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Pesquisa : G02.111.570.080.534 [Categoria DeCS]
Referências encontradas : 217 [refinar]
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  1 / 217 MEDLINE  
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[PMID]:28464286
[Au] Autor:García-Vilchis D; Aranda-Anzaldo A
[Ad] Endereço:Facultad de Medicina, Laboratorio de Biología Molecular y Neurociencias, Universidad Autónoma del Estado de México, Toluca 50180, Edo. Méx., Mexico.
[Ti] Título:DNA Length Modulates the Affinity of Fragments of Genomic DNA for the Nuclear Matrix In Vitro.
[So] Source:J Cell Biochem;118(12):4487-4497, 2017 Dec.
[Is] ISSN:1097-4644
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Classical observations have shown that during the interphase the chromosomal DNA of metazoans is organized in supercoiled loops attached to a compartment known as the nuclear matrix (NM). Fragments of chromosomal DNA able to bind the isolated NM in vitro are known as matrix associated/attachment/addressed regions or MARs. No specific consensus sequence or motif has been found that may constitute a universal, defining feature of MARs. On the other hand, high-salt resistant DNA-NM interactions in situ define true DNA loop anchorage regions or LARs, that might correspond to a subset of the potential MARs but are not necessarily identical to MARs characterized in vitro, since there are several examples of MARs able to bind the NM in vitro but which are not actually bound to the NM in situ. In the present work we assayed the capacity of two LARs, as well as of shorter fragments within such LARs, for binding to the NM in vitro. Paradoxically the isolated (≈2 kb) LARs cannot bind to the NM in vitro while their shorter (≈300 pb) sub-fragments and other non-related but equally short DNA fragments, bind to the NM in a high-salt resistant fashion. Our results suggest that the ability of a given DNA fragment for binding to the NM in vitro primarily depends on the length of the fragment, suggesting that binding to the NM is modulated by the local topology of the DNA fragment in suspension that it is known to depend on the DNA length. J. Cell. Biochem. 118: 4487-4497, 2017. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: DNA/química
Hepatócitos/química
Regiões de Interação com a Matriz
Matriz Nuclear/química
[Mh] Termos MeSH secundário: Animais
DNA/metabolismo
Hepatócitos/metabolismo
Masculino
Matriz Nuclear/metabolismo
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1002/jcb.26106


  2 / 217 MEDLINE  
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[PMID]:28715274
[Au] Autor:Li Q; Wang W; Guo X; Jia YL; Wang YF; Wang TY
[Ad] Endereço:a Department of Biochemistry and Molecular Biology , Xinxiang Medical University , Xinxiang , China.
[Ti] Título:A short synthetic chimeric sequence harboring matrix attachment region/PSAR2 increases transgene expression in Chinese hamster ovary cells.
[So] Source:Biosci Biotechnol Biochem;81(9):1755-1761, 2017 Sep.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A chimeric DNA fragment containing an interferon-beta matrix attachment region (MAR) and an immunoglobulin MAR (PSAR2) was synthesized. PSAR2 was cloned into the upstream or downstream region of an enhanced green fluorescent protein (eGFP) expression cassette in a eukaryotic vector, which was then transfected into CHO cells. The results showed that PSAR2 did not effectively increase transgene expression when it was cloned into the upstream region of the eGFP expression cassette. However, when inserted downstream of the eGFP expression cassette, PSAR2-enhanced transient transgene expression and significantly increased the numbers of stably transfected cells compared with the control vector. Additionally, PSAR2 significantly increased eGFP copy numbers as compared with the control vector. PSAR2 could significantly enhance transgene expression in CHO cells according to the position in the vector and increased transgene copy numbers. We found a short chimeric sequence harboring two MARs effectively increased transgene expression in CHO cells.
[Mh] Termos MeSH primário: Engenharia Genética/métodos
Imunoglobulinas/genética
Regiões de Interação com a Matriz/genética
Transgenes/genética
[Mh] Termos MeSH secundário: Animais
Células CHO
Cricetinae
Cricetulus
Proteínas de Fluorescência Verde/genética
Plasmídeos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulins); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1350563


  3 / 217 MEDLINE  
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[PMID]:27627025
[Au] Autor:Dobson JR; Hong D; Barutcu AR; Wu H; Imbalzano AN; Lian JB; Stein JL; van Wijnen AJ; Nickerson JA; Stein GS
[Ad] Endereço:Department of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, Massachusetts.
[Ti] Título:Identifying Nuclear Matrix-Attached DNA Across the Genome.
[So] Source:J Cell Physiol;232(6):1295-1305, 2017 Jun.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Experimental approaches to define the relationship between gene expression and nuclear matrix attachment regions (MARs) have given contrasting and method-specific results. We have developed a next generation sequencing strategy to identify MARs across the human genome (MAR-Seq). The method is based on crosslinking chromatin to its nuclear matrix attachment sites to minimize changes during biochemical processing. We used this method to compare nuclear matrix organization in MCF-10A mammary epithelial-like cells and MDA-MB-231 breast cancer cells and evaluated the results in the context of global gene expression (array analysis) and positional enrichment of gene-regulatory histone modifications (ChIP-Seq). In the normal-like cells, nuclear matrix-attached DNA was enriched in expressed genes, while in the breast cancer cells, it was enriched in non-expressed genes. In both cell lines, the chromatin modifications that mark transcriptional activation or repression were appropriately associated with gene expression. Using this new MAR-Seq approach, we provide the first genome-wide characterization of nuclear matrix attachment in mammalian cells and reveal that the nuclear matrix-associated genome is highly cell-context dependent. J. Cell. Physiol. 232: 1295-1305, 2017. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: DNA/metabolismo
Genoma Humano
Regiões de Interação com a Matriz/genética
Matriz Nuclear/metabolismo
[Mh] Termos MeSH secundário: Neoplasias da Mama/genética
Linhagem Celular
Cromatina/metabolismo
Reagentes para Ligações Cruzadas/metabolismo
Feminino
Imunofluorescência
Regulação Neoplásica da Expressão Gênica
Histonas/metabolismo
Seres Humanos
Fases de Leitura Aberta/genética
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Cross-Linking Reagents); 0 (Histones); 9007-49-2 (DNA)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160915
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25596


  4 / 217 MEDLINE  
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[PMID]:27575535
[Au] Autor:Kostyrko K; Neuenschwander S; Junier T; Regamey A; Iseli C; Schmid-Siegert E; Bosshard S; Majocchi S; Le Fourn V; Girod PA; Xenarios I; Mermod N
[Ad] Endereço:Department of Fundamental Microbiology, Institute of Biotechnology, University of Lausanne, and Center for Biotechnology UNIL-EPFL, Lausanne, Switzerland.
[Ti] Título:MAR-Mediated transgene integration into permissive chromatin and increased expression by recombination pathway engineering.
[So] Source:Biotechnol Bioeng;114(2):384-396, 2017 Feb.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Untargeted plasmid integration into mammalian cell genomes remains a poorly understood and inefficient process. The formation of plasmid concatemers and their genomic integration has been ascribed either to non-homologous end-joining (NHEJ) or homologous recombination (HR) DNA repair pathways. However, a direct involvement of these pathways has remained unclear. Here, we show that the silencing of many HR factors enhanced plasmid concatemer formation and stable expression of the gene of interest in Chinese hamster ovary (CHO) cells, while the inhibition of NHEJ had no effect. However, genomic integration was decreased by the silencing of specific HR components, such as Rad51, and DNA synthesis-dependent microhomology-mediated end-joining (SD-MMEJ) activities. Genome-wide analysis of the integration loci and junction sequences validated the prevalent use of the SD-MMEJ pathway for transgene integration close to cellular genes, an effect shared with matrix attachment region (MAR) DNA elements that stimulate plasmid integration and expression. Overall, we conclude that SD-MMEJ is the main mechanism driving the illegitimate genomic integration of foreign DNA in CHO cells, and we provide a recombination engineering approach that increases transgene integration and recombinant protein expression in these cells. Biotechnol. Bioeng. 2017;114: 384-396. © 2016 The Authors. Biotechnology and Bioengineering published by Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Cromatina/genética
Engenharia Genética/métodos
Regiões de Interação com a Matriz/genética
Proteínas Recombinantes/genética
Recombinação Genética/genética
[Mh] Termos MeSH secundário: Animais
Anticorpos/química
Anticorpos/genética
Anticorpos/metabolismo
Células CHO
Cricetinae
Cricetulus
Técnicas de Silenciamento de Genes
Seres Humanos
Plasmídeos/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Transgenes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Chromatin); 0 (Recombinant Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160831
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26086


  5 / 217 MEDLINE  
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[PMID]:28026824
[Au] Autor:Wasag P; Lenartowski R
[Ad] Endereço:Zaklad Genetyki, Wydzial Biologii i Ochrony Srodowiska, UMK w Toruniu; Pracownia Izotopowa i Analizy Instrumentalnej, Wydzial Biologii i Ochrony Srodowiska, UMK w Toruniu.
[Ti] Título:Nuclear matrix - structure, function and pathogenesis.
[So] Source:Postepy Hig Med Dosw (Online);70(0):1206-1219, 2016 Dec 20.
[Is] ISSN:1732-2693
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:The nuclear matrix (NM), or nuclear skeleton, is the non-chromatin, ribonucleoproteinaceous framework that is resistant to high ionic strength buffers, nonionic detergents, and nucleolytic enzymes. The NM fulfills a structural role in eukaryotic cells and is responsible for maintaining the shape of the nucleus and the spatial organization of chromatin. Moreover, the NM participates in several cellular processes, such as DNA replication/repair, gene expression, RNA transport, cell signaling and differentiation, cell cycle regulation, apoptosis and carcinogenesis. Short nucleotide sequences called scaffold/matrix attachment regions (S/MAR) anchor the chromatin loops to the NM proteins (NMP). The NMP composition is dynamic and depends on the cell type and differentiation stage or metabolic activity. Alterations in the NMP composition affect anchoring of the S/MARs and thus alter gene expression. This review aims to systematize information about the skeletal structure of the nucleus, with particular emphasis on the organization of the NM and its role in selected cellular processes. We also discuss several diseases that are caused by aberrant NM structure or dysfunction of individual NM elements.
[Mh] Termos MeSH primário: Replicação do DNA
Matriz Nuclear/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Núcleo Celular/metabolismo
Cromatina/metabolismo
Seres Humanos
Regiões de Interação com a Matriz
Neoplasias/metabolismo
Proteínas Nucleares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin); 0 (Nuclear Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE


  6 / 217 MEDLINE  
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[PMID]:27863031
[Au] Autor:Shiokawa Z; Kashiwabara E; Yoshidome D; Fukase K; Inuki S; Fujimoto Y
[Ad] Endereço:Department of Chemistry, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama, Kanagawa, 223-8522, Japan.
[Ti] Título:Discovery of a Novel Scaffold as an Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitor Based on the Pyrrolopiperazinone Alkaloid, Longamide B.
[So] Source:ChemMedChem;11(24):2682-2689, 2016 Dec 16.
[Is] ISSN:1860-7187
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Indoleamine 2,3-dioxygenase 1 (IDO1) has emerged as a key target for cancer therapy, as IDO1 plays a critical role in the capacity of tumor cells to evade the immune system. The pyrrolopiperazinone alkaloid longamide B and its derivatives were identified as novel IDO1 inhibitors based on docking studies and small library synthesis. The thioamide derivative showed higher IDO1 inhibitory activity than longamide B, and displayed an activity similar to that of a representative IDO1 inhibitor, 1-methyl-tryptophan. These results suggest that the pyrrolopiperazinone scaffold of longamide B could be used in the development of IDO1 inhibitors.
[Mh] Termos MeSH primário: Descoberta de Drogas
Indolamina-Pirrol 2,3,-Dioxigenase/antagonistas & inibidores
Pirróis/química
Pirróis/farmacologia
[Mh] Termos MeSH secundário: Ativação Enzimática/efeitos dos fármacos
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Regiões de Interação com a Matriz
Modelos Moleculares
Piperazinas/química
Piperazinas/farmacologia
Pirazóis/química
Pirazóis/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Indoleamine-Pyrrole 2,3,-Dioxygenase); 0 (Piperazines); 0 (Pyrazoles); 0 (Pyrroles); 0 (longamide B); 0 (pyrazolopiperazinone)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1002/cmdc.201600446


  7 / 217 MEDLINE  
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[PMID]:27614752
[Au] Autor:Xu Z; Chen F; Zhang L; Lu J; Xu P; Liu G; Xie X; Mu W; Wang Y; Liu D
[Ad] Endereço:State Key Laboratory of Medical Molecular Biology, Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100005, China.
[Ti] Título:Non-integrating lentiviral vectors based on the minimal S/MAR sequence retain transgene expression in dividing cells.
[So] Source:Sci China Life Sci;59(10):1024-1033, 2016 Oct.
[Is] ISSN:1869-1889
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Safe and efficient gene transfer systems are the basis of gene therapy applications. Non-integrating lentiviral (NIL) vectors are among the most promising candidates for gene transfer tools, because they exhibit high transfer efficiency in both dividing and non-dividing cells and do not present a risk of insertional mutagenesis. However, non-integrating lentiviral vectors cannot introduce stable exogenous gene expression to dividing cells, thereby limiting their application. Here, we report the design of a non-integrating lentiviral vector that contains the minimal scaffold/matrix attachment region (S/MAR) sequence (SNIL), and this SNIL vector is able to retain episomal transgene expression in dividing cells. Using SNIL vectors, we detected the expression of the eGFP gene for 61 days in SNIL-transduced stable CHO cells, either with selection or not. In the NIL group without the S/MAR sequence, however, the transduced cells died under selection for the transient expression of NIL vectors. Furthermore, Southern blot assays demonstrated that the SNIL vectors were retained extrachromosomally in the CHO cells. In conclusion, the minimal S/MAR sequence retained the non-integrating lentiviral vectors in dividing cells, which indicates that SNIL vectors have the potential for use as a gene transfer tool.
[Mh] Termos MeSH primário: Expressão Gênica
Lentivirus/genética
Regiões de Interação com a Matriz/genética
Transgenes/genética
[Mh] Termos MeSH secundário: Animais
Células CHO
Divisão Celular/genética
Cricetinae
Cricetulus
Técnicas de Transferência de Genes
Terapia Genética/métodos
Vetores Genéticos/genética
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HEK293
Seres Humanos
Plasmídeos/genética
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Reprodutibilidade dos Testes
Transfecção/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Fusion Proteins); 147336-22-9 (Green Fluorescent Proteins)
[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:160912
[St] Status:MEDLINE


  8 / 217 MEDLINE  
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[PMID]:27307589
[Au] Autor:Tesfay L; Schulz VV; Frank SB; Lamb LE; Miranti CK
[Ad] Endereço:Laboratory of Integrin Signaling and Tumorigenesis, Van Andel Research Institute, Grand Rapids, MI 49503.
[Ti] Título:Receptor tyrosine kinase Met promotes cell survival via kinase-independent maintenance of integrin α3ß1.
[So] Source:Mol Biol Cell;27(15):2493-504, 2016 08 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Matrix adhesion via integrins is required for cell survival. Adhesion of epithelial cells to laminin via integrin α3ß1 was previously shown to activate at least two independent survival pathways. First, integrin α3ß1 is required for autophagy-induced cell survival after growth factor deprivation. Second, integrin α3ß1 independently activates two receptor tyrosine kinases, EGFR and Met, in the absence of ligands. EGFR signaling to Erk promotes survival independently of autophagy. To determine how Met promotes cell survival, we inhibited Met kinase activity or blocked its expression with RNA interference. Loss of Met expression, but not inhibition of Met kinase activity, induced apoptosis by reducing integrin α3ß1 levels, activating anoikis, and blocking autophagy. Met was specifically required for the assembly of autophagosomes downstream of LC3II processing. Reexpression of wild-type Met, kinase-dead Met, or integrin α3 was sufficient to rescue death upon removal of endogenous Met. Integrin α3ß1 coprecipitated and colocalized with Met in cells. The extracellular and transmembrane domain of Met was required to fully rescue cell death and restore integrin α3 expression. Thus Met promotes survival of laminin-adherent cells by maintaining integrin α3ß1 via a kinase-independent mechanism.
[Mh] Termos MeSH primário: Integrina alfa3beta1/metabolismo
Proteínas Proto-Oncogênicas c-met/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Adesão Celular/fisiologia
Morte Celular
Sobrevivência Celular/fisiologia
Células Epiteliais/metabolismo
Matriz Extracelular/metabolismo
Seres Humanos
Integrina alfa3beta1/genética
Integrinas/metabolismo
Laminina/metabolismo
Sistema de Sinalização das MAP Quinases
Masculino
Regiões de Interação com a Matriz
Fosforilação
Cultura Primária de Células
Próstata
Receptores Proteína Tirosina Quinases/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Integrin alpha3beta1); 0 (Integrins); 0 (Laminin); EC 2.7.10.1 (Proto-Oncogene Proteins c-met); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-09-0649


  9 / 217 MEDLINE  
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[PMID]:27263292
[Au] Autor:Li Q; Zhao CP; Wang XY; Sun QL; Wang TY
[Ti] Título:[Effect of Intron Orientation on the Expression of Transgene Imposed by MAR Expression Vector in Stably Recombinant CHO Cells].
[So] Source:Sichuan Da Xue Xue Bao Yi Xue Ban;47(2):189-91, 243, 2016 Mar.
[Is] ISSN:1672-173X
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To determine the effect of intron orientation on the transgene expression level imposed by matrix attachment region (MAR) expression vector. METHODS: The MAR of ß-globin was amplified by PCR, and then cloned into MAR expression vectors. An intron sequence was digested with restriction enzyme, ligated to the MAR expression vector in reverse orientation, and then transfected into Chinese hamster ovary (CHO) cells. The transfected stable cells were screened by G418. The level of chloramphenicol acetyltransferase (CAT) gene expression was analyzed by ELISA method. RESULTS: The transgene expression levels of CHO cells with the two expression vectors with a positive intron or without MAR were higher than that of CHO cells with an expression vector with reverse intron (P < 0.05). MAR did not improve transgene expression with reverse intron presence. CONCLUSION: Different orientation of intron can affect transgene expression in recombinant CHO cells. The transgene expression level can be increased using positive intron and MAR.
[Mh] Termos MeSH primário: Engenharia Genética/métodos
Vetores Genéticos
Íntrons
Regiões de Interação com a Matriz
Transgenes
[Mh] Termos MeSH secundário: Animais
Células CHO
Cricetinae
Cricetulus
Dosagem de Genes
Transfecção
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160606
[Lr] Data última revisão:
160606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160607
[St] Status:MEDLINE


  10 / 217 MEDLINE  
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PubMed Central Texto completo
Texto completo
[PMID]:27079701
[Au] Autor:Otto GP; Sharma D; Williams RS
[Ti] Título:Non-Catalytic Roles of Presenilin Throughout Evolution.
[So] Source:J Alzheimers Dis;52(4):1177-87, 2016 Apr 12.
[Is] ISSN:1875-8908
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Research into Alzheimer's disease pathology and treatment has often focused on presenilin proteins. These proteins provide the key catalytic activity of the γ-secretase complex in the cleavage of amyloid-ß precursor protein and resultant amyloid tangle deposition. Over the last 25 years, screening novel drugs to control this aberrant proteolytic activity has yet to identify effective treatments for the disease. In the search for other mechanisms of presenilin pathology, several studies have demonstrated that mammalian presenilin proteins also act in a non-proteolytic role as a scaffold to co-localize key signaling proteins. This role is likely to represent an ancestral presenilin function, as it has been described in genetically distant species including non-mammalian animals, plants, and a simple eukaryotic amoeba Dictyostelium that diverged from the human lineage over a billion years ago. Here, we review the non-catalytic scaffold role of presenilin, from mammalian models to other biomedical models, and include recent insights using Dictyostelium, to suggest that this role may provide an early evolutionary function of presenilin proteins.
[Mh] Termos MeSH primário: Presenilinas/fisiologia
[Mh] Termos MeSH secundário: Animais
Evolução Biológica
Dictyostelium/metabolismo
Mamíferos/metabolismo
Regiões de Interação com a Matriz/fisiologia
Camundongos
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Presenilins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160416
[St] Status:MEDLINE
[do] DOI:10.3233/JAD-150940



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