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[PMID]:29050564
[Au] Autor:Thorolfsdottir RB; Sveinbjornsson G; Sulem P; Helgadottir A; Gretarsdottir S; Benonisdottir S; Magnusdottir A; Davidsson OB; Rajamani S; Roden DM; Darbar D; Pedersen TR; Sabatine MS; Jonsdottir I; Arnar DO; Thorsteinsdottir U; Gudbjartsson DF; Holm H; Stefansson K
[Ad] Endereço:deCODE genetics/Amgen, Inc., Reykjavik, Iceland. Electronic address: rosath@decode.is.
[Ti] Título:A Missense Variant in PLEC Increases Risk of Atrial Fibrillation.
[So] Source:J Am Coll Cardiol;70(17):2157-2168, 2017 Oct 24.
[Is] ISSN:1558-3597
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Genome-wide association studies (GWAS) have yielded variants at >30 loci that associate with atrial fibrillation (AF), including rare coding mutations in the sarcomere genes MYH6 and MYL4. OBJECTIVES: The aim of this study was to search for novel AF associations and in doing so gain insights into the mechanisms whereby variants affect AF risk, using electrocardiogram (ECG) measurements. METHODS: The authors performed a GWAS of 14,255 AF cases and 374,939 controls, using whole-genome sequence data from the Icelandic population, and tested novel signals in 2,002 non-Icelandic cases and 12,324 controls. They then tested the AF variants for effect on cardiac electrical function by using measurements in 289,297 ECGs from 62,974 individuals. RESULTS: The authors discovered 2 novel AF variants, the intergenic variant rs72700114, between the genes LINC01142 and METTL11B (risk allele frequency = 8.1%; odds ratio [OR]: 1.26; p = 3.1 × 10 ), and the missense variant p.Gly4098Ser in PLEC (frequency = 1.2%; OR: 1.55; p = 8.0 × 10 ), encoding plectin, a cytoskeletal cross-linking protein that contributes to integrity of cardiac tissue. The authors also confirmed 29 reported variants. p.Gly4098Ser in PLEC significantly affects various ECG measurements in the absence of AF. Other AF variants have diverse effects on the conduction system, ranging from none to extensive. CONCLUSIONS: The discovery of a missense variant in PLEC affecting AF combined with recent discoveries of variants in the sarcomere genes MYH6 and MYL4 points to an important role of myocardial structure in the pathogenesis of the disease. The diverse associations between AF variants and ECG measurements suggest fundamentally different categories of mechanisms contributing to the development of AF.
[Mh] Termos MeSH primário: Fibrilação Atrial/genética
Variação Estrutural do Genoma
[Mh] Termos MeSH secundário: Fibrilação Atrial/fisiopatologia
Eletrocardiografia
Estudo de Associação Genômica Ampla
Seres Humanos
Mutação de Sentido Incorreto/genética
Cadeias Leves de Miosina/genética
Plectina/genética
Risco
Sarcômeros
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myosin Light Chains); 0 (Plectin); 0 (myosin light chain 4, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE


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[PMID]:28867478
[Au] Autor:Chaudhari PR; Charles SE; D'Souza ZC; Vaidya MM
[Ad] Endereço:Advanced Centre for Treatment, Research and Education in Cancer (ACTREC), Tata Memorial Centre (TMC), Kharghar, Navi Mumbai 410210, India; Homi Bhabha National Institute, Training School Complex, Anushakti Nagar, Mumbai 400085, India.
[Ti] Título:Hemidesmosomal linker proteins regulate cell motility, invasion and tumorigenicity in oral squamous cell carcinoma derived cells.
[So] Source:Exp Cell Res;360(2):125-137, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BPAG1e and Plectin are hemidesmosomal linker proteins which anchor intermediate filament proteins to the cell surface through ß4 integrin. Recent reports indicate that these proteins play a role in various cellular processes apart from their known anchoring function. However, the available literature is inconsistent. Further, the previous study from our laboratory suggested that Keratin8/18 pair promotes cell motility and tumor progression by deregulating ß4 integrin signaling in oral squamous cell carcinoma (OSCC) derived cells. Based on these findings, we hypothesized that linker proteins may have a role in neoplastic progression of OSCC. Downregulation of hemidesmosomal linker proteins in OSCC derived cells resulted in reduced cell migration accompanied by alterations in actin organization. Further, decreased MMP9 activity led to reduced cell invasion in linker proteins knockdown cells. Moreover, loss of these proteins resulted in reduced tumorigenic potential. SWATH analysis demonstrated upregulation of N-Myc downstream regulated gene 1 (NDRG1) in linker proteins downregulated cells as compared to vector control cells. Further, the defects in phenotype upon linker proteins ablation were rescued upon loss of NDRG1 in linker proteins knockdown background. These data together indicate that hemidesmosomal linker proteins regulate cell motility, invasion and tumorigenicity possibly through NDRG1 in OSCC derived cells.
[Mh] Termos MeSH primário: Carcinogênese/genética
Carcinoma de Células Escamosas/patologia
Movimento Celular/genética
Proteínas do Citoesqueleto/fisiologia
Hemidesmossomos/fisiologia
Neoplasias Bucais/patologia
[Mh] Termos MeSH secundário: Animais
Carcinogênese/patologia
Carcinoma de Células Escamosas/genética
Linhagem Celular Tumoral
Proteínas do Citoesqueleto/genética
Distonina/fisiologia
Células HEK293
Hemidesmossomos/genética
Hemidesmossomos/metabolismo
Seres Humanos
Camundongos
Camundongos Endogâmicos NOD
Camundongos SCID
Neoplasias Bucais/genética
Invasividade Neoplásica
Plectina/genética
Plectina/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (DST protein, human); 0 (Dystonin); 0 (PLEC protein, human); 0 (Plectin)
[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:170905
[St] Status:MEDLINE


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[PMID]:28576497
[Au] Autor:Matsubara T; Kinbara M; Maeda T; Yoshizawa M; Kokabu S; Takano Yamamoto T
[Ad] Endereço:Dentofacial Orthopedics, Graduate School of Dentistry, Tohoku University, Sendai, Japan; Division of Molecular Signaling and Biochemistry, Department of Health Improvement, Kyushu Dental University, Fukuoka, Japan. Electronic address: r15matsubara@fa.kyu-dent.ac.jp.
[Ti] Título:Regulation of osteoclast differentiation and actin ring formation by the cytolinker protein plectin.
[So] Source:Biochem Biophys Res Commun;489(4):472-476, 2017 Aug 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Osteoclasts are cells that resorb the bone matrix and maintain bone and calcium homeostasis. An actin ring is a characteristic actin structure that is essential for bone resorption by osteoclasts. Tyrosine kinase Src deficient osteoclasts do not form actin rings; thus, Src is a key molecule for actin ring formation in osteoclasts. However, how Src regulates actin ring formation is not fully understood. We identified the cytolinker protein plectin as a Src-binding protein by immunoprecipitation and liquid chromatography tandem mass spectrometry. Plectin is a huge protein (>500 kDa) and regulates the cytoskeleton by binding to actin and tubulin. We assessed the expression and role of plectin in osteoclasts. Plectin was expressed and co-localized with Src close to the actin ring in osteoclasts. Moreover, plectin was tyrosine-phosphorylated by Src. Differentiation and actin ring formation were inhibited by downregulation of plectin. These results suggest an important role for plectin in osteoclast differentiation and actin ring formation through Src binding.
[Mh] Termos MeSH primário: Actinas/biossíntese
Osteoclastos/metabolismo
Plectina/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Camundongos
Osteoclastos/citologia
Células RAW 264.7
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Plectin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170604
[St] Status:MEDLINE


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[PMID]:27878870
[Au] Autor:Mauldin EA; Wang P; Olivry T; Henthorn PS; Casal ML
[Ad] Endereço:Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, 3900 Delancey Street, Philadelphia, PA, 19104, USA.
[Ti] Título:Epidermolysis bullosa simplex in sibling Eurasier dogs is caused by a PLEC non-sense variant.
[So] Source:Vet Dermatol;28(1):10-e3, 2017 Feb.
[Is] ISSN:1365-3164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Plectin, a large linker protein found in many tissues, acts to connect components of the cytoskeleton to each other. In the epidermis, plectin binds keratin intermediate filaments to hemidesmosomes. A deficiency of plectin in the skin leads to blister formation in the basal layer and the disease epidermolysis bullosa simplex (EBS). HYPOTHESIS/OBJECTIVES: To describe a novel blistering disease that arose spontaneously in a litter of puppies. ANIMALS: Two female and one male 20-day-old Eurasier puppies, from a litter of six, were presented for evaluation of failure to thrive and then euthanized due to poor prognosis. The puppies had ulcers on the lips, tongue, nasal planum, paw pads and abdomen. RESULTS: Immunolabelling on frozen skin for basement membrane proteins revealed patchy and weak to absent staining for plectin as compared with strong linear staining in normal dogs. Ultrastructurally, hemidesmosomes were irregularly shaped and had loss of distinction between inner and outer plaques. Pedigree analysis supported an autosomal recessive mode of inheritance. A premature stop codon was discovered in exon 27 of PLEC that resulted in the production of a severely truncated protein. CONCLUSION: The study describes the first documented spontaneous EBS associated with a PLEC variant in domestic animals.
[Mh] Termos MeSH primário: Códon sem Sentido/genética
Doenças do Cão/genética
Epidermólise Bolhosa Simples/veterinária
Plectina/genética
[Mh] Termos MeSH secundário: Animais
Códon sem Sentido/fisiologia
Doenças do Cão/patologia
Cães/genética
Epidermólise Bolhosa Simples/genética
Epidermólise Bolhosa Simples/patologia
Feminino
Masculino
Linhagem
Plectina/fisiologia
Irmãos
Pele/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); 0 (Plectin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161124
[St] Status:MEDLINE
[do] DOI:10.1111/vde.12394


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[PMID]:27833093
[Au] Autor:von der Heide EK; Neumann M; Vosberg S; James AR; Schroeder MP; Ortiz-Tanchez J; Isaakidis K; Schlee C; Luther M; Jöhrens K; Anagnostopoulos I; Mochmann LH; Nowak D; Hofmann WK; Greif PA; Baldus CD
[Ad] Endereço:Department of Hematology and Oncology, Charité, University Hospital Berlin, Berlin, Germany.
[Ti] Título:Molecular alterations in bone marrow mesenchymal stromal cells derived from acute myeloid leukemia patients.
[So] Source:Leukemia;31(5):1069-1078, 2017 May.
[Is] ISSN:1476-5551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The contribution of molecular alterations in bone marrow mesenchymal stromal cells (BM-MSC) to the pathogenesis of acute myeloid leukemia (AML) is poorly understood. Thus we assessed genome-wide genetic, transcriptional and epigenetic alterations in BM-MSC derived from AML patients (AML BM-MSC). Whole-exome sequencing (WES) of AML BM-MSC samples from 21 patients revealed a non-specific pattern of genetic alterations in the stromal compartment. The only mutation present in AML BM-MSC at serial time points of diagnosis, complete remission and relapse was a mutation in the PLEC gene encoding for cytoskeleton key player Plectin in one AML patient. Healthy donor controls did not carry genetic alterations as determined by WES. Transcriptional profiling using RNA sequencing revealed deregulation of proteoglycans and adhesion molecules as well as cytokines in AML BM-MSC. Moreover, KEGG pathway enrichment analysis unravelled deregulated metabolic pathways and endocytosis in both transcriptional and DNA methylation signatures in AML BM-MSC. Taken together, we report molecular alterations in AML BM-MSC suggesting global changes in the AML BM microenvironment. Extended investigations of these altered niche components may contribute to the design of niche-directed therapies in AML.
[Mh] Termos MeSH primário: Medula Óssea/patologia
Exoma/genética
Leucemia Mieloide Aguda/genética
Células Mesenquimais Estromais/patologia
[Mh] Termos MeSH secundário: Idoso
Estudos de Casos e Controles
Metilação de DNA
Perfilação da Expressão Gênica
Seres Humanos
Leucemia Mieloide Aguda/patologia
Meia-Idade
Plectina/genética
Análise de Sequência de DNA
Análise de Sequência de RNA
Fatores de Tempo
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PLEC protein, human); 0 (Plectin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161112
[St] Status:MEDLINE
[do] DOI:10.1038/leu.2016.324


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[PMID]:27813154
[Au] Autor:Walker GD; Woody M; Orrin E; Mellerio JE; Levy ML
[Ad] Endereço:Department of Dermatology, Baylor Scott and White, Temple, Texas.
[Ti] Título:Epidermolysis Bullosa with Pyloric Atresia and Significant Urologic Involvement.
[So] Source:Pediatr Dermatol;34(1):e61-e64, 2017 Jan.
[Is] ISSN:1525-1470
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epidermolysis bullosa (EB) is a rare inherited disease that causes epidermal fragility, blistering, and erosions. EB results from a variety of mutations in proteins of the skin and mucous membranes of the body. Mutations in plectin a protein involved in hemidesmosome integrity and function, are associated with subtypes of EB, including EB with pyloric atresia and EB with muscular dystrophy. We present two cases of EB with significant urologic involvement resulting from mutations in plectin.
[Mh] Termos MeSH primário: Displasia Ectodérmica/genética
Plectina/genética
Pele/patologia
Doenças Urológicas/genética
[Mh] Termos MeSH secundário: Displasia Ectodérmica/diagnóstico
Feminino
Seres Humanos
Recém-Nascido
Masculino
Mutação
Doenças Urológicas/diagnóstico
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS
[Nm] Nome de substância:
0 (PLEC protein, human); 0 (Plectin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170427
[Lr] Data última revisão:
170427
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE
[do] DOI:10.1111/pde.13026


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[PMID]:27404216
[Au] Autor:Castro-Muñozledo F; Meza-Aguilar DG; Domínguez-Castillo R; Hernández-Zequinely V; Sánchez-Guzmán E
[Ad] Endereço:Department of Cell Biology, Centro de Investigación y de Estudios Avanzados del IPN, México City, Mexico.
[Ti] Título:Vimentin as a Marker of Early Differentiating, Highly Motile Corneal Epithelial Cells.
[So] Source:J Cell Physiol;232(4):818-830, 2017 Apr.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vimentin (Vim), a cytoskeletal intermediate filament, is part of a naturally occurring reversible program, the Epithelial-Mesenchymal Transition (EMT), which converts epithelial cells into mesenchymal-like derivatives. Based on previous results showing that epithelial cells co-express Vim and keratin (Krt) as part of a cytoskeletal network which confers them a highly motile phenotype, we explored the role of Vim in rabbit corneal epithelial cells or RCE1(5T5) cells, an established model of corneal epithelial differentiation. Vim and keratin filaments were co-expressed in cells localized at the proliferative/migratory rim of the growing colonies, but not in basal cells from the center of the colonies nor at suprabasal cell layers. Flow cytometry and qPCR demonstrated that there was a decrease in Krt /Vim cell number and ΔNp63α expression when cells reached confluence and formed a 4-5 layered epithelium, while there was a concomitant increase of both Pax-6 expression and Krt /Vim cells. Inhibition of cell proliferation with mitomycin C did not modify cell motility nor the expression of Vim. We studied the distribution and expression of α6 integrin, a protein also involved in cell migration. The results demonstrated that α6 integrin had a distribution which was, in part, co-linear with Vim at the proliferative/migratory rim of cell colonies, suggesting an indirect interaction between these proteins. Immunoprecipitation and immunostaining assays indicated that plectin might be mediating such interaction. These data suggest that Vim expression in corneal epithelium is found in a cell population composed of highly motile cells with a Vim /Krt /ΔNp63α /Pax-6 /α6 integrin phenotype. J. Cell. Physiol. 232: 818-830, 2017. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Diferenciação Celular
Movimento Celular
Células Epiteliais/citologia
Epitélio Anterior/citologia
Vimentina/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores/metabolismo
Diferenciação Celular/efeitos dos fármacos
Linhagem Celular
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Citoesqueleto/efeitos dos fármacos
Citoesqueleto/metabolismo
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Integrina alfa6/metabolismo
Queratinas/metabolismo
Mitomicina/farmacologia
Plectina/metabolismo
Pseudópodes/efeitos dos fármacos
Pseudópodes/metabolismo
Coelhos
Proteínas Supressoras de Tumor/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Integrin alpha6); 0 (Plectin); 0 (Tumor Suppressor Proteins); 0 (Vimentin); 50SG953SK6 (Mitomycin); 68238-35-7 (Keratins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160713
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25487


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[PMID]:27769077
[Au] Autor:Fric P; Skrha J; Sedo A; Zima T; Busek P; Kmochová K; Laclav M; Bunganic B; Solar S; Hrabal P; Belina F; Záruba P; Skrha P; Zavoral M
[Ad] Endereço:Departments of aMedicine/GastroenterologybPathologycSurgery, Military University HospitaldLaboratory of Endocrinology and MetabolismeInstitute of Biochemistry and Experimental OncologyfInstitute of Clinical Biochemistry and Laboratory Diagnostics, General University Hospital, 1st and 2nd Faculty of MedicinegDepartment of Medicine, 3rd Faculty of Medicine, Charles University, Prague, Czech Republic.
[Ti] Título:Early detection of pancreatic cancer: impact of high-resolution imaging methods and biomarkers.
[So] Source:Eur J Gastroenterol Hepatol;28(12):e33-e43, 2016 Dec.
[Is] ISSN:1473-5687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:High-resolution imaging methods (HRIMs) and biomarkers present the second step of pancreatic cancer (PC) diagnostics in at-risk individuals. These include patients with positive risk factors, early symptoms, nonresponders to the initial antidiabetic therapy, patients older than 50 years of age with new-onset unstable diabetes requiring insulin as well as patients with long-term insulin-non-dependent diabetes and recent (up to 6 months) failure of antidiabetic therapy. The procedures should be started without delay and the co-operation between the primary and tertiary medical centers is highly desirable. An early indication of HRIMs and biomarkers is a prerequisite for the diagnosis of a resectable PC. This publication reviews the recent contribution of HRIMs and biomarkers toward an early diagnosis of PC.
[Mh] Termos MeSH primário: Adenoma/diagnóstico por imagem
Carcinoma in Situ/diagnóstico por imagem
Carcinoma Ductal Pancreático/diagnóstico por imagem
Detecção Precoce de Câncer/métodos
MicroRNAs/genética
Neoplasias Císticas, Mucinosas e Serosas/diagnóstico por imagem
Neoplasias Pancreáticas/diagnóstico por imagem
[Mh] Termos MeSH secundário: Adenoma/genética
Adenoma/metabolismo
Anticorpos/metabolismo
Biomarcadores
Carcinoma in Situ/genética
Carcinoma in Situ/metabolismo
Carcinoma Ductal Pancreático/genética
Carcinoma Ductal Pancreático/metabolismo
Colangiopancreatografia Retrógrada Endoscópica
Colangiopancreatografia por Ressonância Magnética
Técnicas de Imagem por Elasticidade
Endossonografia
Seres Humanos
Imagem por Ressonância Magnética
Tomografia Computadorizada Multidetectores
Neoplasias Císticas, Mucinosas e Serosas/genética
Neoplasias Císticas, Mucinosas e Serosas/metabolismo
Neoplasias Pancreáticas/genética
Neoplasias Pancreáticas/metabolismo
Plectina/metabolismo
Tomografia Computadorizada com Tomografia por Emissão de Pósitrons
Ultrassonografia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antibodies); 0 (Biomarkers); 0 (DAS-1 protein, human); 0 (MicroRNAs); 0 (PLEC protein, human); 0 (Plectin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161022
[St] Status:MEDLINE


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[PMID]:27566071
[Au] Autor:Cheng CC; Lai YC; Lai YS; Chao WT; Tseng YH; Hsu YH; Chen YY; Liu YH
[Ad] Endereço:Department of Pathology, Chang Bing Show Chwan Memorial Hospital, Lukang, Taiwan, R.O.C. Center for General Education, Providence University, Taichung City, Taiwan, R.O.C.
[Ti] Título:Cell Pleomorphism and Cytoskeleton Disorganization in Human Liver Cancer.
[So] Source:In Vivo;30(5):549-55, 2016 09-10.
[Is] ISSN:1791-7549
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Nucleoskeleton maintains the framework of a cell nucleus that is required for a variety of nuclear functions. However, the nature of nucleoskeleton structure has not been yet clearly elucidated due to microscopy visualization limitations. Plectin, a nuclear pore-permeable component of cytoskeleton, exhibits a role of cross-linking between cytoplasmic intermediate filaments and nuclear lamins. Presumably, plectin is also a part of nucleoskeleton. Previously, we demonstrated that pleomorphism of hepatoma cells is the consequence of cytoskeletal changes mediated by plectin deficiency. In this study, we applied a variety of technologies to detect the cytoskeletons in liver cells. MATERIALS AND METHODS AND RESULTS: The images of confocal microscopy did not show the existence of plectin, intermediate filaments, microfilaments and microtubules in hepatic nuclei. However, in the isolated nuclear preparation, immunohistochemical staining revealed positive results for plectin and cytoskeletal proteins that may contribute to the contamination derived from cytoplasmic residues. Therefore, confocal microscopy provides a simple and effective technology to observe the framework of nucleoskeleton. Accordingly, we verified that cytoskeletons are not found in hepatic cell nuclei. Furthermore, the siRNA-mediated knockdown of plectin in liver cells leads to collapsed cytoskeleton, cell transformation and pleomorphic nuclei. CONCLUSION: Plectin and cytoskeletons were not detected in the nuclei of liver cells compared to the results of confocal microscopy. Despite the absence of nuclear plectin and cytoskeletal filaments, the evidence provided support that nuclear pleomorphism of cancer cells is correlated with the cytoplasmic disorganization of cytoskeleton.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/genética
Citoesqueleto/genética
Neoplasias Hepáticas/genética
Plectina/genética
[Mh] Termos MeSH secundário: Carcinoma Hepatocelular/diagnóstico por imagem
Carcinoma Hepatocelular/patologia
Linhagem Celular Tumoral
Núcleo Celular/genética
Núcleo Celular/patologia
Transformação Celular Neoplásica/genética
Transformação Celular Neoplásica/patologia
Citoesqueleto/patologia
Hepatócitos/metabolismo
Hepatócitos/patologia
Seres Humanos
Neoplasias Hepáticas/diagnóstico por imagem
Neoplasias Hepáticas/patologia
Microscopia Confocal
Microtúbulos/genética
Microtúbulos/patologia
Plectina/química
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plectin); 0 (RNA, Small Interfering)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160828
[St] Status:MEDLINE


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[PMID]:27413182
[Au] Autor:Ortega E; Manso JA; Buey RM; Carballido AM; Carabias A; Sonnenberg A; de Pereda JM
[Ad] Endereço:From the Instituto de Biología Molecular y Celular del Cancer, Consejo Superior de Investigaciones Científicas, University of Salamanca, 37007 Salamanca, Spain.
[Ti] Título:The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.
[So] Source:J Biol Chem;291(36):18643-62, 2016 09 02.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plakins are large multi-domain proteins that interconnect cytoskeletal structures. Plectin is a prototypical plakin that tethers intermediate filaments to membrane-associated complexes. Most plakins contain a plakin domain formed by up to nine spectrin repeats (SR1-SR9) and an SH3 domain. The plakin domains of plectin and other plakins harbor binding sites for junctional proteins. We have combined x-ray crystallography with small angle x-ray scattering (SAXS) to elucidate the structure of the plakin domain of plectin, extending our previous analysis of the SR1 to SR5 region. Two crystal structures of the SR5-SR6 region allowed us to characterize its uniquely wide inter-repeat conformational variability. We also report the crystal structures of the SR7-SR8 region, refined to 1.8 Å, and the SR7-SR9 at lower resolution. The SR7-SR9 region, which is conserved in all other plakin domains, forms a rigid segment stabilized by uniquely extensive inter-repeat contacts mediated by unusually long helices in SR8 and SR9. Using SAXS we show that in solution the SR3-SR6 and SR7-SR9 regions are rod-like segments and that SR3-SR9 of plectin has an extended shape with a small central kink. Other plakins, such as bullous pemphigoid antigen 1 and microtubule and actin cross-linking factor 1, are likely to have similar extended plakin domains. In contrast, desmoplakin has a two-segment structure with a central flexible hinge. The continuous versus segmented structures of the plakin domains of plectin and desmoplakin give insight into how different plakins might respond to tension and transmit mechanical signals.
[Mh] Termos MeSH primário: Plectina/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Seres Humanos
Plectina/genética
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (PLEC protein, human); 0 (Plectin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160715
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.732909



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