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Pesquisa : A09.371.060.500 [Categoria DeCS]
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  1 / 19295 MEDLINE  
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[PMID]:28465175
[Au] Autor:Malik A; Albogami S; Alsenaidy AM; Aldbass AM; Alsenaidy MA; Khan ST
[Ad] Endereço:Department of Biochemistry. Protein Research Chair. College of Science. King Saud University, PO Box 2455, Riyadh 11451, Saudi Arabia. Electronic address: amalik@ksu.edu.sa.
[Ti] Título:Spectral and thermal properties of novel eye lens ζ-crystallin.
[So] Source:Int J Biol Macromol;102:1052-1058, 2017 Sep.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Eye lenses are exposed to thermal, solar radiations, dryness that enhances cataractogenesis. Some animal lenses contain novel proteins in bulk quantities. ζ-crystallin occurred in three ecologically divergent species, but it's physiological role not known. The truncated variant of ζ-crystallin causes hereditary cataract. Guinea pig ζ-crystallin is temperature-sensitive and rapidly aggregates at 41°C. Camels adopted to survive above 50°C, which raises an interesting question about how it retains lens proteins in the soluble state? Here, we have optimized expression and purification of recombinant camel ζ-crystallin. We have studied thermodynamic and spectroscopic properties using orthogonal techniques. Dynamic multimode spectroscopy results showed that camel ζ-crystallin unfolds via single transition with T value of 60.8±0.1°C and van't Hoff enthalpy of 714.7±7.1kJ/mol. Thermal-shift assay calculates T value of 62°C at pH 7. Additionally, the conformational stability of ζ-crystallin increases with ionic-strength. The influence of pH on ζ-crystallin was evaluated where the protein was found to be stable in the pH range of 6-9, but its stability drastically decreases below pH 6. Our results also showed that quaternary structure of ζ-crystallin drastically changed as a result of lowering pH. This study provides significant understandings onto the conformational, thermodynamic and unfolding pathway of camel ζ-crystallin.
[Mh] Termos MeSH primário: Cristalino/química
Temperatura Ambiente
zeta-Cristalinas/química
[Mh] Termos MeSH secundário: Concentração de Íons de Hidrogênio
Estabilidade Proteica
Desdobramento de Proteína
Análise Espectral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (zeta-Crystallins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  2 / 19295 MEDLINE  
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[PMID]:29338044
[Au] Autor:Andley UP; Tycksen E; McGlasson-Naumann BN; Hamilton PD
[Ad] Endereço:Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, Missouri, United States of America.
[Ti] Título:Probing the changes in gene expression due to α-crystallin mutations in mouse models of hereditary human cataract.
[So] Source:PLoS One;13(1):e0190817, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mammalian eye lens expresses a high concentration of crystallins (α, ß and γ-crystallins) to maintain the refractive index essential for lens transparency. Crystallins are long-lived proteins that do not turnover throughout life. The structural destabilization of crystallins by UV exposure, glycation, oxidative stress and mutations in crystallin genes leads to protein aggregation and development of cataracts. Several destabilizing mutations in crystallin genes are linked with human autosomal dominant hereditary cataracts. To investigate the mechanism by which the α-crystallin mutations Cryaa-R49C and Cryab-R120G lead to cataract formation, we determined whether these mutations cause an altered expression of specific transcripts in the lens at an early postnatal age by RNA-seq analysis. Using knock-in mouse models previously generated in our laboratory, in the present work, we identified genes that exhibited altered abundance in the mutant lenses, including decreased transcripts for Clic5, an intracellular water channel in Cryaa-R49C heterozygous mutant lenses, and increased transcripts for Eno1b in Cryab-R120G heterozygous mutant lenses. In addition, RNA-seq analysis revealed increased histones H2B, H2A, and H4 gene expression in Cryaa-R49C mutant lenses, suggesting that the αA-crystallin mutation regulates histone expression via a transcriptional mechanism. Additionally, these studies confirmed the increased expression of histones H2B, H2A, and H4 by proteomic analysis of Cryaa-R49C knock-in and Cryaa;Cryab gene knockout lenses reported previously. Taken together, these findings offer additional insight into the early transcriptional changes caused by Cryaa and Cryab mutations associated with autosomal dominant human cataracts, and indicate that the transcript levels of certain genes are affected by the expression of mutant α-crystallin in vivo.
[Mh] Termos MeSH primário: Catarata/genética
Mutação
Cadeia A de alfa-Cristalina/genética
Cadeia B de alfa-Cristalina/genética
[Mh] Termos MeSH secundário: Animais
Carboxipeptidases/genética
Carboxipeptidases/metabolismo
Catarata/metabolismo
Canais de Cloreto/genética
Canais de Cloreto/metabolismo
Modelos Animais de Doenças
Expressão Gênica
Técnicas de Introdução de Genes
Histonas/genética
Histonas/metabolismo
Seres Humanos
Cristalino/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Mutantes
Camundongos Transgênicos
Proteínas/genética
Proteínas/metabolismo
Proteômica
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Cadeia A de alfa-Cristalina/metabolismo
Cadeia B de alfa-Cristalina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Aebp1 protein, mouse); 0 (CLIC5 protein, mouse); 0 (Chloride Channels); 0 (Cryab protein, mouse); 0 (Histones); 0 (Proteins); 0 (Repressor Proteins); 0 (alpha-Crystallin A Chain); 0 (alpha-Crystallin B Chain); 0 (vig1 protein, mouse); EC 3.4.- (Carboxypeptidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190817


  3 / 19295 MEDLINE  
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[PMID]:29267365
[Au] Autor:Bennett TM; M'Hamdi O; Hejtmancik JF; Shiels A
[Ad] Endereço:Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, Missouri, United States of America.
[Ti] Título:Germ-line and somatic EPHA2 coding variants in lens aging and cataract.
[So] Source:PLoS One;12(12):e0189881, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rare germ-line mutations in the coding regions of the human EPHA2 gene (EPHA2) have been associated with inherited forms of pediatric cataract, whereas, frequent, non-coding, single nucleotide variants (SNVs) have been associated with age-related cataract. Here we sought to determine if germ-line EPHA2 coding SNVs were associated with age-related cataract in a case-control DNA panel (> 50 years) and if somatic EPHA2 coding SNVs were associated with lens aging and/or cataract in a post-mortem lens DNA panel (> 48 years). Micro-fluidic PCR amplification followed by targeted amplicon (exon) next-generation (deep) sequencing of EPHA2 (17-exons) afforded high read-depth coverage (1000x) for > 82% of reads in the cataract case-control panel (161 cases, 64 controls) and > 70% of reads in the post-mortem lens panel (35 clear lens pairs, 22 cataract lens pairs). Novel and reference (known) missense SNVs in EPHA2 that were predicted in silico to be functionally damaging were found in both cases and controls from the age-related cataract panel at variant allele frequencies (VAFs) consistent with germ-line transmission (VAF > 20%). Similarly, both novel and reference missense SNVs in EPHA2 were found in the post-mortem lens panel at VAFs consistent with a somatic origin (VAF > 3%). The majority of SNVs found in the cataract case-control panel and post-mortem lens panel were transitions and many occurred at di-pyrimidine sites that are susceptible to ultraviolet (UV) radiation induced mutation. These data suggest that novel germ-line (blood) and somatic (lens) coding SNVs in EPHA2 that are predicted to be functionally deleterious occur in adults over 50 years of age. However, both types of EPHA2 coding variants were present at comparable levels in individuals with or without age-related cataract making simple genotype-phenotype correlations inconclusive.
[Mh] Termos MeSH primário: Catarata/genética
Mutação em Linhagem Germinativa
Cristalino/fisiologia
Polimorfismo de Nucleotídeo Único
Receptor EphA2/genética
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Envelhecimento
Estudos de Casos e Controles
Feminino
Seres Humanos
Masculino
Meia-Idade
Mudanças Depois da Morte
Proteína Supressora de Tumor p53/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Tumor Suppressor Protein p53); EC 2.7.10.1 (Receptor, EphA2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189881


  4 / 19295 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


  5 / 19295 MEDLINE  
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[PMID]:29258473
[Au] Autor:Wu X; Liu Z; Zhang X; Wang D; Long E; Wang J; Li W; Lai W; Cao Q; Hu K; Chen W; Lin H; Liu Y
[Ad] Endereço:State Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Center, Sun Yat-sen University, 54# Xianlie Road, Guangzhou, Guangdong, 510060, China.
[Ti] Título:Proteomics analysis and proteogenomic characterization of different physiopathological human lenses.
[So] Source:BMC Ophthalmol;17(1):253, 2017 Dec 19.
[Is] ISSN:1471-2415
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The aim of the present study was to identify the proteomic differences among human lenses in different physiopathological states and to screen for susceptibility genes/proteins via proteogenomic characterization. METHODS: The total proteomes identified across the regenerative lens with secondary cataract (RLSC), congenital cataract (CC) and age-related cataract (ARC) groups were compared to those of normal lenses using isobaric tagging for relative and absolute protein quantification (iTRAQ). The up-regulated proteins between the groups were subjected to biological analysis. Whole exome sequencing (WES) was performed to detect genetic variations. RESULTS: The most complete human lens proteome to date, which consisted of 1251 proteins, including 55.2% previously unreported proteins, was identified across the experimental groups. Bioinformatics functional annotation revealed the common involvement of cellular metabolic processes, immune responses and protein folding disturbances among the groups. RLSC-over-expressed proteins were characteristically enriched in the intracellular immunological signal transduction pathways. The CC groups featured biological processes relating to gene expression and vascular endothelial growth factor (VEGF) signaling transduction, whereas the molecular functions corresponding to external stress were specific to the ARC groups. Combined with WES, the proteogenomic characterization narrowed the list to 16 candidate causal molecules. CONCLUSIONS: These findings revealed common final pathways with diverse upstream regulation of cataractogenesis in different physiopathological states. This proteogenomic characterization shows translational potential for detecting susceptibility genes/proteins in precision medicine.
[Mh] Termos MeSH primário: Catarata/metabolismo
Proteínas do Olho/metabolismo
Cristalino/metabolismo
Proteoma/análise
[Mh] Termos MeSH secundário: Adulto
Pré-Escolar
Cromatografia Líquida
Feminino
Seres Humanos
Masculino
Meia-Idade
Proteogenômica
Proteoma/genética
Proteômica
Espectrometria de Massas em Tandem
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eye Proteins); 0 (Proteome)
[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/s12886-017-0642-9


  6 / 19295 MEDLINE  
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[PMID]:29208844
[Au] Autor:Bawankar P; Das D; Agarwal B; Bhattacharjee K; Tayab S; Deka P; Singh A; Borah E; Dhar S
[Ad] Endereço:Department of ophthalmology, Sri Sankaradeva Nethralaya, Guwahati, India.
[Ti] Título:A rare case of traumatic subretinal migration of crystalline lens, corroborated histologically.
[So] Source:Indian J Ophthalmol;65(12):1495-1497, 2017 Dec.
[Is] ISSN:1998-3689
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:Blunt trauma is the most common cause of posterior dislocation of the crystalline lens. We describe a rare case of subretinal migration of crystalline lens through the giant retinal tear following blunt ocular trauma. This incidental finding of subretinal dislocation of lens following blunt ocular trauma was confirmed on histopathological examination of the enucleated eye. This complication has not been described by histopathological examination in literature so far.
[Mh] Termos MeSH primário: Traumatismos Oculares/complicações
Subluxação do Cristalino/etiologia
Cristalino/patologia
Ferimentos não Penetrantes/complicações
[Mh] Termos MeSH secundário: Adulto
Traumatismos Oculares/diagnóstico
Traumatismos Oculares/cirurgia
Seres Humanos
Subluxação do Cristalino/diagnóstico
Subluxação do Cristalino/cirurgia
Cristalino/lesões
Masculino
Procedimentos Cirúrgicos Oftalmológicos/métodos
Doenças Raras
Perfurações Retinianas/diagnóstico
Perfurações Retinianas/etiologia
Perfurações Retinianas/cirurgia
Ferimentos não Penetrantes/diagnóstico
Ferimentos não Penetrantes/cirurgia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.4103/ijo.IJO_613_17


  7 / 19295 MEDLINE  
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[PMID]:29208825
[Au] Autor:Narang P; Agarwal A
[Ad] Endereço:Narang Eye Care and Laser Centre, Ahmedabad, Gujarat, India.
[Ti] Título:Spatula scaffold: An iris-sparing technique for lensectomy.
[So] Source:Indian J Ophthalmol;65(12):1419-1421, 2017 Dec.
[Is] ISSN:1998-3689
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:Lensectomy with vitrectomy is often performed for crystalline lenticular subluxation. We report a new technique and a practical approach that involves the placement of a spatula beneath the iris tissue that facilitates retroiridial removal of subluxated lens and acts as a scaffold by protecting the iris tissue from being accidentally trapped into the vitrectomy cutter port. Our technique facilitates management of the lens and vitreous without any trauma to the iris and secondarily obviates the need to perform an iris repair procedure that may arise due to iatrogenic reasons.
[Mh] Termos MeSH primário: Iris/cirurgia
Subluxação do Cristalino/cirurgia
Cristalino/cirurgia
Tecidos Suporte
Vitrectomia/métodos
[Mh] Termos MeSH secundário: Seres Humanos
Acuidade Visual
[Pt] Tipo de publicação:JOURNAL ARTICLE; TECHNICAL REPORT; VIDEO-AUDIO MEDIA
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.4103/ijo.IJO_601_17


  8 / 19295 MEDLINE  
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[PMID]:29260191
[Au] Autor:Wu HD; Howse LA; Vaghefi E
[Ad] Endereço:School of Optometry and Vision Sciences, University of Auckland, New Zealand.
[Ti] Título:Effect of Age-Related Human Lens Sutures Growth on Its Fluid Dynamics.
[So] Source:Invest Ophthalmol Vis Sci;58(14):6351-6357, 2017 Dec 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: Age-related nuclear cataract is the opacification of the clear ocular lens due to oxidative damage as we age, and is the leading cause of blindness in the world. A lack of antioxidant supply to the core of ever-growing ocular lens could contribute to the cause of this condition. In this project, a computational model was developed to study the sutural fluid inflow of the aging human lens. Methods: Three different SOLIDWORKS computational fluid dynamics models of the human lens (7 years old; 28 years old; 46 years old) were created, based on available literature data. The fluid dynamics of the lens sutures were modelled using the Stokes flow equations, combined with realistic physiological boundary conditions and embedded in COMSOL Multiphysics. Results: The flow rate, volume, and flow rate per volume of fluid entering the aging lens were examined, and all increased over the 40 years modelled. However, while the volume of the lens grew by ∼300% and the flow rate increased by ∼400%, the flow rate per volume increased only by very moderate ∼38%. Conclusions: Here, sutural information from humans of 7 to 46 years of age was obtained. In this modelled age range, an increase of flow rate per volume was observed, albeit at very slow rate. We hypothesize that with even further increasing age (60+ years old), the lens volume growth would outpace its flow rate increases, which would eventually lead to malnutrition of the lens nucleus and onset of cataracts.
[Mh] Termos MeSH primário: Envelhecimento/fisiologia
Catarata/fisiopatologia
Hidrodinâmica
Cristalino/fisiopatologia
[Mh] Termos MeSH secundário: Adulto
Criança
Feminino
Seres Humanos
Masculino
Meia-Idade
Modelos Teóricos
Estresse Oxidativo/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22099


  9 / 19295 MEDLINE  
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[PMID]:29228915
[Au] Autor:Suwan Y; Jiamsawad S; Tantraworasin A; Geyman L; Supakontanasan W; Teekhasaenee C
[Ad] Endereço:From the Department of Ophthalmology, Faculty of Medicine, Ramathibodi Hospital, Mahidol University, Bangkok, Thailand.
[Ti] Título:Qualitative and quantitative evaluation of acute angle-closure mechanisms.
[So] Source:BMC Ophthalmol;17(1):246, 2017 Dec 11.
[Is] ISSN:1471-2415
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: To evaluate ocular biometric parameters in different subtypes of acute angle closure and compared to fellow eyes of AAC and PACS eyes. METHODS: This is a retrospective chart review study. A total of 167 eyes (96 patients) consisting of 71 AAC eyes, 71 fellow eyes of AAC, and 25 PACS eyes were recruited. All patients underwent ocular examination and biometry. The mechanism of AAC was confirmed by ultrasound biomicroscopy. We then subdivided AAC eyes into four subgroups: crowded-angle (CR), lens subluxation (LS) pupillary block (PB), and plateau iris syndrome (PL). Outcome variables included anterior chamber depth (ACD), lens thickness (LT), vitreal length (VL), axial length (AL), lens position and relative lens position (LP and RLP, respectively), and lens axial length factor (LAF). RESULTS: Among the three groups, ACD was shallower in AAC eyes than fellow eyes of AAC and PACS eyes (p < 0.01 for both) and AAC eyes demonstrated a lesser LP and RLP. The LT, VL, AL, and LAF were not significantly different among the three groups. Among the four subgroups, LS displayed the most shallow ACD (p = 0.01). The lens position in PL was greater than in CR and LS (p < 0.05 and <0.01, respectively). CONCLUSIONS: AAC eyes had a more anterior lens position than fellow eyes and PACS eyes, though lens thickness did not differ among the groups. As such, an anterior lens position may offer more sensitive prognostication regarding future development of AAC compared to lens thickness.
[Mh] Termos MeSH primário: Glaucoma de Ângulo Fechado/patologia
[Mh] Termos MeSH secundário: Idoso
Análise de Variância
Câmara Anterior/diagnóstico por imagem
Comprimento Axial do Olho/diagnóstico por imagem
Biometria/métodos
Feminino
Glaucoma de Ângulo Fechado/diagnóstico por imagem
Seres Humanos
Cristalino/diagnóstico por imagem
Masculino
Meia-Idade
Estudos Retrospectivos
Corpo Vítreo/diagnóstico por imagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1186/s12886-017-0635-8


  10 / 19295 MEDLINE  
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[PMID]:29196765
[Au] Autor:Kumari S; Gao J; Mathias RT; Sun X; Eswaramoorthy A; Browne N; Zhang N; Varadaraj K
[Ad] Endereço:Department of Physiology and Biophysics, Stony Brook University, Stony Brook, New York, United States.
[Ti] Título:Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.
[So] Source:Invest Ophthalmol Vis Sci;58(14):6006-6019, 2017 Dec 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: The objective of this study was to understand the molecular and physiologic mechanisms behind the lens cataract differences in Aquaporin 0-knockout-Heterozygous (AQP0-Htz) mice developed in C57 and FVB (lacks beaded filaments [BFs]) strains. Methods: Lens transparency was studied using dark field light microscopy. Water permeability (Pf) was measured in fiber cell membrane vesicles. Western blotting/immunostaining was performed to verify expression of BF proteins and connexins. Microelectrode-based intact lens intracellular impedance was measured to determine gap junction (GJ) coupling resistance. Lens intracellular hydrostatic pressure (HP) was determined using a microelectrode/manometer system. Results: Lens opacity and spherical aberration were more distinct in AQP0-Htz lenses from FVB than C57 strains. In either background, compared to wild type (WT), AQP0-Htz lenses showed decreased Pf (approximately 50%), which was restored by transgenic expression of AQP1 (TgAQP1/AQP0-Htz), but the opacities and differences between FVB and C57 persisted. Western blotting revealed no change in connexin expression levels. However, in C57 AQP0-Htz and TgAQP1/AQP0-Htz lenses, GJ coupling resistance decreased approximately 2.8-fold and the HP gradient decreased approximately 1.9-fold. Increased Pf in TgAQP1/AQP0-Htz did not alter GJ coupling resistance or HP. Conclusions: In C57 AQP0-Htz lenses, GJ coupling resistance decreased. HP reduction was smaller than the coupling resistance reduction, a reflection of an increase in fluid circulation, which is one reason for the less severe cataract in C57 than FVB. Overall, our results suggest that AQP0 modulates GJs in the presence of BF proteins to maintain lens transparency and homeostasis.
[Mh] Termos MeSH primário: Aquaporina 1/genética
Catarata/genética
Proteínas do Olho/genética
Regulação da Expressão Gênica
Proteínas de Filamentos Intermediários/genética
Cristalino/metabolismo
RNA/genética
[Mh] Termos MeSH secundário: Animais
Aquaporina 1/biossíntese
Western Blotting
Catarata/metabolismo
Catarata/patologia
Modelos Animais de Doenças
Impedância Elétrica
Proteínas do Olho/biossíntese
Junções Comunicantes/genética
Junções Comunicantes/metabolismo
Genótipo
Heterozigoto
Proteínas de Filamentos Intermediários/biossíntese
Cristalino/patologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microeletrodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp1 protein, mouse); 0 (Eye Proteins); 0 (Intermediate Filament Proteins); 0 (filensin); 146410-94-8 (Aquaporin 1); 63231-63-0 (RNA)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22153



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