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Pesquisa : D12.776.306.366 [Categoria DeCS]
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  1 / 5014 MEDLINE  
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[PMID]:29253022
[Au] Autor:Ha S; Kim I; Takata T; Kinouchi T; Isoyama M; Suzuki M; Fujii N
[Ad] Endereço:Graduate School of Science, Kyoto University, Kyoto, Japan.
[Ti] Título:Identification of á´…-amino acid-containing peptides in human serum.
[So] Source:PLoS One;12(12):e0189972, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biologically uncommon d-aspartate (d-Asp) residues have been shown to accumulate in proteins associated with age-related human disorders, such as cataract and Alzheimer disease. Such d-Asp-containing proteins are unlikely to be broken down completely because metabolic enzymes recognize only proteins or peptides composed exclusively of l-amino acids. Therefore, undigested d-Asp-containing peptides may exist in blood and, if detectable, may be a useful biomarker for associated diseases. In this study, we investigated d-amino acid-containing peptides in adult human serum by a qualitative d-amino acid analysis based on a diastereomer method and LC-MS/MS method. As a result, two d-Asp-containing peptides were detected in serum, both derived from the fibrinogen ß-chain, a glycoprotein that helps in the formation of blood clots. One of the peptides was fibrinopeptide B, which prevents fibrinogen from forming polymers of fibrin, and the other was same peptide with C-terminal Arginine missing. To our knowledge, this is the first report of the presence of d-amino acid-containing peptides in serum and the approach described will provide a new direction on the serum proteome and fragmentome.
[Mh] Termos MeSH primário: Aminoácidos/sangue
Peptídeos/sangue
[Mh] Termos MeSH secundário: Adulto
Doença de Alzheimer/sangue
Aminoácidos/química
Ácido Aspártico/metabolismo
Biomarcadores/sangue
Catarata/sangue
Cromatografia Líquida
Cristalinas/metabolismo
Fibrinogênio/metabolismo
Fibrinopeptídeo B/análise
Seres Humanos
Meia-Idade
Proteômica
Espectrometria de Massas em Tandem
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Biomarkers); 0 (Crystallins); 0 (Peptides); 30KYC7MIAI (Aspartic Acid); 36204-23-6 (Fibrinopeptide B); 9001-32-5 (Fibrinogen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189972


  2 / 5014 MEDLINE  
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[PMID]:28458505
[Au] Autor:Wang E; Geng A; Seo R; Maniar A; Gong X
[Ad] Endereço:School of Optometry and Vision Science Program, University of California, Berkeley, Berkeley, CA.
[Ti] Título:Knock-in of Cx46 partially rescues fiber defects in lenses lacking Cx50.
[So] Source:Mol Vis;23:160-170, 2017.
[Is] ISSN:1090-0535
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Connexins 46 (Cx46) and 50 (Cx50) support lens development and homeostasis. Knockout (KO) of Cx50, but not Cx46, causes defects in lens fiber organization, F-actin enrichment, gap junction (GJ) size, ball-and-socket (BS) maturation, and GJ-associated protein distributions. To further determine the unique roles of Cx50 and Cx46, we investigated whether these defects persisted in Cx46 knock-in (Ki) lenses. Ki mice had Cx46 knocked-in to their Cx50 loci, where it was expressed under endogenous Cx50 promoters. METHODS: Fiber cell morphology and the distribution of lens membrane/cytoskeleton proteins from wild-type (WT), Ki, and Cx50 KO mice were visualized by immunofluorescent labeling and confocal microscopy. RESULTS: Cx46 Ki partially rescued Cx50 KO lens fiber defects. Three-week-old Ki lens fibers had typical F-actin distributions but were nonuniformly sized and disorganized. The Cx-associated proteins zonula occludens-1 (ZO-1) and ß-dystroglycan (ßDys) no longer localized to the nuclei but remained absent from GJs. BS formed, but this occurred with lower than WT frequency. BS appeared with greater frequency in 8-week-old Ki lenses, but so did aberrant balloon-like structures similar to those in Cx50 KO lenses. Unexpectedly, 8-week-old Cx50 KO and Ki cortical lens fibers were no longer disorganized. CONCLUSIONS: Cx identity is important for some aspects of fiber development (organization, Cx association with ZO-1 and ßDys) but not others (F-actin enrichment). Either Cx supports BS maturation, but the sparsity of BS and presence of balloon-like structures in Ki lenses suggest that Cx50 is more capable of doing so. The partial rescue of BS structures may support the rapid growth of cortical fibers to the improved growth of Ki lenses compared to Cx50 KO lenses at young ages. Neither absence of Cx50 nor presence of Ki Cx46 affects cortical fiber cell organization by the age of 8 weeks.
[Mh] Termos MeSH primário: Conexinas/genética
Conexinas/fisiologia
Cristalinas/fisiologia
Técnicas de Introdução de Genes
Técnicas de Inativação de Genes
Cristalino/citologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Envelhecimento/fisiologia
Animais
Citoesqueleto/metabolismo
Distroglicanas/metabolismo
Técnica Indireta de Fluorescência para Anticorpo
Junções Comunicantes/metabolismo
Cristalino/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microscopia Confocal
Proteína da Zônula de Oclusão-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Connexins); 0 (Crystallins); 0 (Tjp1 protein, mouse); 0 (Zonula Occludens-1 Protein); 0 (connexin 46); 0 (connexin 50); 146888-27-9 (Dystroglycans)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  3 / 5014 MEDLINE  
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[PMID]:29258460
[Au] Autor:Kohmoto R; Kobayashi T; Sato T; Kimura D; Fukumoto M; Tajiri K; Kida T; Ikeda T
[Ad] Endereço:Department of Ophthalmology, Osaka Medical College, 2-7 Daigaku-machi, Takatsuki City, Osaka, 569-8686, Japan.
[Ti] Título:A case of proliferative diabetic retinopathy in which scintillating particles appeared in the intravitreal cavity after laser photocoagulation.
[So] Source:BMC Ophthalmol;17(1):254, 2017 Dec 19.
[Is] ISSN:1471-2415
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: To report a case of proliferative diabetic retinopathy (PDR) exhibiting the appearance of scintillating particles presumed to be crystallin inside the intravitreal cavity after laser photocoagulation. CASE PRESENTATION: A 56-year-old male patient presented at our outpatient clinic after becoming aware of decreased vision in his right eye. Ocular examination performed at the patient's initial visit revealed a massive preretinal macular hemorrhage due to PDR in his right eye. Fundus fluorescein angiography revealed extensive retinal non-perfusion areas and neovascularization in both eyes. However, no opacity was observed in the intravitreal cavity of his left eye. Vitreous surgery was performed on the patient's right eye after ultrasonic phacoemulsification aspiration and intraocular lens implantation. Post surgery, the corrected VA in that eye improved from 0.1 to 1.0. In correlation with the treatment performed on the patient's right eye, we began panretinal photocoagulation on his left eye. Examination performed prior to the patient's third session of panretinal photocoagulation revealed a large number of scintillating particles in the posterior vitreous gel in front of the retina. Examination via slit-lamp microscopy revealed that the particles were of varied hues, and closely resembled a 'Christmas tree' cataract. No posterior vitreous detachment was observed, and since these particles were situated as if captured in the posterior vitreous gel, no eye-movement-associated mobility of the particles was observed. Since the cloudiness was not severe enough to interfere with photocoagulation, additional photocoagulation was performed, and the patient is currently under observation. Six months have now passed since the fourth photocoagulation procedure was performed, and there has been no change in the state of the particles. Optical coherence tomography imaging revealed no change before and after the panretinal photocoagulation. The corrected VA in his left eye has remained at 1.0 during the postoperative follow-up period. CONCLUSIONS: We speculate that the production of crystallin in the retina in this case was triggered by the photocoagulation procedure performed for diabetic retinopathy.
[Mh] Termos MeSH primário: Cristalinas/metabolismo
Retinopatia Diabética/cirurgia
Fotocoagulação a Laser/efeitos adversos
Corpo Vítreo/patologia
[Mh] Termos MeSH secundário: Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crystallins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1186/s12886-017-0654-5


  4 / 5014 MEDLINE  
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[PMID]:28747635
[Au] Autor:Haffner MC; Esopi DM; Chaux A; Gürel M; Ghosh S; Vaghasia AM; Tsai H; Kim K; Castagna N; Lam H; Hicks J; Wyhs N; Biswal Shinohara D; Hurley PJ; Simons BW; Schaeffer EM; Lotan TL; Isaacs WB; Netto GJ; De Marzo AM; Nelson WG; An SS; Yegnasubramanian S
[Ad] Endereço:Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University, Baltimore, MD, USA.
[Ti] Título:AIM1 is an actin-binding protein that suppresses cell migration and micrometastatic dissemination.
[So] Source:Nat Commun;8(1):142, 2017 07 26.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A defining hallmark of primary and metastatic cancers is the migration and invasion of malignant cells. These invasive properties involve altered dynamics of the cytoskeleton and one of its major structural components ß-actin. Here we identify AIM1 (absent in melanoma 1) as an actin-binding protein that suppresses pro-invasive properties in benign prostate epithelium. Depletion of AIM1 in prostate epithelial cells increases cytoskeletal remodeling, intracellular traction forces, cell migration and invasion, and anchorage-independent growth. In addition, decreased AIM1 expression results in increased metastatic dissemination in vivo. AIM1 strongly associates with the actin cytoskeleton in prostate epithelial cells in normal tissues, but not in prostate cancers. In addition to a mislocalization of AIM1 from the actin cytoskeleton in invasive cancers, advanced prostate cancers often harbor AIM1 deletion and reduced expression. These findings implicate AIM1 as a key suppressor of invasive phenotypes that becomes dysregulated in primary and metastatic prostate cancer.Invasion of malignant cells involves changes in cytoskeleton dynamics. Here the authors identify absent in melanoma 1 as an actin binding protein and show that it regulates cytoskeletal remodeling and cell migration in prostate epithelial cells, acting as a metastatic suppressor in cancer cells.
[Mh] Termos MeSH primário: Actinas/metabolismo
Movimento Celular
Cristalinas/metabolismo
Proteínas de Membrana/metabolismo
Neoplasias da Próstata/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Actinas/genética
Animais
Linhagem Celular
Linhagem Celular Tumoral
Cristalinas/genética
Células HEK293
Seres Humanos
Masculino
Proteínas de Membrana/genética
Camundongos
Microscopia Eletrônica de Transmissão
Microscopia de Fluorescência
Invasividade Neoplásica
Micrometástase de Neoplasia
Neoplasias da Próstata/genética
Neoplasias da Próstata/ultraestrutura
Ligação Proteica
Interferência de RNA
Transplante Heterólogo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AIM1 protein, human); 0 (Actins); 0 (Crystallins); 0 (Membrane Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00084-8


  5 / 5014 MEDLINE  
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[PMID]:28755661
[Au] Autor:Zhao Z; Fan Q; Zhou P; Ye H; Cai L; Lu Y
[Ad] Endereço:Department of Ophthalmology, Eye and ENT Hospital of Fudan University, 83 Fenyang Road, Shanghai, 200031, People's Republic of China.
[Ti] Título:Association of alpha A-crystallin polymorphisms with susceptibility to nuclear age-related cataract in a Han Chinese population.
[So] Source:BMC Ophthalmol;17(1):133, 2017 Jul 29.
[Is] ISSN:1471-2415
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Alpha A-crystallin (CRYAA) is considered critical for the maintenance of lens transparency and is related to the pathogenesis of age-related cataracts (ARCs), especially the nuclear subtype. As the 5' untranslated region (5' UTR) modulates gene expression, the purpose of current study was to investigate whether single nucleotide polymorphisms (SNPs) in the 5' UTR of CRYAA were associated with susceptibility to ARC in a Han Chinese population and to clarify the mechanism of this association. METHODS: SNPs in the 5' UTR (-1 to -1000) of CRYAA were identified in 243 nuclear ARC patients and 263 controls using polymerase chain reaction and DNA sequencing. Allele and genotype frequencies were calculated and compared between two groups. Haploview 4.2 was used to calculate the linkage disequilibrium index, and the SHEsis analysis platform was used to infer haplotype construction. A dual-luciferase reporter gene assay was used for transcription of CRYAA in the presence of a protective haplotype with individual SNP alteration, Chromatin immunoprecipitation (ChIP) was employed to determine whether SNPs regulated CRYAA expression by altering the binding affinity of transcription factors. RESULTS: Three polymorphisms were identified in the 5' UTR of CRYAA: rs3761381 (P = 0.000357, odds ratio [OR] = 1.837), rs13053109 (P = 0.788, OR = 1.086), and rs7278468 (P = 0.00136, OR = 0.652). The haplotype C-G-T (P = 0.0014, OR = 1.536) increased the risk of nuclear ARC, whereas the haplotype T-G-G (P = 0.00029, OR = 0.535) decreased the risk. The haplotype C-G-T decreased CRYAA transcription through rs7278468, which is located in the binding site of specificity protein 1 (Sp1). Furthermore, the G allele of rs7278468 increased CRYAA transcription by enhancing the binding affinity of Sp1. CONCLUSIONS: These data indicate that the CRYAA polymorphism is a genetic marker of inter-individual differences in the risk of nuclear ARC.
[Mh] Termos MeSH primário: Catarata/genética
Cristalinas/genética
DNA/genética
Grupos Étnicos
Predisposição Genética para Doença
Cristalino/metabolismo
Polimorfismo de Nucleotídeo Único
[Mh] Termos MeSH secundário: Idoso
Alelos
Catarata/etnologia
Catarata/metabolismo
Células Cultivadas
China/epidemiologia
Cristalinas/metabolismo
Feminino
Frequência do Gene
Genótipo
Haplótipos
Seres Humanos
Incidência
Cristalino/patologia
Masculino
Razão de Chances
Reação em Cadeia da Polimerase
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRYAA protein, human); 0 (Crystallins); 9007-49-2 (DNA)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170731
[St] Status:MEDLINE
[do] DOI:10.1186/s12886-017-0529-9


  6 / 5014 MEDLINE  
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[PMID]:28655832
[Au] Autor:McLendon PM; Davis G; Gulick J; Singh SR; Xu N; Salomonis N; Molkentin JD; Robbins J
[Ad] Endereço:From the Division of Molecular Cardiovascular Biology, Heart Institute, Cincinnati Children's Hospital Medical Center, OH (P.M.M., G.D., J.G., S.R.S., N.X., J.D.M., J.R.); Division of Biomedical Informatics, Cincinnati Children's Hospital, OH (N.S.); and UES, Inc, Dayton, OH (P.M.M.).
[Ti] Título:An Unbiased High-Throughput Screen to Identify Novel Effectors That Impact on Cardiomyocyte Aggregate Levels.
[So] Source:Circ Res;121(6):604-616, 2017 Sep 01.
[Is] ISSN:1524-4571
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RATIONALE: Postmitotic cells, such as cardiomyocytes, seem to be particularly susceptible to proteotoxic stimuli, and large, proteinaceous deposits are characteristic of the desmin-related cardiomyopathies and crystallin cardiomyopathic diseases. Increased activity of protein clearance pathways in the cardiomyocyte, such as proteasomal degradation and autophagy, has proven to be beneficial in maintaining cellular and cardiac function in the face of multiple proteotoxic insults, holding open the possibility of targeting these processes for the development of effective therapeutics. OBJECTIVE: Here, we undertake an unbiased, total genome screen for RNA transcripts and their protein products that affect aggregate accumulations in the cardiomyocytes. METHODS AND RESULTS: Primary mouse cardiomyocytes that accumulate aggregates as a result of a mutant CryAB (αB-crystallin) causative for human desmin-related cardiomyopathy were used for a total genome-wide screen to identify gene products that affected aggregate formation. We infected cardiomyocytes using a short hairpin RNA lentivirus library in which the mouse genome was represented. The screen identified multiple candidates in many cell signaling pathways that were able to mediate significant decreases in aggregate levels. CONCLUSIONS: Subsequent validation of one of these candidates, Jak1 (Janus kinase 1), a tyrosine kinase of the nonreceptor type, confirmed the usefulness of this approach in identifying previously unsuspected players in proteotoxic processes.
[Mh] Termos MeSH primário: Cardiomiopatias/genética
Clonagem Molecular/métodos
Cristalinas/genética
Desmina/genética
Ensaios de Triagem em Larga Escala/métodos
Miócitos Cardíacos/metabolismo
Transcriptoma
[Mh] Termos MeSH secundário: Animais
Agregação Celular/genética
Células Cultivadas
Janus Quinase 1/genética
Janus Quinase 1/metabolismo
Camundongos
Miócitos Cardíacos/fisiologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crystallins); 0 (Desmin); EC 2.7.10.2 (Janus Kinase 1)
[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:170629
[St] Status:MEDLINE
[do] DOI:10.1161/CIRCRESAHA.117.310945


  7 / 5014 MEDLINE  
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[PMID]:28640093
[Au] Autor:Cui XJ; Lv FY; Li FH; Zeng K
[Ad] Endereço:aDepartment of Ophthalmology, Linyi People's Hospital bDepartment of Infectious Diseases, Affiliated Hospital of Shandong Medical College, Linyi cShenzhen Key Laboratory of Ophthalmology, Shenzhen Eye Hospital, Shenzhen, P.R. China.
[Ti] Título:Correlations of single nucleotide polymorphisms of CRYAA and CRYAB genes with the risk and clinicopathological features of children suffering from congenital cataract.
[So] Source:Medicine (Baltimore);96(25):e7158, 2017 Jun.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The study aims to explore the correlations of the single nucleotide polymorphisms (SNPs) of CRYAA and CRYAB with the risk and clinicopathological features of children with congenital cataract. METHODS: The study enrolled 168 children diagnosed as congenital cataract (case group) and 172 normal children (control group) from May 2015 to May 2016. Genomic DNA extraction was performed using a QIAamp DNA blood mini kit. Polymerase chain reaction (PCR) products were genotyped using an ABI direct sequencer. Haplotype, allele, and genotype frequencies of CRYAA and CRYAB gene polymorphisms analyses were carried out using the SHEsis software. Logistic regression analysis was performed in order to analyze the risk factors for children suffering from congenital cataract. RESULTS: Presence of significant differences between the case and control groups' genotype and allele frequencies of CRYAA rs7278468 and CRYAB rs370803064/rs387907338. TA of CRYAB gene might increase congenital cataract risk in children, while GCG of CRYAA gene and GC of CRYAB gene might decrease congenital cataract risk in children. CRYAA rs7278468, CRYAB rs370803064/rs387907338 polymorphisms were significantly correlated to uncorrected visual acuity, best-corrected visual acuity, nystagmus, visual axis opacification, microcornea, lens opacity, posterior capsular thickening, and degrees of posterior capsule opacification after operation in children with congenital cataract. Logistic regression analysis revealed that the T allele of CRYAA rs7278468, A allele of CRYAB rs370803064, T allele of CRYAB rs387907338, family history, and TA haplotype of CRYAB gene were risk factors for children with congenital cataract. CONCLUSION: Our findings demonstrated that CRYAA rs7278468 and CRYAB rs370803064/rs387907338 are correlated with the risk and clinicopathological features of children suffering from congenital cataract.
[Mh] Termos MeSH primário: Catarata/genética
Cristalinas/genética
Predisposição Genética para Doença
Polimorfismo de Nucleotídeo Único
Cadeia B de alfa-Cristalina/genética
[Mh] Termos MeSH secundário: Catarata/patologia
Catarata/fisiopatologia
Extração de Catarata
Pré-Escolar
Feminino
Frequência do Gene
Técnicas de Genotipagem
Haplótipos
Seres Humanos
Modelos Logísticos
Masculino
Reação em Cadeia da Polimerase
Software
Resultado do Tratamento
Acuidade Visual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRYAA protein, human); 0 (CRYAB protein, human); 0 (Crystallins); 0 (alpha-Crystallin B Chain)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000007158


  8 / 5014 MEDLINE  
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[PMID]:28525556
[Au] Autor:Whitson JA; Zhang X; Medvedovic M; Chen J; Wei Z; Monnier VM; Fan X
[Ad] Endereço:Department of Pathology, Case Western Reserve University, Cleveland, Ohio, United States.
[Ti] Título:Transcriptome of the GSH-Depleted Lens Reveals Changes in Detoxification and EMT Signaling Genes, Transport Systems, and Lipid Homeostasis.
[So] Source:Invest Ophthalmol Vis Sci;58(5):2666-2684, 2017 May 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: To understand the effects of glutathione (GSH)-deficiency on genetic processes that regulate lens homeostasis and prevent cataractogenesis. Methods: The transcriptome of lens epithelia and fiber cells was obtained from C57BL/6 LEGSKO (lens GSH-synthesis knockout) and buthionine sulfoximine (BSO)-treated LEGSKO mice and compared to C57BL/6 wild-type mice using RNA-Seq. Transcriptomic data were confirmed by qPCR and Western blot/ELISA on a subset of genes. Results: RNA-Seq results were in excellent agreement with qPCR (correlation coefficients 0.87-0.94 and P < 5E-6 for a subset of 36 mRNAs). Of 24,415 transcripts mapped to the mouse genome, 441 genes showed significantly modulated expression. Pathway analysis indicated major changes in epithelial-mesenchymal transition (EMT) signaling, visual cycle, small molecule biochemistry, and lipid metabolism. GSH-deficient lenses showed upregulation of detoxification genes, including Aldh1a1, Aldh3a1 (aldehyde dehydrogenases), Mt1, Mt2 (metallothioneins), Ces1g (carboxylesterase), and Slc14a1 (urea transporter UT-B). Genes in canonical EMT pathways, including Wnt10a, showed upregulation in lens epithelia samples. Severely GSH-deficient lens epithelia showed downregulation of vision-related genes (including crystallins). The BSO-treated LEGSKO lens epithelia transcriptome has significant correlation (r = 0.63, P < 0.005) to that of lens epithelia undergoing EMT. Protein expression data correlated with transcriptomic data and confirmed EMT signaling activation. Conclusions: These results show that GSH-deficiency in the lens leads to expression of detoxifying genes and activation of EMT signaling, in addition to changes in transport systems and lipid homeostasis. These data provide insight into the adaptation and consequences of GSH-deficiency in the lens and suggest that GSH plays an important role in lenticular EMT pathology.
[Mh] Termos MeSH primário: Transição Epitelial-Mesenquimal/genética
Glutationa/fisiologia
Cristalino/metabolismo
Metabolismo dos Lipídeos/fisiologia
Proteínas de Membrana Transportadoras/genética
Desentoxicação Metabólica Fase I/genética
Transcriptoma
[Mh] Termos MeSH secundário: Animais
Western Blotting
Butionina Sulfoximina/farmacologia
Cristalinas/genética
Inibidores Enzimáticos/farmacologia
Ensaio de Imunoadsorção Enzimática
Glutationa/deficiência
Homeostase
Cristalino/efeitos dos fármacos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crystallins); 0 (Enzyme Inhibitors); 0 (Membrane Transport Proteins); 0 (RNA, Messenger); 5072-26-4 (Buthionine Sulfoximine); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.16-21398


  9 / 5014 MEDLINE  
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[PMID]:28477155
[Au] Autor:Stahl AL; Charlton-Perkins M; Buschbeck EK; Cook TA
[Ad] Endereço:Department of Biological Sciences, University of Cincinnati, Cincinnati, OH, 45221, USA.
[Ti] Título:The cuticular nature of corneal lenses in Drosophila melanogaster.
[So] Source:Dev Genes Evol;227(4):271-278, 2017 Jul.
[Is] ISSN:1432-041X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The dioptric visual system relies on precisely focusing lenses that project light onto a neural retina. While the proteins that constitute the lenses of many vertebrates are relatively well characterized, less is known about the proteins that constitute invertebrate lenses, especially the lens facets in insect compound eyes. To address this question, we used mass spectrophotometry to define the major proteins that comprise the corneal lenses from the adult Drosophila melanogaster compound eye. This led to the identification of four cuticular proteins: two previously identified lens proteins, drosocrystallin and retinin, and two newly identified proteins, Cpr66D and Cpr72Ec. To determine which ommatidial cells contribute each of these proteins to the lens, we conducted in situ hybridization at 50% pupal development, a key age for lens secretion. Our results confirm previous reports that drosocrystallin and retinin are expressed in the two primary corneagenous cells-cone cells and primary pigment cells. Cpr72Ec and Cpr66D, on the other hand, are more highly expressed in higher order interommatidial pigment cells. These data suggest that the complementary expression of cuticular proteins give rise to the center vs periphery of the corneal lens facet, possibly facilitating a refractive gradient that is known to reduce spherical aberration. Moreover, these studies provide a framework for future studies aimed at understanding the cuticular basis of corneal lens function in holometabolous insect eyes.
[Mh] Termos MeSH primário: Cristalinas/análise
Proteínas de Drosophila/análise
Drosophila melanogaster/química
Drosophila melanogaster/genética
[Mh] Termos MeSH secundário: Animais
Olho Composto de Artrópodes/química
Córnea/química
Cristalinas/genética
Proteínas de Drosophila/química
Proteínas de Drosophila/genética
Drosophila melanogaster/citologia
Drosophila melanogaster/crescimento & desenvolvimento
Evolução Molecular
Proteínas do Olho/genética
Regulação da Expressão Gênica
Hibridização In Situ
Cristalino/química
Espectrometria de Massas
Pupa/química
Pupa/citologia
Pupa/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crystallins); 0 (Drosophila Proteins); 0 (Eye Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170903
[Lr] Data última revisão:
170903
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170507
[St] Status:MEDLINE
[do] DOI:10.1007/s00427-017-0582-7


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[PMID]:28411463
[Au] Autor:Wang CH; Huang CC; Chen W
[Ad] Endereço:Department of Applied Chemistry, National Chiayi University, 300 University Road, Chiayi 60083, Taiwan.
[Ti] Título:Simultaneous separation of taxon-specific crystallins from Mule duck and characterization of their enzymatic activities and structures.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1053:34-41, 2017 May 15.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Methods to obtain pure proteins in large amounts are indispensible in protein research. We report here a large-scale/simultaneous isolation of taxon-specific crystallins (É›- and δ-crystallin) from the eye lenses of Mule duck. We also investigate the compositions, enzymatic activities, and structures of these purified taxon-specific proteins. A relatively mild method of ion-exchange chromatography was developed to fractionate É›-crystallin and δ-crystallin in large amount, ca. ∼6.60mg/g-lens and ∼41.0mg/g-lens, respectively. Both crystallins were identified by electrophoresis, HPLC, and MALDI-TOF-MS. É›-Crystallin, with native composition of M 142kDa, consisted of two subunits of 35kDa and 36kDa, while δ-Crystallin, with native molecular mass of 200kDa, comprised single subunit of M ∼50kDa. Both É›- and δ-crystallin were tetramers. The former showed lactate dehydrogenase (LDH) activity, while the latter appeared slightly active in an argininosuccinate lyase (ASL) assay. Raman spectroscopic results indicated that the secondary structures of É›- and δ-crystallin were predominantly α-helix as evidenced by the vibrational stretching of amide III over 1260cm and amide I at 1255cm , in greatly contrast to the anti-parallel ß-sheet of α- and ß-crystallin as demonstrated by amide III at 1238cm and amide I at 1672cm . The microenvironments of aromatic amino acids and the status of thiol groups also vary in different crystallins. The compositions, enzyme activities, and structures of the É›- and δ-crystalline of Mule duck are different from those of Muscovy duck (Cairina moschata) or Kaiya duck (Anas Platyrhynchos var. domestica), which reflect faithfully species specificity.
[Mh] Termos MeSH primário: Proteínas Aviárias/química
Cromatografia por Troca Iônica/métodos
Cristalinas/química
Patos/metabolismo
Cristalino/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas Aviárias/isolamento & purificação
Proteínas Aviárias/metabolismo
Cromatografia Líquida de Alta Pressão/métodos
Cristalinas/isolamento & purificação
Cristalinas/metabolismo
Patos/classificação
Cristalino/enzimologia
Cristalino/metabolismo
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Especificidade da Espécie
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
Análise Espectral Raman/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Avian Proteins); 0 (Crystallins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170416
[St] Status:MEDLINE



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