimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (Integrins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E17-03-0134


  6 / 3317 MEDLINE  
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[PMID]:28339476
[Au] Autor:Brodehl A; Belke DD; Garnett L; Martens K; Abdelfatah N; Rodriguez M; Diao C; Chen YX; Gordon PM; Nygren A; Gerull B
[Ad] Endereço:Department of Cardiac Sciences and Libin Cardiovascular Institute of Alberta, University of Calgary, Calgary, Alberta, Canada.
[Ti] Título:Transgenic mice overexpressing desmocollin-2 (DSC2) develop cardiomyopathy associated with myocardial inflammation and fibrotic remodeling.
[So] Source:PLoS One;12(3):e0174019, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Arrhythmogenic cardiomyopathy is an inherited heart muscle disorder leading to ventricular arrhythmias and heart failure, mainly as a result of mutations in cardiac desmosomal genes. Desmosomes are cell-cell junctions mediating adhesion of cardiomyocytes; however, the molecular and cellular mechanisms underlying the disease remain widely unknown. Desmocollin-2 is a desmosomal cadherin serving as an anchor molecule required to reconstitute homeostatic intercellular adhesion with desmoglein-2. Cardiac specific lack of desmoglein-2 leads to severe cardiomyopathy, whereas overexpression does not. In contrast, the corresponding data for desmocollin-2 are incomplete, in particular from the view of protein overexpression. Therefore, we developed a mouse model overexpressing desmocollin-2 to determine its potential contribution to cardiomyopathy and intercellular adhesion pathology. METHODS AND RESULTS: We generated transgenic mice overexpressing DSC2 in cardiac myocytes. Transgenic mice developed a severe cardiac dysfunction over 5 to 13 weeks as indicated by 2D-echocardiography measurements. Corresponding histology and immunohistochemistry demonstrated fibrosis, necrosis and calcification which were mainly localized in patches near the epi- and endocardium of both ventricles. Expressions of endogenous desmosomal proteins were markedly reduced in fibrotic areas but appear to be unchanged in non-fibrotic areas. Furthermore, gene expression data indicate an early up-regulation of inflammatory and fibrotic remodeling pathways between 2 to 3.5 weeks of age. CONCLUSION: Cardiac specific overexpression of desmocollin-2 induces necrosis, acute inflammation and patchy cardiac fibrotic remodeling leading to fulminant biventricular cardiomyopathy.
[Mh] Termos MeSH primário: Cardiomiopatias/genética
Glicoproteínas de Membrana/genética
Miocardite/genética
Miocárdio/patologia
Miócitos Cardíacos/patologia
[Mh] Termos MeSH secundário: Animais
Cardiomiopatias/metabolismo
Cardiomiopatias/patologia
Desmossomos/metabolismo
Fibrose/genética
Fibrose/metabolismo
Fibrose/patologia
Glicoproteínas de Membrana/metabolismo
Camundongos
Camundongos Transgênicos
Miocardite/metabolismo
Miocardite/patologia
Miocárdio/metabolismo
Miócitos Cardíacos/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dsc2 protein, mouse); 0 (Membrane Glycoproteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174019


  7 / 3317 MEDLINE  
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[PMID]:28323918
[Au] Autor:Kiseljak-Vassiliades K; Mills TS; Zhang Y; Xu M; Lillehei KO; Kleinschmidt-DeMasters BK; Wierman ME
[Ad] Endereço:Division of Endocrinology, Metabolism, and Diabetes, Department of Medicine, University of Colorado, Aurora, Colorado 80045.
[Ti] Título:Elucidating the Role of the Desmosome Protein p53 Apoptosis Effector Related to PMP-22 in Growth Hormone Tumors.
[So] Source:Endocrinology;158(5):1450-1460, 2017 May 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Densely granulated and sparsely granulated (SG) growth hormone (GH) pituitary adenomas differ in biological behavior, which may be correlated with their known differences in cytoplasmic keratin distribution and E-cadherin expression. We wanted to explore candidate genes that might further explain this behavior. Exon expression microarray was performed on 21 GH tumors (10 SG and 11 densely granulated) and 20 normal control pituitaries from autopsy. Bioinformatic analyses confirmed a differential molecular signature between normal pituitary and GH tumors as well as between the GH tumor subtypes. There was a consistent downregulation of transcripts involved in the structure and function of the desmosome, including desmoplakin (eightfold), desmoglein 2 (sixfold), plakophilin 2 (sevenfold), and p53 apoptosis effector related to PMP-22 (PERP; sixfold) in SG tumors compared with normal pituitary. PERP is lost in more aggressive SG human GH pituitary tumors. PERP re-expression in GH3 rat GH tumor cells resulted in decreased colony formation compared with vector transfectants, confirming the role of PERP as a tumor suppressor with no effects on proliferation. Increased PERP expression was associated with loss of a survival advantage in a hypoxic environment, as assessed by terminal deoxynucleotidyltransferase-mediated dUTP nick end labeling (P < 0.05) and cleaved caspase-3 (P < 0.05). Downregulation of desmosomal formation transcripts including PERP may contribute to the aggressive phenotype seen in SG GH pituitary tumors and their behavior in response to surgery and medical therapy.
[Mh] Termos MeSH primário: Adenoma/genética
Desmossomos/metabolismo
Genes Supressores de Tumor/fisiologia
Adenoma Hipofisário Secretor de Hormônio do Crescimento/genética
Proteínas de Membrana/fisiologia
Hipófise/metabolismo
[Mh] Termos MeSH secundário: Adenoma/patologia
Biomarcadores Tumorais/genética
Perfilação da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Adenoma Hipofisário Secretor de Hormônio do Crescimento/patologia
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Análise em Microsséries
Transcriptoma
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Membrane Proteins); 0 (PERP protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171028
[Lr] Data última revisão:
171028
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1210/en.2016-1841


  8 / 3317 MEDLINE  
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[PMID]:28124277
[Au] Autor:Lara-Diaz VJ; Castilla-Cortazar I; Martín-Estal I; García-Magariño M; Aguirre GA; Puche JE; de la Garza RG; Morales LA; Muñoz U
[Ad] Endereço:Escuela de Medicina, Tecnologico de Monterrey, Avenida Morones Prieto No. 3000 Pte. Col. Los Doctores, 64710, Monterrey, Nuevo León, Mexico.
[Ti] Título:IGF-1 modulates gene expression of proteins involved in inflammation, cytoskeleton, and liver architecture.
[So] Source:J Physiol Biochem;73(2):245-258, 2017 May.
[Is] ISSN:1877-8755
[Cp] País de publicação:Spain
[La] Idioma:eng
[Ab] Resumo:Even though the liver synthesizes most of circulating IGF-1, it lacks its receptor under physiological conditions. However, according to previous studies, a damaged liver expresses the receptor. For this reason, herein, we examine hepatic histology and expression of genes encoding proteins of the cytoskeleton, extracellular matrix, and cell-cell molecules and inflammation-related proteins. A partial IGF-1 deficiency murine model was used to investigate IGF-1's effects on liver by comparing wild-type controls, heterozygous igf1 , and heterozygous mice treated with IGF-1 for 10 days. Histology, microarray for mRNA gene expression, RT-qPCR, and lipid peroxidation were assessed. Microarray analyses revealed significant underexpression of igf1 in heterozygous mice compared to control mice, restoring normal liver expression after treatment, which then normalized its circulating levels. IGF-1 receptor mRNA was overexpressed in Hz mice liver, while treated mice displayed a similar expression to that of the controls. Heterozygous mice showed overexpression of several genes encoding proteins related to inflammatory and acute-phase proteins and underexpression or overexpression of genes which coded for extracellular matrix, cytoskeleton, and cell junction components. Histology revealed an altered hepatic architecture. In addition, liver oxidative damage was found increased in the heterozygous group. The mere IGF-1 partial deficiency is associated with relevant alterations of the hepatic architecture and expression of genes involved in cytoskeleton, hepatocyte polarity, cell junctions, and extracellular matrix proteins. Moreover, it induces hepatic expression of the IGF-1 receptor and elevated acute-phase and inflammation mediators, which all resulted in liver oxidative damage.
[Mh] Termos MeSH primário: Proteínas da Fase Aguda/metabolismo
Regulação da Expressão Gênica
Hepatite/metabolismo
Mediadores da Inflamação/metabolismo
Fator de Crescimento Insulin-Like I/metabolismo
Fígado/metabolismo
Receptores de Somatomedina/metabolismo
[Mh] Termos MeSH secundário: Proteínas da Fase Aguda/genética
Animais
Caderinas/genética
Caderinas/metabolismo
Cruzamentos Genéticos
Proteínas do Citoesqueleto/genética
Proteínas do Citoesqueleto/metabolismo
Desmossomos/imunologia
Desmossomos/metabolismo
Desmossomos/patologia
Proteínas da Matriz Extracelular/genética
Proteínas da Matriz Extracelular/metabolismo
Perfilação da Expressão Gênica
Hepatite/imunologia
Hepatite/patologia
Hepatite/prevenção & controle
Injeções Subcutâneas
Fator de Crescimento Insulin-Like I/administração & dosagem
Fator de Crescimento Insulin-Like I/genética
Fator de Crescimento Insulin-Like I/uso terapêutico
Peroxidação de Lipídeos
Fígado/imunologia
Fígado/patologia
Masculino
Camundongos
Camundongos Transgênicos
Estresse Oxidativo
Receptores de Somatomedina/genética
Proteínas de Junções Íntimas/genética
Proteínas de Junções Íntimas/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acute-Phase Proteins); 0 (Cadherins); 0 (Cytoskeletal Proteins); 0 (Extracellular Matrix Proteins); 0 (Inflammation Mediators); 0 (Receptors, Somatomedin); 0 (Tight Junction Proteins); 0 (insulin-like growth factor-1, mouse); 67763-96-6 (Insulin-Like Growth Factor I)
[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:170127
[St] Status:MEDLINE
[do] DOI:10.1007/s13105-016-0545-x


  9 / 3317 MEDLINE  
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[PMID]:28069669
[Au] Autor:Vermij SH; Abriel H; van Veen TA
[Ad] Endereço:Department of Medical Physiology, Division of Heart & Lungs, University Medical Center Utrecht, Utrecht, the Netherlands.
[Ti] Título:Refining the molecular organization of the cardiac intercalated disc.
[So] Source:Cardiovasc Res;113(3):259-275, 2017 Mar 01.
[Is] ISSN:1755-3245
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This review presents an extensively integrated model of the cardiac intercalated disc (ID), a highly orchestrated structure that connects adjacent cardiomyocytes. Classically, three main structures are distinguished: gap junctions (GJs) metabolically and electrically connect cytoplasm of adjacent cardiomyocytes; adherens junctions (AJs) connect the actin cytoskeleton of adjacent cells; and desmosomes function as cell anchors and connect intermediate filaments. Furthermore, ion channels reside in the ID. Mutations in ID proteins have been associated with cardiac arrhythmias such as Brugada syndrome and arrhythmogenic cardiomyopathy. However, rather than being independent, all ID components work together intensively by multifunctional proteins such as ZO-1, Ankyrin G, and ß-catenin, integrating mechanical and electrical functions. GJs form a plaque surrounded by the perinexus in which free connexons reside; the connexome integrates NaV channels, the desmosome and GJs; and the area composita hosts AJs and desmosomes, also integrated as adhering junctions. Furthermore, the transitional junction connects sarcomeres to the plasma membrane. Lastly, this review integrates all these findings in comprehensible figures, illustrating the interdependencies of ID proteins.
[Mh] Termos MeSH primário: Arritmias Cardíacas/metabolismo
Comunicação Celular
Junções Intercelulares/metabolismo
Proteínas de Membrana/metabolismo
Miócitos Cardíacos/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Junções Aderentes/metabolismo
Junções Aderentes/patologia
Animais
Arritmias Cardíacas/genética
Arritmias Cardíacas/patologia
Arritmias Cardíacas/fisiopatologia
Desmossomos/metabolismo
Desmossomos/patologia
Junções Comunicantes/metabolismo
Junções Comunicantes/patologia
Predisposição Genética para Doença
Seres Humanos
Junções Intercelulares/genética
Junções Intercelulares/patologia
Canais Iônicos/metabolismo
Mecanotransdução Celular
Proteínas de Membrana/genética
Mutação
Miócitos Cardíacos/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ion Channels); 0 (Membrane Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170111
[St] Status:MEDLINE
[do] DOI:10.1093/cvr/cvw259


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[PMID]:28024684
[Au] Autor:Yoshida K; Ishii K; Shimizu A; Yokouchi M; Amagai M; Shiraishi K; Shirakata Y; Stanley JR; Ishiko A
[Ad] Endereço:Dermatology, Toho University School of Medicine, Tokyo, Japan.
[Ti] Título:Non-pathogenic pemphigus foliaceus (PF) IgG acts synergistically with a directly pathogenic PF IgG to increase blistering by p38MAPK-dependent desmoglein 1 clustering.
[So] Source:J Dermatol Sci;85(3):197-207, 2017 Mar.
[Is] ISSN:1873-569X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pemphigus foliaceus (PF) is an autoimmune blistering disease caused by autoantibodies (Abs) against desmoglein 1 (Dsg1). PF sera contain polyclonal Abs which are heterogeneous mixture of both pathogenic and non-pathogenic Abs, as shown by isolation of monoclonal Abs (mAbs). OBJECTIVE: To investigate how pathogenic and non-pathogenic anti-Dsg1 Abs contribute to blister formation in PF. METHODS: Using organ-cultured human skin, we compared the effect of a single pathogenic anti-Dsg1 IgG mAb, a single non-pathogenic anti-Dsg1 IgG mAb, and their mixture on blister formation as analyzed by histology, subcellular localization of IgG deposits and desmosomal proteins by confocal microscopy, and desmosomal structure by electron microscopy. In addition, we measured keratinocyte adhesion by an in vitro dissociation assay. RESULTS: 24h after injection, a single pathogenic anti-Dsg1 IgG caused a subcorneal blister with IgG and Dsg1 localized linearly on the cell surface of keratinocytes. A single non-pathogenic anti-Dsg1 IgG bound linearly on the keratinocytes but did not induce blisters. A pathogenic and a non-pathogenic IgG mAb injected together caused an aberrant granular pattern of IgG and Dsg1 in the lower epidermis with blister formation in the superficial epidermis. Electron microscopy demonstrated that the mixture of mAbs shortened desmosomal lengths more than a single mAb in the basal and spinous layers. Furthermore, although Dsg1 clustering required both cross-linking of Dsg1 molecules by the non-pathogenic IgG plus a pathogenic antibody, the latter could be in the form of a monovalent single chain variable fragment, suggesting that loss of trans-interaction of Dsg1 is required for clustering. Finally, a p38MAPK inhibitor blocked Dsg1 clustering. When pathogenic strength was measured by the dissociation assay, a mixture of pathogenic and non-pathogenic IgG mAbs disrupted keratinocyte adhesion more than a single pathogenic mAb. This pathogenic effect was only partially suppressed by the p38MAPK inhibitor. CONCLUSION: These findings indicate that a polyclonal mixture of anti-Dsg1 IgG antibodies enhances pathogenic activity for blister formation associated with p38MAPK-dependent Dsg1 clustering and that not only pathogenic antibodies but also non-pathogenic antibodies coordinately contribute to blister formation in PF.
[Mh] Termos MeSH primário: Autoanticorpos/imunologia
Desmogleína 1/imunologia
Imunoglobulina G/imunologia
Queratinócitos/fisiologia
Pênfigo/imunologia
Anticorpos de Cadeia Única/imunologia
Pele/imunologia
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Mh] Termos MeSH secundário: Adesão Celular
Desmogleína 1/metabolismo
Desmossomos/ultraestrutura
Imunofluorescência
Seres Humanos
Imidazóis/farmacologia
Queratinócitos/imunologia
Microscopia Eletrônica
Técnicas de Cultura de Órgãos
Pênfigo/sangue
Cultura Primária de Células
Piridinas/farmacologia
Proteínas Quinases p38 Ativadas por Mitógeno/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (DSG1 protein, human); 0 (Desmoglein 1); 0 (Imidazoles); 0 (Immunoglobulin G); 0 (Pyridines); 0 (Single-Chain Antibodies); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); PVX798P8GI (4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170716
[Lr] Data última revisão:
170716
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE



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