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Pesquisa : D05.750.078.593.450.300 [Categoria DeCS]
Referências encontradas : 54 [refinar]
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[PMID]:28362807
[Au] Autor:Min M; Chen XB; Wang P; Landeck L; Chen JQ; Li W; Cai SQ; Zheng M; Man XY
[Ad] Endereço:Department of Dermatology, Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
[Ti] Título:Role of keratin 24 in human epidermal keratinocytes.
[So] Source:PLoS One;12(3):e0174626, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Keratin 24 (K24) is a new kind of keratin genes, which encodes a novel keratin protein, K24 that bears high similarity to the type I keratins and displays a unique expression profile. However, the role of K24 is incompletely understood. In our study, we investigated the localization of K24 within the epidermis and possible functions. Keratin 24 was found to be modestly overexpressed in senescent keratinocytes and was mainly restricted to the upper stratum spinosum of epidermis. The protein was required for terminal differentiation upon CaCl2-induced differentiation. In vitro results showed that increased K24 in keratinocytes dramatically changed the differentiation of primary keratinocytes. It also inhibited cell survival by G1/S phase cell cycle arrest and induced senescence, autophagy and apoptosis of keratinocytes. In addition, K24 activated PKCδ signal pathway involving in cellular survival. In summary, K24 may be suggested as a potential differentiation marker and anti-proliferative factor in the epidermis.
[Mh] Termos MeSH primário: Epiderme/citologia
Queratinócitos/metabolismo
Queratinas Tipo I/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Apoptose/genética
Apoptose/fisiologia
Western Blotting
Ciclo Celular/genética
Ciclo Celular/fisiologia
Diferenciação Celular/genética
Diferenciação Celular/fisiologia
Sobrevivência Celular/genética
Sobrevivência Celular/fisiologia
Células Cultivadas
Feminino
Imunofluorescência
Seres Humanos
Queratinas Tipo I/genética
Masculino
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Meia-Idade
Transdução de Sinais/genética
Transdução de Sinais/fisiologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KRT24 protein, human); 0 (Keratins, Type I)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174626


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[PMID]:27477171
[Au] Autor:Stypczynska E; Placek W; Zegarska B; Czajkowski R
[Ti] Título:Keratinization Disorders and Genetic Aspects in Palmar and Plantar Keratodermas.
[So] Source:Acta Dermatovenerol Croat;24(2):116-23, 2016 Jun.
[Is] ISSN:1847-6538
[Cp] País de publicação:Croatia
[La] Idioma:eng
[Ab] Resumo:Palmoplantar keratoderma (PPK) is a heterogeneous group of hereditary and acquired disorders characterized by abnormal thickening of the palms and soles. There are three clinical patterns: diffuse, focal, and punctuate. Palmoplantar keratodermas can be divided into the following functional subgroups: disturbed gene functions in structural proteins (keratins), cornified envelope (loricrin, transglutaminase), cohesion (plakophilin, desmoplakin, desmoglein 1), cell-to-cell communication (connexins) and transmembrane signal transduction (cathepsin C). Unna-Thost disease is the most common variety of hereditary PPK. Mutations in keratin 1 have been reported in Unna-Thost disease. We report 12 cases in which Unna-Thost disease was diagnosed. Genealogical study demonstrated that the genodermatosis was a familial disease inherited as an autosomal dominant disorder. Dermatological examination revealed yellowish hyperkeratosis on the palms and soles. Oral mucosa, teeth, and nails remained unchanged. Histopathological examination of the biopsy sample taken from the soles of the patients showed orthokeratotic keratosis, hypergranulosis, and acanthosis without epidermolysis.
[Mh] Termos MeSH primário: Ceratodermia Palmar e Plantar/genética
Ceratodermia Palmar e Plantar/patologia
[Mh] Termos MeSH secundário: Adolescente
Feminino
Seres Humanos
Queratinas Tipo I/genética
Masculino
Meia-Idade
Mutação
Linhagem
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Keratins, Type I)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170331
[Lr] Data última revisão:
170331
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE


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[PMID]:26497548
[Au] Autor:Wang J; Yang X; Xiao H; Kong J; Bing M
[Ad] Endereço:Department of Anesthesiology, Shanghai Baoshan District Integrated Traditional and Western Medicine Hospital, Shanghai 201900, P.R. China.
[Ti] Título:Determination of the mechanism of action of repetitive halothane exposure on rat brain tissues using a combined method of microarray gene expression profiling and bioinformatics analysis.
[So] Source:Mol Med Rep;12(6):8071-6, 2015 Dec.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:The present study aimed to investigate the gene expression profiles of rats brain tissues treated with halothane compared with untreated controls to improve current understanding of the mechanism of action of the inhaled anesthetic. The GSE357 gene expression profile was dowloaded from the Gene Expression Omnibus database, and included six gene chips of samples repeatedly exposed to halothane and 12 gene chips of untreated controls. The differentially expressed genes (DEGs) between these two groups were identified using the Limma package in R language. Subsequently, the Database for Annotation, Visualization and Integrated Discovery was used to annotate the function of these DEGs. In addition, the most significantly upregulated gene and downregulated gene were annotated, to reveal the functional interactions with other associated genes, in FuncBase database. A total of 44 DEGs were obtained between The control and halothane exposure samples. Following Gene Ontology functional classification, these DEGs were found to be involved predominantly in the circulatory system, regulation of cell proliferation and response to endogenous stimulus and corticosteroid stimulus processes. KRT31 and HMGCS2, which were identified as the most significantly downregulated and upregulated DEGs, respectively, were associated with the lipid metabolic process and T cell activation, respectively. These results provided a basis for the development of improved inhalational anesthetics with minimal side effects and are essential for optimization of inhaled anesthetic techniques for advanced surgical procedures.
[Mh] Termos MeSH primário: Anestésicos Inalatórios/farmacologia
Encéfalo/efeitos dos fármacos
Regulação para Baixo/efeitos dos fármacos
Halotano/farmacologia
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Biologia Computacional
Bases de Dados Genéticas
Perfilação da Expressão Gênica
Redes Reguladoras de Genes/efeitos dos fármacos
Hidroximetilglutaril-CoA Sintase/metabolismo
Queratinas Tipo I/genética
Queratinas Tipo I/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anesthetics, Inhalation); 0 (Keratins, Type I); EC 2.3.3.10 (Hydroxymethylglutaryl-CoA Synthase); UQT9G45D1P (Halothane)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151120
[Lr] Data última revisão:
151120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151027
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2015.4462


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[PMID]:26160856
[Au] Autor:Ansar M; Raza SI; Lee K; Irfanullah; Shahi S; Acharya A; Dai H; Smith JD; Shendure J; Bamshad MJ; Nickerson DA; Santos-Cortez RL; Ahmad W; Leal SM
[Ad] Endereço:Department of Biochemistry, Faculty of Biological Sciences, Quaid-i-Azam University, Islamabad, Pakistan Department of Molecular and Human Genetics, Center for Statistical Genetics, Baylor College of Medicine, Houston, Texas, USA.
[Ti] Título:A homozygous missense variant in type I keratin KRT25 causes autosomal recessive woolly hair.
[So] Source:J Med Genet;52(10):676-80, 2015 Oct.
[Is] ISSN:1468-6244
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Woolly hair (WH) is a hair abnormality that is primarily characterised by tightly curled hair with abnormal growth. METHODS: In two unrelated consanguineous Pakistani families with non-syndromic autosomal recessive (AR) WH, homozygosity mapping and linkage analysis identified a locus within 17q21.1-q22, which contains the type I keratin gene cluster. A DNA sample from an affected individual from each family underwent exome sequencing. RESULTS: A homozygous missense variant c.950T>C (p.(Leu317Pro)) within KRT25 segregated with ARWH in both families, and has a combined maximum two-point LOD score of 7.9 at Ï´=0. The KRT25 variant is predicted to result in disruption of the second α-helical rod domain and the entire protein structure, thus possibly interfering with heterodimerisation of K25 with type II keratins within the inner root sheath (IRS) of the hair follicle and the medulla of the hair shaft. CONCLUSIONS: Our findings implicate a novel gene involved in human hair abnormality, and are consistent with the curled, fragile hair found in mice with Krt25 mutations, and further support the role of IRS-specific type I keratins in hair follicle development and maintenance of hair texture.
[Mh] Termos MeSH primário: Doenças do Cabelo/genética
Cabelo/anormalidades
Queratinas Tipo I/genética
Mutação de Sentido Incorreto
[Mh] Termos MeSH secundário: Criança
Pré-Escolar
Consanguinidade
Seres Humanos
Masculino
Paquistão
Linhagem
Análise de Sequência de DNA
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Keratins, Type I)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150711
[St] Status:MEDLINE
[do] DOI:10.1136/jmedgenet-2015-103255


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[PMID]:26154324
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Dipartimento Bigea, University of Bologna, Italy. lorenzo.alibardi@unibo.it.
[Ti] Título:Transition from embryonic to adult epidermis in reptiles occurs by the production of corneous beta-proteins.
[So] Source:Int J Dev Biol;58(10-12):829-39, 2014.
[Is] ISSN:1696-3547
[Cp] País de publicação:Spain
[La] Idioma:eng
[Ab] Resumo:The adaptation of the epidermis in amniote vertebrates to life on land took place by a drastic change from an embryonic epidermis made of two-four periderm layers to a terrestrial-proof epidermis. This transition occurred by the increase in types and number of specialized corneous proteins coded by genes of the Epidermal Differentiation Complex. The prevalent types of corneous proteins produced in the reptilian epidermis contain a beta-sheet region of high amino acid homology which allows their polymerization into a meshwork of filaments forming the hard corneous material of scales and claws. The present immunogold ultrastructural study shows that this transition occurs with the synthesis of glycine-rich corneous beta-proteins (formerly indicated as beta-keratins) that are added to the initial framework of acidic intermediate filaments produced in the embryonic epidermis of lizards, snake, alligator and turtle. These corneous beta-proteins are accumulated in the transitional and definitive layers of reptilian epidermis formed underneath the transitory two-four layered embryonic epidermis. In the more specialized reptiles capable of shedding the epidermis as a single unit, such as lizards and snakes, special glycine-cysteine rich beta-proteins are initially produced in a single layer immediately formed beneath the embryonic epidermis, the oberhautchen. The latter layer allows the in ovo shedding of the embryonic epidermis in preparation for hatching, and in the following shedding cycles of the adult epidermis. The production of specialized corneous-specific beta-proteins in addition to intermediate filament keratins was probably an essential addition for terrestrial life during the evolution of reptiles into different lineages, including birds. The increase of glycine and cysteine in epidermal proteins enhanced the hydrophobicity, insolubility and mechanical strength of the stratum corneum in these amniotes.
[Mh] Termos MeSH primário: Epiderme/embriologia
Queratinas Tipo I/metabolismo
Répteis/embriologia
Proteínas de Répteis/genética
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Evolução Biológica
Diferenciação Celular/genética
Embrião não Mamífero/embriologia
Epiderme/crescimento & desenvolvimento
Interações Hidrofóbicas e Hidrofílicas
Proteínas de Répteis/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Keratins, Type I); 0 (Reptilian Proteins); 0 (beta-Keratins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150709
[Lr] Data última revisão:
150709
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150709
[St] Status:MEDLINE
[do] DOI:10.1387/ijdb.140325la


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[PMID]:25041831
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Department of Bigea, University of Bologna, Italy. Electronic address: lorenzo.alibardi@unibo.it.
[Ti] Título:Immunodetection of type I acidic keratins associated to periderm granules during the transition of cornification from embryonic to definitive chick epidermis.
[So] Source:Micron;65:51-61, 2014 Oct.
[Is] ISSN:1878-4291
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The change in the modality of cornification from embryonic to definitive epidermis in the chick has been studied using immunocytochemistry and electron microscopy to show that the initial soft cornification based on an acidic type I alpha-keratin transits to a definitive hard cornification based on beta-proteins in the claw, scales and feathers. The first two periderm layers contain acidic keratins associated with periderm granules and participate in a mild form of cornification before shedding of the periderm. The transition from embryonic to adult cornification is best seen in the transitional layers of the claw where numerous periderm granules merge with packets or bundles of corneous beta-proteins. This process is hardly seen in scale and feathers where periderm granules remain most in the periderm or in the feather sheath. Periderm granules disappear in corneocytes generated underneath the periderm in scales or in the transitional layer in claws and are replaced by beta-proteins associated to other types of acidic alpha-keratins. This process produces a mechanically resistant corneous material underneath the softer periderm, adapted to terrestrial demand for mechanical protection in scales and in the dorsal part of the claw, the unguis. In the ventral part of the claw, the sub-unguis, scarce or no beta-proteins are accumulated resulting in a softer corneous layer. The study indicates that specific alpha-keratins form the cytoskeletal framework of definitive corneocytes in claws, scales and feathers, and that specialized corneous beta-proteins are deposited over this framework to produce epidermal layers with higher mechanical resistance.
[Mh] Termos MeSH primário: Embrião de Galinha/metabolismo
Galinhas/metabolismo
Grânulos Citoplasmáticos/metabolismo
Epiderme/metabolismo
Queratinas Tipo I/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular/fisiologia
Embrião de Galinha/embriologia
Galinhas/fisiologia
Grânulos Citoplasmáticos/fisiologia
Epiderme/fisiologia
Plumas/embriologia
Plumas/metabolismo
Imuno-Histoquímica/métodos
Microscopia Eletrônica/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Keratins, Type I)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:140721
[Lr] Data última revisão:
140721
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140722
[St] Status:MEDLINE


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[PMID]:24430440
[Au] Autor:Honda Y; Koike K; Kubo Y; Masuko S; Arakawa Y; Ando S
[Ad] Endereço:Department of Anatomy and Physiology, Faculty of Medicine, Saga University.
[Ti] Título:In vitro assembly properties of human type I and II hair keratins.
[So] Source:Cell Struct Funct;39(1):31-43, 2014.
[Is] ISSN:1347-3700
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Multiple type I and II hair keratins are expressed in hair-forming cells but the role of each protein in hair fiber formation remains obscure. In this study, recombinant proteins of human type I hair keratins (K35, K36 and K38) and type II hair keratins (K81 and K85) were prepared using bacterial expression systems. The heterotypic subunit interactions between the type I and II hair keratins were characterized using two-dimensional gel electrophoresis and surface plasmon resonance (SPR). Gel electrophoresis showed that the heterotypic complex-forming urea concentrations differ depending on the combination of keratins. K35-K85 and K36-K81 formed relatively stable heterotypic complexes. SPR revealed that soluble K35 bound to immobilized K85 with a higher affinity than to immobilized K81. The in vitro intermediate filament (IF) assembly of the hair keratins was explored by negative-staining electron microscopy. While K35-K81, K36-K81 and K35-K36-K81 formed IFs, K35-K85 afforded tight bundles of short IFs and large paracrystalline assemblies, and K36-K85 formed IF tangles. K85 promotes lateral association rather than elongation of short IFs. The in vitro assembly properties of hair keratins depended on the combination of type I and II hair keratins. Our data suggest the functional significance of K35-K85 and K36-K81 with distinct assembly properties in the formation of macrofibrils.
[Mh] Termos MeSH primário: Queratinas Tipo II/química
Queratinas Tipo II/metabolismo
Queratinas Tipo I/química
Queratinas Tipo I/metabolismo
Multimerização Proteica
[Mh] Termos MeSH secundário: Regulação da Expressão Gênica
Seres Humanos
Ligação Proteica
Estrutura Quaternária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Keratins, Type I); 0 (Keratins, Type II); 0 (Recombinant Proteins)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:140313
[Lr] Data última revisão:
140313
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140117
[St] Status:MEDLINE


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[PMID]:24276370
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Dipartimento di Biologia, Geologia e Scienze Ambientali, University of Bologna, Bologna, Italy, lorenzo.alibardi@unibo.it.
[Ti] Título:Immunolocalization of alpha-keratins and associated beta-proteins in lizard epidermis shows that acidic keratins mix with basic keratin-associated beta-proteins.
[So] Source:Protoplasma;251(4):827-37, 2014 Jul.
[Is] ISSN:1615-6102
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:The differentiation of the corneous layers of lizard epidermis has been analyzed by ultrastructural immunocytochemistry using specific antibodies against alpha-keratins and keratin associated beta-proteins (KAbetaPs, formerly indicated as beta-keratins). Both beta-cells and alpha-cells of the corneous layer derive from the same germinal layer. An acidic type I alpha-keratin is present in basal and suprabasal layers, early differentiating clear, oberhautchen, and beta-cells. Type I keratin apparently disappears in differentiated beta- and alpha-layers of the mature corneous layers. Conversely, a basic type II alpha-keratin rich in glycine is absent or very scarce in basal and suprabasal layers and this keratin likely does not pair with type I keratin to form intermediate filaments but is weakly detected in the pre-corneous and corneous alpha-layer. Single and double labeling experiments show that in differentiating beta-cells, basic KAbetaPs are added and replace type-I keratin to form the hard beta-layer. Epidermal alpha-keratins contain scarce cysteine (0.2-1.4 %) that instead represents 4-19 % of amino acids present in KAbetaPs. Possible chemical bonds formed between alpha-keratins and KAbetaPs may derive from electrostatic interactions in addition to cross-linking through disulphide bonds. Both the high content in glycine of keratins and KAbetaPs may also contribute to increase the hydrophobicy of the beta- and alpha-layers and the resistance of the corneous layer. The increase of gly-rich KAbetaPs amount and the bonds to the framework of alpha-keratins give rise to the inflexible beta-layer while the cys-rich KAbetaPs produce a pliable alpha-layer.
[Mh] Termos MeSH primário: Epiderme/metabolismo
Queratinas Tipo I/metabolismo
Queratinas/metabolismo
Lagartos/metabolismo
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Animais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Keratins, Type I); 0 (beta-Keratins); 68238-35-7 (Keratins)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131127
[St] Status:MEDLINE
[do] DOI:10.1007/s00709-013-0585-9


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[PMID]:24107002
[Au] Autor:Takemoto R; Jinnin M; Wang Z; Kudo H; Inoue K; Nakayama W; Ichihara A; Igata T; Kajihara I; Fukushima S; Ihn H
[Ad] Endereço:Department of Dermatology and Plastic Surgery, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
[Ti] Título:Hair miR-29a levels are decreased in patients with scleroderma.
[So] Source:Exp Dermatol;22(12):832-3, 2013 Dec.
[Is] ISSN:1600-0625
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:In the present study, we evaluated the possibility that we can utilize hair shaft miR-29a levels as disease marker of scleroderma. Hair samples were obtained from 20 scleroderma patients, five dermatomyositis patients and 13 controls. microRNAs were purified from hairs as well as skins or sera, and miR-29a levels were measured with quantitative real-time polymerase chain reaction. Mean hair miR-29a levels in scleroderma patients were significantly lower than those in control subjects or dermatomyositis, while expression levels of hair shaft marker keratin 34 were similar among them. There was no strong correlation among the miR-29a levels in the hair, skin and serum of each patient, suggesting that hair microRNAs can be independent biomarkers. We found scleroderma patients with decreased miR-29a levels had contracture of the phalanges at a significantly higher prevalence than those without. To confirm the clinical usefulness of hair microRNAs, large-scale researches are needed in the future.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica
Cabelo/metabolismo
MicroRNAs/metabolismo
Escleroderma Sistêmico/metabolismo
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Biomarcadores/metabolismo
Dermatomiosite/imunologia
Dermatomiosite/metabolismo
Feminino
Perfilação da Expressão Gênica
Seres Humanos
Queratinas Específicas do Cabelo/metabolismo
Queratinas Tipo I/metabolismo
Masculino
Meia-Idade
Técnicas de Diagnóstico Molecular
Projetos Piloto
Reação em Cadeia da Polimerase em Tempo Real
Pele/metabolismo
Pele/patologia
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (KRT34 protein, human); 0 (Keratins, Hair-Specific); 0 (Keratins, Type I); 0 (MIRN29 microRNA, human); 0 (MicroRNAs)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131011
[St] Status:MEDLINE
[do] DOI:10.1111/exd.12245


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[PMID]:24039993
[Au] Autor:Birkenkamp-Demtröder K; Hahn SA; Mansilla F; Thorsen K; Maghnouj A; Christensen R; Øster B; Ørntoft TF
[Ad] Endereço:Department of Molecular Medicine MOMA, Aarhus University Hospital, Skejby, Aarhus N, Denmark.
[Ti] Título:Keratin23 (KRT23) knockdown decreases proliferation and affects the DNA damage response of colon cancer cells.
[So] Source:PLoS One;8(9):e73593, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Keratin 23 (KRT23) is strongly expressed in colon adenocarcinomas but absent in normal colon mucosa. Array based methylation profiling of 40 colon samples showed that the promoter of KRT23 was methylated in normal colon mucosa, while hypomethylated in most adenocarcinomas. Promoter methylation correlated with absent expression, while increased KRT23 expression in tumor samples correlated with promoter hypomethylation, as confirmed by bisulfite sequencing. Demethylation induced KRT23 expression in vitro. Expression profiling of shRNA mediated stable KRT23 knockdown in colon cancer cell lines showed that KRT23 depletion affected molecules of the cell cycle and DNA replication, recombination and repair. In vitro analyses confirmed that KRT23 depletion significantly decreased the cellular proliferation of SW948 and LS1034 cells and markedly decreased the expression of genes involved in DNA damage response, mainly molecules of the double strand break repair homologous recombination pathway. KRT23 knockdown decreased the transcript and protein expression of key molecules as e.g. MRE11A, E2F1, RAD51 and BRCA1. Knockdown of KRT23 rendered colon cancer cells more sensitive to irradiation and reduced proliferation of the KRT23 depleted cells compared to irradiated control cells.
[Mh] Termos MeSH primário: Proliferação Celular
Reparo do DNA/genética
Queratinas Tipo I/genética
Interferência de RNA
[Mh] Termos MeSH secundário: Sequência de Bases
Western Blotting
Ciclo Celular/genética
Linhagem Celular Tumoral
Sobrevivência Celular/genética
Sobrevivência Celular/efeitos da radiação
Neoplasias do Colo/genética
Neoplasias do Colo/metabolismo
Neoplasias do Colo/patologia
Dano ao DNA
Metilação de DNA
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Raios gama
Regulação Neoplásica da Expressão Gênica/genética
Células HCT116
Células HEK293
Seres Humanos
Queratinas Tipo I/metabolismo
Proteína Homóloga a MRE11
Microscopia de Fluorescência
Dados de Sequência Molecular
Análise de Sequência com Séries de Oligonucleotídeos
Rad51 Recombinase/genética
Rad51 Recombinase/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transcriptoma/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (KRT23 protein, human); 0 (Keratins, Type I); 0 (MRE11A protein, human); EC 2.7.7.- (Rad51 Recombinase); EC 3.1.- (MRE11 Homologue Protein)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130917
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0073593



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