Base de dados : MEDLINE
Pesquisa : D12.776.543.990.300.300 [Categoria DeCS]
Referências encontradas : 459 [refinar]
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[PMID]:28646128
[Au] Autor:Duangtum N; Junking M; Phadngam S; Sawasdee N; Castiglioni A; Charngkaew K; Limjindaporn T; Isidoro C; Yenchitsomanus PT
[Ad] Endereço:Division of Molecular Medicine, Department of Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand.
[Ti] Título:γ-COPI mediates the retention of kAE1 G701D protein in Golgi apparatus - a mechanistic explanation of distal renal tubular acidosis associated with the G701D mutation.
[So] Source:Biochem J;474(15):2573-2584, 2017 Jul 17.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations of the ( ) gene encoding kidney anion (chloride/bicarbonate ion) exchanger 1 (kAE1) can cause genetic distal renal tubular acidosis (dRTA). Different mutations give rise to mutant kAE1 proteins with distinct defects in protein trafficking. The mutant kAE1 protein may be retained in endoplasmic reticulum (ER) or Golgi apparatus, or mis-targeted to the apical membrane, failing to display its function at the baso-lateral membrane. The ER-retained mutant kAE1 interacts with calnexin chaperone protein; disruption of this interaction permits the mutant kAE1 to reach the cell surface and display anion exchange activity. However, the mechanism of Golgi retention of mutant kAE1 G701D protein, which is otherwise functional, is still unclear. In the present study, we show that Golgi retention of kAE1 G701D is due to a stable interaction with the Golgi-resident protein, coat protein complex I (COPI), that plays a role in retrograde vesicular trafficking and Golgi-based quality control. The interaction and co-localization of kAE1 G701D with the γ-COPI subunit were demonstrated in human embryonic kidney (HEK-293T) cells by co-immunoprecipitation and immunofluorescence staining. Small interference RNA (siRNA) silencing of COPI expression in the transfected HEK-293T cells increased the cell surface expression of transgenic kAE1 G701D, as shown by immunofluorescence staining. Our data unveil the molecular mechanism of Golgi retention of kAE1 G701D and suggest that disruption of the COPI-kAE1 G701D interaction could be a therapeutic strategy to treat dRTA caused by this mutant.
[Mh] Termos MeSH primário: Acidose Tubular Renal/metabolismo
Proteína 1 de Troca de Ânion do Eritrócito/genética
Proteína Coatomer/metabolismo
Complexo de Golgi/metabolismo
Mutação/genética
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal
Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Técnicas de Silenciamento de Genes
Complexo de Golgi/ultraestrutura
Células HEK293
Seres Humanos
Rim/patologia
Rim/ultraestrutura
Modelos Biológicos
Proteínas Mutantes/metabolismo
Ligação Proteica
Subunidades Proteicas/metabolismo
RNA Interferente Pequeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Anion Exchange Protein 1, Erythrocyte); 0 (COPG protein, human); 0 (Coatomer Protein); 0 (Mutant Proteins); 0 (Protein Subunits); 0 (RNA, Small Interfering)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170625
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170088


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[PMID]:28442536
[Au] Autor:Maeda M; Katada T; Saito K
[Ad] Endereço:Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan.
[Ti] Título:TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient secretion.
[So] Source:J Cell Biol;216(6):1731-1743, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian endoplasmic reticulum (ER) exit sites export a variety of cargo molecules including oversized cargoes such as collagens. However, the mechanisms of their assembly and organization are not fully understood. TANGO1L is characterized as a collagen receptor, but the function of TANGO1S remains to be investigated. Here, we show that direct interaction between both isoforms of TANGO1 and Sec16 is not only important for their correct localization but also critical for the organization of ER exit sites. The depletion of TANGO1 disassembles COPII components as well as membrane-bound ER-resident complexes, resulting in fewer functional ER exit sites and delayed secretion. The ectopically expressed TANGO1 C-terminal domain responsible for Sec16 binding in mitochondria is capable of recruiting Sec16 and other COPII components. Moreover, TANGO1 recruits membrane-bound macromolecular complexes consisting of cTAGE5 and Sec12 to the ER exit sites. These data suggest that mammalian ER exit sites are organized by TANGO1 acting as a scaffold, in cooperation with Sec16 for efficient secretion.
[Mh] Termos MeSH primário: Translocador Nuclear Receptor Aril Hidrocarboneto/metabolismo
Retículo Endoplasmático/metabolismo
Proteínas de Transporte Vesicular/metabolismo
[Mh] Termos MeSH secundário: Antígenos de Neoplasias/genética
Antígenos de Neoplasias/metabolismo
Translocador Nuclear Receptor Aril Hidrocarboneto/genética
Proteína Coatomer/metabolismo
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Retículo Endoplasmático/secreção
Fatores de Troca do Nucleotídeo Guanina/genética
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Proteínas de Neoplasias/genética
Proteínas de Neoplasias/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Interferência de RNA
Transdução de Sinais
Fatores de Tempo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Transfecção
Proteínas de Transporte Vesicular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARNT protein, human); 0 (Antigens, Neoplasm); 0 (CTAGE5 protein, human); 0 (Coatomer Protein); 0 (DNA-Binding Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (Neoplasm Proteins); 0 (PREB protein, human); 0 (SEC16A protein, human); 0 (Transcription Factors); 0 (Vesicular Transport Proteins); 138391-32-9 (Aryl Hydrocarbon Receptor Nuclear Translocator)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201703084


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[PMID]:28428367
[Au] Autor:Gorur A; Yuan L; Kenny SJ; Baba S; Xu K; Schekman R
[Ad] Endereço:Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720.
[Ti] Título:COPII-coated membranes function as transport carriers of intracellular procollagen I.
[So] Source:J Cell Biol;216(6):1745-1759, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The coat protein complex II (COPII) is essential for the transport of large cargo, such as 300-nm procollagen I (PC1) molecules, from the endoplasmic reticulum (ER) to the Golgi. Previous work has shown that the CUL3-KLHL12 complex increases the size of COPII vesicles at ER exit sites to more than 300 nm in diameter and accelerates the secretion of PC1. However, the role of large COPII vesicles as PC1 transport carriers was not unambiguously demonstrated. In this study, using stochastic optical reconstruction microscopy, correlated light electron microscopy, and live-cell imaging, we demonstrate the existence of mobile COPII-coated vesicles that completely encapsulate the cargo PC1 and are physically separated from ER. We also developed a cell-free COPII vesicle budding reaction that reconstitutes the capture of PC1 into large COPII vesicles. This process requires COPII proteins and the GTPase activity of the COPII subunit SAR1. We conclude that large COPII vesicles are bona fide carriers of PC1.
[Mh] Termos MeSH primário: Vesículas Revestidas pelo Complexo de Proteína do Envoltório/metabolismo
Proteína Coatomer/metabolismo
Colágeno Tipo I/metabolismo
Corpos Multivesiculares/metabolismo
Pró-Colágeno/metabolismo
[Mh] Termos MeSH secundário: Vesículas Revestidas pelo Complexo de Proteína do Envoltório/ultraestrutura
Linhagem Celular Tumoral
Colágeno Tipo I/genética
Proteínas Culina/genética
Proteínas Culina/metabolismo
Seres Humanos
Proteínas dos Microfilamentos/genética
Proteínas dos Microfilamentos/metabolismo
Microscopia de Fluorescência
Microscopia Imunoeletrônica
Microscopia de Vídeo
Proteínas Monoméricas de Ligação ao GTP/genética
Proteínas Monoméricas de Ligação ao GTP/metabolismo
Corpos Multivesiculares/ultraestrutura
Pró-Colágeno/genética
Transporte Proteico
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (CUL3 protein, human); 0 (Coatomer Protein); 0 (Collagen Type I); 0 (Cullin Proteins); 0 (KLHL12 protein, human); 0 (Microfilament Proteins); 0 (Procollagen); 0 (collagen type I, alpha 1 chain); EC 3.6.1.- (SAR1A protein, human); EC 3.6.5.2 (Monomeric GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201702135


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[PMID]:28045387
[Au] Autor:Lunev S; Semmelink MF; Xian JL; Ma KY; Leenders AJ; Dömling AS; Shtutman M; Groves MR
[Ad] Endereço:Department of Drug Design, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9700 AD Groningen, The Netherlands.
[Ti] Título:Crystal structure of truncated human coatomer protein complex subunit ζ1 (Copζ1).
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 1):1-8, 2017 01 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The majority of modern anticancer approaches target DNA/protein targets involved in tumour-cell proliferation. Such approaches have a major drawback, as nonproliferating cancer cells remain unaffected and may cause relapse or remission. Human coatomer protein complex I (COPI) subunit ζ (Copζ), a component of the coat protein involved in cell apoptosis and intracellular trafficking, has recently been proposed as a potential anticancer drug target. Previous studies have shown that two different isoforms of the Copζ subunit exist in mammalian cells. While normal cells express both Copζ1 and Copζ2 isoforms, various types of tumour cells display a loss of Copζ2 expression and rely solely on Copζ1 for growth and survival. Subsequent knockdown of Copζ1 results in specific inhibition of both proliferating and dormant tumour-cell populations, with no adverse growth effects on normal cells. Therefore, a Copζ1-targeting therapy was proposed to bypass the problem of dormant cancer cells that are resistant to conventional antiproliferative drugs, which is the major cause of tumour relapse. In order to aid in structure-based inhibitor design, a crystal structure is required. In this article, the recombinant expression, purification, crystallization and crystal structure of Copζ1, as well as the expression and purification of Copζ2, are reported.
[Mh] Termos MeSH primário: Proteína Coatomer/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Seres Humanos
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Coatomer Protein)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170411
[Lr] Data última revisão:
170411
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X16018896


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[PMID]:27986120
[Au] Autor:Mi Y; Yu M; Zhang L; Sun C; Wei B; Ding W; Zhu Y; Tang J; Xia G; Zhu L
[Ad] Endereço:Department of Urology, Huashan Hospital, Fudan University, Shanghai, PR China; Department of Urology, Third Affiliated Hospital of Nantong University, Wuxi, Jiangsu, PR China.
[Ti] Título:COPB2 Is Upregulated in Prostate Cancer and Regulates PC-3 Cell Proliferation, Cell Cycle, and Apoptosis.
[So] Source:Arch Med Res;47(6):411-418, 2016 Aug.
[Is] ISSN:1873-5487
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND AIMS: Transport of membranes and proteins in eukaryotic cells is mediated by vesicular carriers. Coatomer complex I (COPI)-coated vesicles are involved in the transport between endoplasmic reticulum (ER) and Golgi complex. Several studies indicated that some subunits of COPI were correlated with the cell proliferation of malignant tumors. The present study focused on the function of coatomer protein complex subunit ß 2 (COPB2), one of seven proteins in COPI, in prostate cancer (PCa). METHODS: COPB2 gene expression was first analyzed by immunohistochemistry (IHC) in 15 paired PCa and carcinoma adjacent normal tissue from patients. To investigate the role of COPB2 in PCa, we used lentivirus-mediated small interfering RNA (siRNA) to knockdown COPB2 expression in human PCa cell line PC-3 and assessed it by RT-qPCR. Cellomics ArrayScan VTI imaging and colony formation were conducted to evaluate cell proliferation. Cell cycle phase arrest and apoptosis were assayed by flow cytometry. RESULTS: COPB2 gene was upregulated in the PCa tissue. Cell proliferation was significantly inhibited in COPB2-silenced PC-3 cells using both Cellomics ArrayScan VTI imaging and colony formation assays. S-phase cell counts were significantly decreased; G1- and G2-phase cell counts were significantly increased in COPB2-siRNA group than the control group. Apoptosis was significantly increased in COPB2-siRNA cells. CONCLUSIONS: COPB2 significantly promoted PC-3 cell proliferation and colony formation through the cell cycle and apoptosis pathway. Moreover, COPB2 showed a clinical correlation and may serve as a biomarker for the detection for PCa.
[Mh] Termos MeSH primário: Apoptose
Proteína Coatomer/metabolismo
Neoplasias da Próstata/metabolismo
Neoplasias da Próstata/patologia
[Mh] Termos MeSH secundário: Ciclo Celular
Linhagem Celular Tumoral
Proliferação Celular
Proteína Coatomer/genética
Citometria de Fluxo
Seres Humanos
Masculino
RNA Interferente Pequeno/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (COPB2 protein, human); 0 (Coatomer Protein); 0 (RNA, Small Interfering)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170526
[Lr] Data última revisão:
170526
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE


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[PMID]:27744351
[Au] Autor:Rajappa-Titu L; Suematsu T; Munoz-Tello P; Long M; Demir Ö; Cheng KJ; Stagno JR; Luecke H; Amaro RE; Aphasizheva I; Aphasizhev R; Thore S
[Ad] Endereço:Department of Molecular Biology, University of Geneva, 1211 Geneva, Switzerland.
[Ti] Título:RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting.
[So] Source:Nucleic Acids Res;44(22):10862-10878, 2016 Dec 15.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species. Uridylation plays a particularly prominent role in RNA processing pathways of kinetoplastid protists typified by the causative agent of African sleeping sickness, Trypanosoma brucei In mitochondria of this pathogen, most mRNAs are internally modified by U-insertion/deletion editing while guide RNAs and rRNAs are U-tailed. The founding member of TUTase family, RNA editing TUTase 1 (RET1), functions as a subunit of the 3' processome in uridylation of gRNA precursors and mature guide RNAs. Along with KPAP1 poly(A) polymerase, RET1 also participates in mRNA translational activation. RET1 is divergent from human TUTases and is essential for parasite viability in the mammalian host and the insect vector. Given its robust in vitro activity, RET1 represents an attractive target for trypanocide development. Here, we report high-resolution crystal structures of the RET1 catalytic core alone and in complex with UTP analogs. These structures reveal a tight docking of the conserved nucleotidyl transferase bi-domain module with a RET1-specific C2H2 zinc finger and RNA recognition (RRM) domains. Furthermore, we define RET1 region required for incorporation into the 3' processome, determinants for RNA binding, subunit oligomerization and processive UTP incorporation, and predict druggable pockets.
[Mh] Termos MeSH primário: Proteína Coatomer/química
Proteínas de Protozoários/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Cristalografia por Raios X
Desenho de Drogas
Ligações de Hidrogênio
Cinética
Leishmania/enzimologia
Simulação de Dinâmica Molecular
Ligação Proteica
Conformação Proteica em alfa-Hélice
Edição de RNA
Especificidade por Substrato
Tripanossomicidas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coatomer Protein); 0 (Protozoan Proteins); 0 (Trypanocidal Agents)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161017
[St] Status:MEDLINE


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[PMID]:27476655
[Au] Autor:Izumi K; Brett M; Nishi E; Drunat S; Tan ES; Fujiki K; Lebon S; Cham B; Masuda K; Arakawa M; Jacquinet A; Yamazumi Y; Chen ST; Verloes A; Okada Y; Katou Y; Nakamura T; Akiyama T; Gressens P; Foo R; Passemard S; Tan EC; El Ghouzzi V; Shirahige K
[Ad] Endereço:Research Center for Epigenetic Disease, Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan; Division of Medical Genetics, Nagano Children's Hospital, Azumino 399-8205, Japan; Division of Human Genetics, The Children's Hospital of Philadelphia, Philadelphi
[Ti] Título:ARCN1 Mutations Cause a Recognizable Craniofacial Syndrome Due to COPI-Mediated Transport Defects.
[So] Source:Am J Hum Genet;99(2):451-9, 2016 Aug 04.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular homeostasis is maintained by the highly organized cooperation of intracellular trafficking systems, including COPI, COPII, and clathrin complexes. COPI is a coatomer protein complex responsible for intracellular protein transport between the endoplasmic reticulum and the Golgi apparatus. The importance of such intracellular transport mechanisms is underscored by the various disorders, including skeletal disorders such as cranio-lenticulo-sutural dysplasia and osteogenesis imperfect, caused by mutations in the COPII coatomer complex. In this article, we report a clinically recognizable craniofacial disorder characterized by facial dysmorphisms, severe micrognathia, rhizomelic shortening, microcephalic dwarfism, and mild developmental delay due to loss-of-function heterozygous mutations in ARCN1, which encodes the coatomer subunit delta of COPI. ARCN1 mutant cell lines were revealed to have endoplasmic reticulum stress, suggesting the involvement of ER stress response in the pathogenesis of this disorder. Given that ARCN1 deficiency causes defective type I collagen transport, reduction of collagen secretion represents the likely mechanism underlying the skeletal phenotype that characterizes this condition. Our findings demonstrate the importance of COPI-mediated transport in human development, including skeletogenesis and brain growth.
[Mh] Termos MeSH primário: Complexo I de Proteína do Envoltório/metabolismo
Proteína Coatomer/genética
Anormalidades Craniofaciais/genética
Mutação
[Mh] Termos MeSH secundário: Adulto
Proteína Coatomer/metabolismo
Colágeno/metabolismo
Estresse do Retículo Endoplasmático
Heterozigoto
Seres Humanos
Lactente
Recém-Nascido
Masculino
Síndrome
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coat Protein Complex I); 0 (Coatomer Protein); 9007-34-5 (Collagen)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE


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[PMID]:27472951
[Au] Autor:Wang S; Zhai Y; Pang X; Niu T; Ding YH; Dong MQ; Hsu VW; Sun Z; Sun F
[Ad] Endereço:National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
[Ti] Título:Structural characterization of coatomer in its cytosolic state.
[So] Source:Protein Cell;7(8):586-600, 2016 Aug.
[Is] ISSN:1674-8018
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Studies on coat protein I (COPI) have contributed to a basic understanding of how coat proteins generate vesicles to initiate intracellular transport. The core component of the COPI complex is coatomer, which is a multimeric complex that needs to be recruited from the cytosol to membrane in order to function in membrane bending and cargo sorting. Previous structural studies on the clathrin adaptors have found that membrane recruitment induces a large conformational change in promoting their role in cargo sorting. Here, pursuing negative-stain electron microscopy coupled with single-particle analyses, and also performing CXMS (chemical cross-linking coupled with mass spectrometry) for validation, we have reconstructed the structure of coatomer in its soluble form. When compared to the previously elucidated structure of coatomer in its membrane-bound form we do not observe a large conformational change. Thus, the result uncovers a key difference between how COPI versus clathrin coats are regulated by membrane recruitment.
[Mh] Termos MeSH primário: Proteína Coatomer/química
Citosol/química
Membranas Artificiais
[Mh] Termos MeSH secundário: Fator 1 de Ribosilação do ADP/química
Fator 1 de Ribosilação do ADP/metabolismo
Animais
Proteína Coatomer/metabolismo
Citosol/metabolismo
Proteínas Ativadoras de GTPase/química
Proteínas Ativadoras de GTPase/metabolismo
Seres Humanos
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arfgap1 protein, rat); 0 (Coatomer Protein); 0 (GTPase-Activating Proteins); 0 (Membranes, Artificial); EC 3.6.5.2 (ADP-Ribosylation Factor 1)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160731
[St] Status:MEDLINE
[do] DOI:10.1007/s13238-016-0296-z


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[PMID]:27265324
[Au] Autor:Boot A; Oosting J; de Miranda NF; Zhang Y; Corver WE; van de Water B; Morreau H; van Wezel T
[Ad] Endereço:Department of Pathology, Leiden University Medical Center, Leiden, The Netherlands.
[Ti] Título:Imprinted survival genes preclude loss of heterozygosity of chromosome 7 in cancer cells.
[So] Source:J Pathol;240(1):72-83, 2016 09.
[Is] ISSN:1096-9896
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The genomes of a wide range of cancers, including colon, breast, and thyroid cancers, frequently show copy number gains of chromosome 7 and rarely show loss of heterozygosity. The molecular basis for this phenomenon is unknown. Strikingly, oncocytic follicular thyroid carcinomas can display an extreme genomic profile, with homozygosity of all chromosomes except for chromosome 7. The observation that homozygosity of chromosome 7 is never observed suggests that retention of heterozygosity is essential for cells. We hypothesized that cell survival genes are genetically imprinted on either of two copies of chromosome 7, which thwarts loss of heterozygosity at this chromosome in cancer cells. By employing a DNA methylation screen and gene expression analysis, we identified six imprinted genes that force retention of heterozygosity on chromosome 7. Subsequent knockdown of gene expression showed that CALCR, COPG2, GRB10, KLF14, MEST, and PEG10 were essential for cancer cell survival, resulting in reduced cell proliferation, G1 -phase arrest, and increased apoptosis. We propose that imprinted cell survival genes provide a genetic basis for retention of chromosome 7 heterozygosity in cancer cells. The monoallelically expressed cell survival genes identified in this study, and the cellular pathways that they are involved in, offer new therapeutic targets for the treatment of tumours showing retention of heterozygosity on chromosome 7. Copyright © 2016 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Carcinoma Medular/genética
Sobrevivência Celular/genética
Cromossomos Humanos Par 7
Regulação Neoplásica da Expressão Gênica
Impressão Genômica
Perda de Heterozigosidade
Neoplasias da Glândula Tireoide/genética
[Mh] Termos MeSH secundário: Proteína Semelhante a Receptor de Calcitonina/genética
Carcinoma Medular/patologia
Proliferação Celular/genética
Proteína Coatomer/genética
Metilação de DNA
Proteína Adaptadora GRB10/genética
Seres Humanos
Proteínas/genética
Fatores de Transcrição Sp/genética
Glândula Tireoide/patologia
Neoplasias da Glândula Tireoide/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CALCRL protein, human); 0 (COPG2 protein, human); 0 (Calcitonin Receptor-Like Protein); 0 (Coatomer Protein); 0 (KLF14 protein, human); 0 (PEG10 protein, human); 0 (Proteins); 0 (Sp Transcription Factors); 0 (mesoderm specific transcript protein); 151441-47-3 (GRB10 Adaptor Protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160607
[St] Status:MEDLINE
[do] DOI:10.1002/path.4756


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[PMID]:27232380
[Au] Autor:Kociucka B; Jackowiak H; Kamyczek M; Szydlowski M; Szczerbal I
[Ad] Endereço:Department of Genetics and Animal Breeding, Poznan University of Life Sciences, 60-637 Poznan, Poland.
[Ti] Título:The relationship between adipocyte size and the transcript levels of SNAP23, BSCL2 and COPA genes in pigs.
[So] Source:Meat Sci;121:12-8, 2016 Nov.
[Is] ISSN:1873-4138
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Breed-specific differences in fat tissue accumulation in the pig provide an opportunity to study the genetic background of this process. In the present study three pig breeds, differing in fatness, were analyzed in terms of the size of adipocytes derived from three tissues (subcutaneous, visceral and longissimus dorsi muscle) in relation to transcript levels of genes (SNAP23, BSCL2 and COPA), which encode proteins involved in lipid droplet formation. The analysis of adipocyte size revealed significant effects of breed and tissue and confirmed earlier reports that an elevated backfat thickness in some pig breeds is correlated with a larger adipocyte size. Variability in the transcript abundance of the studied genes among breeds and tissues was observed. We found a positive correlation between the abundance of the SNAP23 transcript and adipocyte diameter. The obtained results indicate that SNAP23 may be considered as an interesting candidate gene involved in adipose tissue growth in the pig.
[Mh] Termos MeSH primário: Adipócitos/citologia
Proteína Coatomer/genética
Subunidades gama da Proteína de Ligação ao GTP/genética
Proteínas Qb-SNARE/genética
Proteínas Qc-SNARE/genética
Suínos/genética
[Mh] Termos MeSH secundário: Tecido Adiposo/metabolismo
Animais
Cruzamento
Tamanho Celular
Proteína Coatomer/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Técnicas de Genotipagem
Modelos Lineares
Músculo Esquelético/metabolismo
Polimorfismo de Nucleotídeo Único
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
Análise de Sequência de DNA
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coatomer Protein); 0 (GTP-Binding Protein gamma Subunits); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160528
[St] Status:MEDLINE



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