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  1 / 9102 MEDLINE  
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[PMID]:29281629
[Au] Autor:Ojeda Naharros I; Gesemann M; Mateos JM; Barmettler G; Forbes A; Ziegler U; Neuhauss SCF; Bachmann-Gagescu R
[Ad] Endereço:Institute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland.
[Ti] Título:Loss-of-function of the ciliopathy protein Cc2d2a disorganizes the vesicle fusion machinery at the periciliary membrane and indirectly affects Rab8-trafficking in zebrafish photoreceptors.
[So] Source:PLoS Genet;13(12):e1007150, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ciliopathies are human disorders caused by dysfunction of primary cilia, ubiquitous organelles involved in transduction of environmental signals such as light sensation in photoreceptors. Concentration of signal detection proteins such as opsins in the ciliary membrane is achieved by RabGTPase-regulated polarized vesicle trafficking and by a selective barrier at the ciliary base, the transition zone (TZ). Dysfunction of the TZ protein CC2D2A causes Joubert/Meckel syndromes in humans and loss of ciliary protein localization in animal models, including opsins in retinal photoreceptors. The link between the TZ and upstream vesicle trafficking has been little explored to date. Moreover, the role of the small GTPase Rab8 in opsin-carrier vesicle (OCV) trafficking has been recently questioned in a mouse model. Using correlative light and electron microscopy and live imaging in zebrafish photoreceptors, we provide the first live characterization of Rab8-mediated trafficking in photoreceptors in vivo. Our results support a possibly redundant role for both Rab8a/b paralogs in OCV trafficking, based on co-localization of Rab8 and opsins in vesicular structures, and joint movement of Rab8-tagged particles with opsin. We further investigate the role of the TZ protein Cc2d2a in Rab8-mediated trafficking using cc2d2a zebrafish mutants and identify a requirement for Cc2d2a in the latest step of OCV trafficking, namely vesicle fusion. Progressive accumulation of opsin-containing vesicles in the apical portion of photoreceptors lacking Cc2d2a is caused by disorganization of the vesicle fusion machinery at the periciliary membrane with mislocalization and loss of the t-SNAREs SNAP25 and Syntaxin3 and of the exocyst component Exoc4. We further observe secondary defects on upstream Rab8-trafficking with cytoplasmic accumulation of Rab8. Taken together, our results support participation of Rab8 in OCV trafficking and identify a novel role for the TZ protein Cc2d2a in fusion of incoming ciliary-directed vesicles, through organization of the vesicle fusion machinery at the periciliary membrane.
[Mh] Termos MeSH primário: Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Transporte Biológico
Movimento Celular
Cílios/genética
Cílios/metabolismo
Seres Humanos
Membranas/metabolismo
Opsinas/genética
Opsinas/metabolismo
Células Fotorreceptoras de Vertebrados/metabolismo
Transporte Proteico
Peixe-Zebra
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CC2D2A protein, zebrafish); 0 (Opsins); 0 (Vesicular Transport Proteins); 0 (Zebrafish Proteins); EC 3.6.1.- (Rab8a protein, zebrafish); EC 3.6.1.-. (RAB8A protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007150


  2 / 9102 MEDLINE  
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[PMID]:29231925
[Au] Autor:Zhang L; Zhang X; Zhang G; Pang CP; Leung YF; Zhang M; Zhong W
[Ad] Endereço:Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907, USA.
[Ti] Título:Expression profiling of the retina of pde6c, a zebrafish model of retinal degeneration.
[So] Source:Sci Data;4:170182, 2017 12 12.
[Is] ISSN:2052-4463
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Retinal degeneration often affects the whole retina even though the disease-causing gene is specifically expressed in the light-sensitive photoreceptors. The molecular basis of the retinal defect can potentially be determined by gene-expression profiling of the whole retina. In this study, we measured the gene-expression profile of retinas microdissected from a zebrafish pde6c (pde6c) mutant. This retinal-degeneration model not only displays cone degeneration caused by a cone-specific mutation, but also other secondary cellular changes starting from 4 days postfertilization (dpf). To capture the underlying molecular changes, we subjected pde6c and wild-type (WT) retinas at 5 dpf/ 120 h postfertilization (hpf) to RNA sequencing (RNA-Seq) on the Illumina HiSeq 2,000 platform. We also validated the RNA-Seq results by Reverse Transcription Quantitative Polymerase Chain Reaction (RT-qPCR) of seven phototransduction genes. Our analyses indicate that the RNA-Seq dataset was of high quality, and effectively captured the molecular changes in the whole pde6c retina. This dataset will facilitate the characterization of the molecular defects in the pde6c retina at the initial stage of retinal degeneration.
[Mh] Termos MeSH primário: Nucleotídeo Cíclico Fosfodiesterase do Tipo 6/genética
Retina/metabolismo
Degeneração Retiniana/genética
Proteínas de Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Animais
Análise em Microsséries
Transcriptoma
Peixe-Zebra
[Pt] Tipo de publicação:DATASET; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Zebrafish Proteins); EC 3.1.4.- (Pde6c protein, zebrafish); EC 3.1.4.35 (Cyclic Nucleotide Phosphodiesterases, Type 6)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1038/sdata.2017.182


  3 / 9102 MEDLINE  
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[PMID]:28449103
[Au] Autor:Li H; Pei W; Vergarajauregui S; Zerfas PM; Raben N; Burgess SM; Puertollano R
[Ad] Endereço:Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
[Ti] Título:Novel degenerative and developmental defects in a zebrafish model of mucolipidosis type IV.
[So] Source:Hum Mol Genet;26(14):2701-2718, 2017 07 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mucolipidosis type IV (MLIV) is a lysosomal storage disease characterized by neurologic and ophthalmologic abnormalities. There is currently no effective treatment. MLIV is caused by mutations in MCOLN1, a lysosomal cation channel from the transient receptor potential (TRP) family. In this study, we used genome editing to knockout the two mcoln1 genes present in Danio rerio (zebrafish). Our model successfully reproduced the retinal and neuromuscular defects observed in MLIV patients, indicating that this model is suitable for studying the disease pathogenesis. Importantly, our model revealed novel insights into the origins and progression of the MLIV pathology, including the contribution of autophagosome accumulation to muscle dystrophy and the role of mcoln1 in embryonic development, hair cell viability and cellular maintenance. The generation of a MLIV model in zebrafish is particularly relevant given the suitability of this organism for large-scale in vivo drug screening, thus providing unprecedented opportunities for therapeutic discovery.
[Mh] Termos MeSH primário: Mucolipidoses/genética
Canais de Receptores Transientes de Potencial/genética
Proteínas de Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Autofagossomos/metabolismo
Modelos Animais de Doenças
Técnicas de Inativação de Genes
Mucolipidoses/metabolismo
Mucolipidoses/patologia
Mutação
Canais de Receptores Transientes de Potencial/metabolismo
Peixe-Zebra
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (MCOLN1.1 protein, zebrafish); 0 (Transient Receptor Potential Channels); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180225
[Lr] Data última revisão:
180225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx158


  4 / 9102 MEDLINE  
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[PMID]:29395088
[Au] Autor:Loganathan K; Moriya S; Parhar IS
[Ad] Endereço:Brain Research Institute, Monash University Malaysia, Jalan Lagoon Selatan, Bandar Sunway, Selangor, 47500, Malaysia.
[Ti] Título:Trek2a regulates gnrh3 expression under control of melatonin receptor Mt1 and α -adrenoceptor.
[So] Source:Biochem Biophys Res Commun;496(3):927-933, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gonadotrophin-releasing hormone (GnRH) expression is associated with the two-pore domain potassium ion (K ) channel-related K (TREK) channel trek2a expression and melatonin levels. We aimed to investigate correlation of trek2a expression with gnrh3 expression, and regulatory mechanisms of trek2a expression by the melatonin receptor Mt1 and α -adrenoceptor which are regulated by melatonin. trek2a specific siRNA, Mt1 antagonist luzindole and α -adrenoceptor antagonist prazosin were administered into the adult zebrafish brain and gene expressions were examined by real-time PCR. trek2a specific siRNA administration significantly reduced expression levels of trek2a, gnrh3 and mt1. Luzindole administration suppressed trek2a and gnrh3 expressions. Prazosin administration reduced trek2a and gnrh3 expressions. It is suggested that Trek2a regulates gnrh3 expression under the control of Mt1 and α -adrenoceptor.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Hormônio Liberador de Gonadotropina/metabolismo
Melatonina/metabolismo
Canais de Potássio de Domínios Poros em Tandem/metabolismo
Ácido Pirrolidonocarboxílico/análogos & derivados
Receptor MT1 de Melatonina/metabolismo
Receptores Adrenérgicos alfa 2/metabolismo
Proteínas de Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Regulação da Expressão Gênica/fisiologia
Masculino
Ácido Pirrolidonocarboxílico/metabolismo
Transdução de Sinais/fisiologia
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (K(2P)10.1 protein, zebrafish); 0 (Potassium Channels, Tandem Pore Domain); 0 (Receptor, Melatonin, MT1); 0 (Receptors, Adrenergic, alpha-2); 0 (Zebrafish Proteins); 0 (gonadotropin-releasing hormone-III); 33515-09-2 (Gonadotropin-Releasing Hormone); JL5DK93RCL (Melatonin); SZB83O1W42 (Pyrrolidonecarboxylic Acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180204
[St] Status:MEDLINE


  5 / 9102 MEDLINE  
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[PMID]:28448962
[Au] Autor:Muñoz-Culla M; Irizar H; Gorostidi A; Alberro A; Osorio-Querejeta I; Ruiz-Martínez J; Olascoaga J; López de Munain A; Otaegui D
[Ad] Endereço:Multiple Sclerosis Group, Biodonostia Health Research institute, San Sebastian, Spain.
[Ti] Título:Progressive changes in non-coding RNA profile in leucocytes with age.
[So] Source:Aging (Albany NY);9(4):1202-1218, 2017 Apr.
[Is] ISSN:1945-4589
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It has been observed that immune cell deterioration occurs in the elderly, as well as a chronic low-grade inflammation called inflammaging. These cellular changes must be driven by numerous changes in gene expression and in fact, both protein-coding and non-coding RNA expression alterations have been observed in peripheral blood mononuclear cells from elder people. In the present work we have studied the expression of small non-coding RNA (microRNA and small nucleolar RNA -snoRNA-) from healthy individuals from 24 to 79 years old. We have observed that the expression of 69 non-coding RNAs (56 microRNAs and 13 snoRNAs) changes progressively with chronological age. According to our results, the age range from 47 to 54 is critical given that it is the period when the expression trend (increasing or decreasing) of age-related small non-coding RNAs is more pronounced. Furthermore, age-related miRNAs regulate genes that are involved in immune, cell cycle and cancer-related processes, which had already been associated to human aging. Therefore, human aging could be studied as a result of progressive molecular changes, and different age ranges should be analysed to cover the whole aging process.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Leucócitos/metabolismo
RNA Longo não Codificante/biossíntese
RNA Longo não Codificante/genética
Proteínas de Peixe-Zebra/biossíntese
Proteínas de Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Simulação por Computador
Feminino
Regulação da Expressão Gênica no Desenvolvimento/genética
Seres Humanos
Masculino
Meia-Idade
RNA Mensageiro/biossíntese
RNA Mensageiro/genética
RNA Nucleolar Pequeno/biossíntese
RNA Nucleolar Pequeno/genética
Transcriptoma
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Long Noncoding); 0 (RNA, Messenger); 0 (RNA, Small Nucleolar); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.18632/aging.101220


  6 / 9102 MEDLINE  
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[PMID]:29293625
[Au] Autor:Kell MJ; Riccio RE; Baumgartner EA; Compton ZJ; Pecorin PJ; Mitchell TA; Topczewski J; LeClair EE
[Ad] Endereço:Department of Pediatrics, Northwestern University Feinberg School of Medicine / Stanley Manne Children's Research Center, Chicago, Illinois, United States of America.
[Ti] Título:Targeted deletion of the zebrafish actin-bundling protein L-plastin (lcp1).
[So] Source:PLoS One;13(1):e0190353, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulation of the cytoskeleton is essential for cell migration in health and disease. Lymphocyte cytosolic protein 1 (lcp1, also called L-plastin) is a hematopoietic-specific actin-bundling protein that is highly conserved in zebrafish, mice and humans. In addition, L-plastin expression is documented as both a genetic marker and a cellular mechanism contributing to the invasiveness of tumors and transformed cell lines. Despite L-plastin's role in both immunity and cancer, in zebrafish there are no direct studies of its function, and no mutant, knockout or reporter lines available. Using CRISPR-Cas9 genome editing, we generated null alleles of zebrafish lcp1 and examined the phenotypes of these fish throughout the life cycle. Our editing strategy used gRNA to target the second exon of lcp1, producing F0 mosaic fish that were outcrossed to wild types to confirm germline transmission. F1 heterozygotes were then sequenced to identify three unique null alleles, here called 'Charlie', 'Foxtrot' and 'Lima'. In silico, each allele truncates the endogenous protein to less than 5% normal size and removes both essential actin-binding domains (ABD1 and ABD2). Although none of the null lines express detectable LCP1 protein, homozygous mutant zebrafish (-/-) can develop and reproduce normally, a finding consistent with that of the L-plastin null mouse (LPL -/-). However, such mice do have a profound immune defect when challenged by lung bacteria. Interestingly, we observed reduced long-term survival of zebrafish lcp1 -/- homozygotes (~30% below the expected numbers) in all three of our knockout lines, with greatest mortality corresponding to the period (4-6 weeks post-fertilization) when the innate immune system is functional, but the adaptive immune system is not yet mature. This suggests that null zebrafish may have reduced capacity to combat opportunistic infections, which are more easily transmissible in the aquatic environment. Overall, our novel mutant lines establish a sound genetic model and an enhanced platform for further studies of L-plastin gene function in hematopoiesis and cancer.
[Mh] Termos MeSH primário: Deleção de Genes
Glicoproteínas de Membrana/genética
Proteínas dos Microfilamentos/genética
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Alelos
Sequência de Aminoácidos
Animais
Clonagem Molecular
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Seres Humanos
Camundongos
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (Microfilament Proteins); 0 (Zebrafish Proteins); 0 (plastin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190353


  7 / 9102 MEDLINE  
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[PMID]:29331378
[Au] Autor:Paone C; Rudeck S; Etard C; Strähle U; Rottbauer W; Just S
[Ad] Endereço:Molecular Cardiology, Department of Inner Medicine II, University of Ulm, Ulm, Germany.
[Ti] Título:Loss of zebrafish Smyd1a interferes with myofibrillar integrity without triggering the misfolded myosin response.
[So] Source:Biochem Biophys Res Commun;496(2):339-345, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sarcomeric protein turnover needs to be tightly balanced to assure proper assembly and renewal of sarcomeric units within muscle tissues. The mechanisms regulating these fundamental processes are only poorly understood, but of great clinical importance since many cardiac and skeletal muscle diseases are associated with defective sarcomeric organization. The SET- and MYND domain containing protein 1b (Smyd1b) is known to play a crucial role in myofibrillogenesis by functionally interacting with the myosin chaperones Unc45b and Hsp90α1. In zebrafish, Smyd1b, Unc45b and Hsp90α1 are part of the misfolded myosin response (MMR), a regulatory transcriptional response that is activated by disturbed myosin homeostasis. Genome duplication in zebrafish led to a second smyd1 gene, termed smyd1a. Morpholino- and CRISPR/Cas9-mediated knockdown of smyd1a led to significant perturbations in sarcomere structure resulting in decreased cardiac as well as skeletal muscle function. Similar to Smyd1b, we found Smyd1a to localize to the sarcomeric M-band in skeletal and cardiac muscles. Overexpression of smyd1a efficiently compensated for the loss of Smyd1b in flatline (fla) mutant zebrafish embryos, rescued the myopathic phenotype and suppressed the MMR in Smyd1b-deficient embryos, suggesting overlapping functions of both Smyd1 paralogs. Interestingly, Smyd1a is not transcriptionally activated in Smyd1b-deficient fla mutants, demonstrating lack of genetic compensation despite the functional redundancy of both zebrafish Smyd1 paralogs.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica no Desenvolvimento
Histona-Lisina N-Metiltransferase/genética
Músculo Esquelético/metabolismo
Miócitos Cardíacos/metabolismo
Miosinas/genética
Sarcômeros/metabolismo
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Sistemas CRISPR-Cas
Embrião não Mamífero
Duplicação Gênica
Edição de Genes
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Proteínas de Choque Térmico HSP90/genética
Proteínas de Choque Térmico HSP90/metabolismo
Histona-Lisina N-Metiltransferase/antagonistas & inibidores
Histona-Lisina N-Metiltransferase/deficiência
Seres Humanos
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Morfolinos/genética
Morfolinos/metabolismo
Músculo Esquelético/patologia
Miócitos Cardíacos/patologia
Miosinas/metabolismo
Dobramento de Proteína
Isoformas de Proteínas/deficiência
Isoformas de Proteínas/genética
Sarcômeros/patologia
Peixe-Zebra/crescimento & desenvolvimento
Peixe-Zebra/metabolismo
Proteínas de Peixe-Zebra/antagonistas & inibidores
Proteínas de Peixe-Zebra/deficiência
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HSP90 Heat-Shock Proteins); 0 (Molecular Chaperones); 0 (Morpholinos); 0 (Protein Isoforms); 0 (Unc45b protein, zebrafish); 0 (Zebrafish Proteins); 147336-22-9 (Green Fluorescent Proteins); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (SmyD1 protein, zebrafish); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180115
[St] Status:MEDLINE


  8 / 9102 MEDLINE  
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[PMID]:29112878
[Au] Autor:Liu G; Ke M; Fan X; Zhang M; Zhu Y; Lu T; Sun L; Qian H
[Ad] Endereço:College of Environment, Zhejiang University of Technology, Hangzhou, 310032, PR China; Department of Food Science and Technology, Zhejiang University of Technology, Hangzhou, 310032, PR China.
[Ti] Título:Reproductive and endocrine-disrupting toxicity of Microcystis aeruginosa in female zebrafish.
[So] Source:Chemosphere;192:289-296, 2018 Feb.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Microcystis aeruginosa, a primary species in cyanobacterial blooms, is ubiquitously distributed in water. Microcystins (MCs) purified from M. aeruginosa can exert reproductive toxicity in fish. However, the effects of M. aeruginosa at environmentally relevant levels on the reproductive and endocrine systems of zebrafish are still unknown. The present study investigated the reproductive and endocrine-disrupting toxicity of M. aeruginosa on female zebrafish (Danio rerio) by short-term exposure (96 h). After exposure, marked histological lesions in the liver or gonads, such as nuclear pyknosis and deformation, were observed, and the fertilization rate and hatchability of eggs spawned from treated females were both significantly lower than they were in females in the control group, suggesting the possibility of transgenerational effects of M. aeruginosa exposure. Moreover, M. aeruginosa exposure decreased the concentration of 17ß-estradiol (E2) and testosterone (T) in female zebrafish. Interestingly, the vtg1 transcriptional level significantly decreased in the liver, whereas plasma vitellogenin (VTG) protein levels increased. The present findings indicate that M. aeruginosa could modulate endocrine function by disrupting transcription of hypothalamic-pituitary-gonadal-liver (HPGL) axis-related genes, and impair the reproductive capacity of female zebrafish, suggesting that M. aeruginosa causes potential adverse effects on fish reproduction in Microcystis bloom-contaminated aquatic environments.
[Mh] Termos MeSH primário: Sistema Endócrino/efeitos dos fármacos
Microcistinas/toxicidade
Microcystis/patogenicidade
Reprodução/efeitos dos fármacos
Peixe-Zebra/microbiologia
[Mh] Termos MeSH secundário: Animais
Toxinas Bacterianas/farmacologia
Disruptores Endócrinos/farmacologia
Estradiol/análise
Estradiol/metabolismo
Feminino
Gônadas/efeitos dos fármacos
Gônadas/metabolismo
Gônadas/patologia
Fígado/efeitos dos fármacos
Fígado/metabolismo
Fígado/patologia
Microcistinas/isolamento & purificação
Microcystis/metabolismo
Testosterona/análise
Testosterona/sangue
Vitelogeninas/sangue
Vitelogeninas/metabolismo
Poluentes Químicos da Água/toxicidade
Peixe-Zebra/metabolismo
Peixe-Zebra/fisiologia
Proteínas de Peixe-Zebra/análise
Proteínas de Peixe-Zebra/efeitos dos fármacos
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Endocrine Disruptors); 0 (Microcystins); 0 (Vitellogenins); 0 (Water Pollutants, Chemical); 0 (Zebrafish Proteins); 3XMK78S47O (Testosterone); 4TI98Z838E (Estradiol); 77238-39-2 (microcystin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171108
[St] Status:MEDLINE


  9 / 9102 MEDLINE  
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[PMID]:28456961
[Au] Autor:Heyn P; Neugebauer KM
[Ad] Endereço:Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307, Dresden, Germany. Patricia.Heyn@igmm.ed.ac.uk.
[Ti] Título:Purification of Zygotically Transcribed RNA through Metabolic Labeling of Early Zebrafish Embryos.
[So] Source:Methods Mol Biol;1605:121-131, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Early embryonic development in all known metazoans is characterized by a transcriptionally silent phase, during which development is under control of maternally loaded protein and RNA. The zygotic genome becomes transcriptionally active after a series of rapid reductive cleavage divisions. In this chapter, we present a method to metabolically label, purify, and analyze newly transcribed RNAs in early zebrafish embryos. We previously used this method, which is adaptable to other embryos and systems, to determine the onset of zygotic transcription activation and identify the first zygotic transcripts.
[Mh] Termos MeSH primário: RNA Mensageiro/análise
Uridina Trifosfato/análogos & derivados
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/embriologia
[Mh] Termos MeSH secundário: Animais
Desenvolvimento Embrionário
Regulação da Expressão Gênica no Desenvolvimento
RNA Mensageiro/química
Ativação Transcricional
Uridina Trifosfato/administração & dosagem
Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Zebrafish Proteins); 31556-28-2 (4-thiouridine triphosphate); UT0S826Z60 (Uridine Triphosphate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6988-3_8


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[PMID]:29326245
[Au] Autor:Rana MS; Kumar P; Lee CJ; Verardi R; Rajashankar KR; Banerjee A
[Ad] Endereço:Cell Biology and Neurobiology Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
[Ti] Título:Fatty acyl recognition and transfer by an integral membrane -acyltransferase.
[So] Source:Science;359(6372), 2018 01 12.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DHHC (Asp-His-His-Cys) palmitoyltransferases are eukaryotic integral membrane enzymes that catalyze protein palmitoylation, which is important in a range of physiological processes, including small guanosine triphosphatase (GTPase) signaling, cell adhesion, and neuronal receptor scaffolding. We present crystal structures of two DHHC palmitoyltransferases and a covalent intermediate mimic. The active site resides at the membrane-cytosol interface, which allows the enzyme to catalyze thioester-exchange chemistry by using fatty acyl-coenzyme A and explains why membrane-proximal cysteines are candidates for palmitoylation. The acyl chain binds in a cavity formed by the transmembrane domain. We propose a mechanism for acyl chain-length selectivity in DHHC enzymes on the basis of cavity mutants with preferences for shorter and longer acyl chains.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Aciltransferases/química
Proteínas de Peixe-Zebra/química
[Mh] Termos MeSH secundário: Aciltransferases/genética
Aciltransferases/metabolismo
Animais
Domínio Catalítico
Cristalização
Cristalografia por Raios X
Cisteína/química
Seres Humanos
Lipoilação
Modelos Moleculares
Mutação
Domínios Proteicos
Estrutura Secundária de Proteína
Especificidade por Substrato
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Zebrafish Proteins); EC 2.3.- (Acyltransferases); EC 2.3.- (ZDHHC20 protein, human); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE



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