Base de dados : MEDLINE
Pesquisa : D12.776.306.366.300.200 [Categoria DeCS]
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[PMID]:28384305
[Au] Autor:Anders F; Teister J; Liu A; Funke S; Grus FH; Thanos S; von Pein HD; Pfeiffer N; Prokosch V
[Ad] Endereço:Experimental and Translational Ophthalmology, Department of Ophthalmology, University Medical Center of the Johannes Gutenberg-University Mainz, Mainz, Germany.
[Ti] Título:Intravitreal injection of ß-crystallin B2 improves retinal ganglion cell survival in an experimental animal model of glaucoma.
[So] Source:PLoS One;12(4):e0175451, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose of this study was to investigate firstly specific proteomic changes within the retina in the course of an animal glaucoma model and to identify secondly new approaches for neuroprotective, therapeutic options in glaucoma by addressing those specific changes. Intraocular pressure was elevated through cauterization of episcleral veins in adult Sprague Dawley rats. Molecular and morphological changes were surveyed using mass spectrometry, optical coherence tomography as well as immunohistochemical cross section- and flat mount stainings. By quantifying more than 1500 retinal proteins, it was found that the HspB5 protein and numerous beta-crystallins showed a uniform and unique shifting expression pattern as a result of different periods of elevated IOP exposure. Crystallins showed a significant downregulation (p<0.05) after 3 weeks of elevated IOP and an upregulation after 7 weeks. Counteracting those typical changes, an intravitreal injection of ß-crystallin B2 at the time of IOP elevation was found to reduce retinal ganglion cell loss (p<0.05), decrease of the retinal nerve fiber layer (p<0.05) and impairment of the optic nerve. Ultimately, proteomic data revealed that ß-crystallin B2 might influence calcium-depended cell signaling pathways with severe effect on apoptosis and gene regulation. In this context especially annexin A5, calcium-transporting ATPase 1 and various histone proteins seem to play a major role.
[Mh] Termos MeSH primário: Modelos Animais de Doenças
Glaucoma/patologia
Células Ganglionares da Retina/efeitos dos fármacos
Cadeia B de beta-Cristalina/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Sobrevivência Celular/efeitos dos fármacos
Glaucoma/fisiopatologia
Pressão Intraocular
Injeções Intravítreas
Masculino
Ratos
Células Ganglionares da Retina/patologia
Cadeia B de beta-Cristalina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Crystallin B Chain); 0 (beta-crystallin B2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175451


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[PMID]:28272538
[Au] Autor:Siggs OM; Javadiyan S; Sharma S; Souzeau E; Lower KM; Taranath DA; Black J; Pater J; Willoughby JG; Burdon KP; Craig JE
[Ad] Endereço:Department of Ophthalmology, Flinders University, Flinders Medical Centre, Bedford Park, South Australia, Australia.
[Ti] Título:Partial duplication of the CRYBB1-CRYBA4 locus is associated with autosomal dominant congenital cataract.
[So] Source:Eur J Hum Genet;25(6):711-718, 2017 Jun.
[Is] ISSN:1476-5438
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Congenital cataract is a rare but severe paediatric visual impediment, often caused by variants in one of several crystallin genes that produce the bulk of structural proteins in the lens. Here we describe a pedigree with autosomal dominant isolated congenital cataract and linkage to the crystallin gene cluster on chromosome 22. No rare single nucleotide variants or short indels were identified by exome sequencing, yet copy number variant analysis revealed a duplication spanning both CRYBB1 and CRYBA4. While the CRYBA4 duplication was complete, the CRYBB1 duplication was not, with the duplicated CRYBB1 product predicted to create a gain of function allele. This association suggests a new genetic mechanism for the development of isolated congenital cataract.
[Mh] Termos MeSH primário: Catarata/genética
Oftalmopatias Hereditárias/genética
Duplicação Gênica
Cadeia A de beta-Cristalina/genética
Cadeia B de beta-Cristalina/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Catarata/patologia
Criança
Pré-Escolar
Cromossomos Humanos Par 22/genética
Variações do Número de Cópias de DNA
Oftalmopatias Hereditárias/patologia
Feminino
Seres Humanos
Masculino
Meia-Idade
Linhagem
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRYBA4 protein, human); 0 (CRYBB1 protein, human); 0 (beta-Crystallin A Chain); 0 (beta-Crystallin B Chain)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1038/ejhg.2017.33


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[PMID]:28238532
[Au] Autor:Xi Z; Whitley MJ; Gronenborn AM
[Ad] Endereço:Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA.
[Ti] Título:Human ßB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.
[So] Source:Structure;25(3):496-505, 2017 Mar 07.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ßγ-Crystallins are long-lived eye lens proteins that are crucial for lens transparency and refractive power. Each ßγ-crystallin comprises two homologous domains, which are connected by a short linker. γ-Crystallins are monomeric, while ß-crystallins crystallize as dimers and multimers. In the crystal, human ßB2-crystallin is a domain-swapped dimer while the N-terminally truncated ßB1-crystallin forms a face-en-face dimer. Combining and integrating data from multi-angle light scattering, nuclear magnetic resonance, and small-angle X-ray scattering of full-length and terminally truncated human ßB2-crystallin in solution, we show that both these ßB2-crystallin proteins are dimeric, possess C2 symmetry, and are more compact than domain-swapped dimers. Importantly, no inter-molecular paramagnetic relaxation enhancement effects compatible with domain swapping were detected. Our collective experimental results unambiguously demonstrate that, in solution, human ßB2-crystallin is not domain swapped and exhibits a face-en-face dimer structure similar to the crystal structure of truncated ßB1-crystallin.
[Mh] Termos MeSH primário: Cadeia B de beta-Cristalina/química
Cadeia B de beta-Cristalina/genética
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Multimerização Proteica
Estrutura Quaternária de Proteína
Espalhamento a Baixo Ângulo
Deleção de Sequência
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Crystallin B Chain); 0 (beta-crystallin B2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170823
[Lr] Data última revisão:
170823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170228
[St] Status:MEDLINE


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[PMID]:28131617
[Au] Autor:Dulle JE; Rübsam A; Garnai SJ; Pawar HS; Fort PE
[Ad] Endereço:Department of Ophthalmology and Visual Sciences, University of Michigan, Ann Arbor, MI, USA.
[Ti] Título:BetaB2-crystallin mutations associated with cataract and glaucoma leads to mitochondrial alterations in lens epithelial cells and retinal neurons.
[So] Source:Exp Eye Res;155:85-90, 2017 Feb.
[Is] ISSN:1096-0007
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Crystallin proteins are the most prominent protein of the lens and have been increasingly shown to play critical roles in other tissues, especially the retina. Members of all 3 sub-families of crystallins, alpha-, beta- and gamma-crystallins have been reported in the retina during diabetes, traumatic injury and other retinal diseases. While their specific role in the retina is still unclear and may vary, beta-crystallin proteins have been shown to play a critical role in ganglion cell survival following trauma. We recently reported the correlation between a gene conversion in the betaB2-crystallin gene and a phenotype of familial congenital cataract. Interestingly, in half of the patients, this phenotype was associated with glaucoma. Taken together, these data suggested that the mutations we recently reported could have an impact on the role of betaB2-crystallin in both lens epithelial cells and retinal neurons. Consistent with this hypothesis, we show in the current study that the gene conversion leading to an amino acid conversion lead to a loss of solubility and a change of subcellular localization of betaB2-crystallin in both cell types. While the overall observations were similar in both cell types, there were some important nuances between them, suggesting different roles and regulation of betaB2-crystallin in lens cells versus retinal neurons. The data reported in this study strongly support a significant role of betaB2-crystallin in both lenticular and retinal ocular tissues and warrant further analysis of its regulation and its impact not only in cataract formation but also in retinal neurodegenerative diseases.
[Mh] Termos MeSH primário: Catarata/genética
DNA/genética
Glaucoma/genética
Cristalino/metabolismo
Mutação
Neurônios Retinianos/metabolismo
Cadeia B de beta-Cristalina/genética
[Mh] Termos MeSH secundário: Animais
Catarata/metabolismo
Catarata/patologia
Análise Mutacional de DNA
Células Epiteliais/metabolismo
Células Epiteliais/patologia
Glaucoma/metabolismo
Glaucoma/patologia
Seres Humanos
Fenótipo
Neurônios Retinianos/patologia
Cadeia B de beta-Cristalina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Crystallin B Chain); 0 (beta-crystallin B2); 9007-49-2 (DNA)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170130
[St] Status:MEDLINE


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[PMID]:26593886
[Au] Autor:Graw J
[Ad] Endereço:Helmholtz Zentrum München, Institute of Developmental Genetics, Ingolstaedter Landstr, 1, D-85764 Neuherberg, Germany. Electronic address: graw@helmholtz-muenchen.de.
[Ti] Título:From eyeless to neurological diseases.
[So] Source:Exp Eye Res;156:5-9, 2017 Mar.
[Is] ISSN:1096-0007
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Age-related cataracts are frequently associated with degenerative changes in the ocular lens including the aggregation of proteins - mainly crystallins, but also other proteins including amyloids (Aß) leading to the hypothesis that cataracts could be used as "biomarkers" for Alzheimer disease. Even if this hypothesis was rejected by David Beebe's last paper (Bei et al., Exp. Eye Res., 2015), it is a fascinating aspect to look for commonalities between eye diseases and neurological disorders. In this review, I discuss such commonalities between eye and brain mainly from a developmental point of view. The finding of the functional homology of the Drosophila eyeless gene with the mammalian Pax6 gene marks a first highlight in the developmental genetics of the eye - this result destroyed the "dogma" of the different evolutionary routes of eye development in flies and mammals. The second highlight was the finding that Pax6 is also involved in the development of the forebrain supporting the pleiotropic role of many genes. These findings opened a new avenue for research showing that a broad variety of transcription factors, but also structural proteins are involved both, in eye and brain development as well as into the maintenance of the functional integrity of the corresponding tissue(s). In this review recent findings are summarized demonstrating that genes whose mutations have been identified first to be causative for congenital or juvenile eye disorders are also involved in regenerative processes and neurogenesis (Pax6), but also in neurodegenerative diseases like Parkinson (e.g. Pitx3) or in neurological disorders like Schizophrenia (e.g. Crybb1, Crybb2).
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/genética
Proteínas de Drosophila/genética
Oftalmopatias/genética
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Doenças do Sistema Nervoso/genética
[Mh] Termos MeSH secundário: Animais
Drosophila melanogaster
Proteínas de Homeodomínio/genética
Seres Humanos
Mutação
Fator de Transcrição PAX6/genética
Fatores de Transcrição/genética
Cadeia B de beta-Cristalina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (CRYBB1 protein, human); 0 (DNA-Binding Proteins); 0 (Drosophila Proteins); 0 (Homeodomain Proteins); 0 (PAX6 Transcription Factor); 0 (PAX6 protein, human); 0 (Transcription Factors); 0 (beta-Crystallin B Chain); 0 (beta-crystallin B2); 0 (eyeless protein, Drosophila); 0 (homeobox protein PITX3)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170721
[Lr] Data última revisão:
170721
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151124
[St] Status:MEDLINE


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[PMID]:28120589
[Au] Autor:Mohebi M; Akbari A; Babaei N; Sadeghi A; Heidari M
[Ad] Endereço:Farabi Eye Research Center, Farabi Eye Hospital, Tehran University of Medical Sciences, Tehran, Iran.
[Ti] Título:Identification of a De Novo 3bp Deletion in CRYBA1/A3 Gene in Autosomal Dominant Congenital Cataract.
[So] Source:Acta Med Iran;54(12):778-783, 2016 Dec.
[Is] ISSN:1735-9694
[Cp] País de publicação:Iran
[La] Idioma:eng
[Ab] Resumo:Autosomal dominant congenital cataract (ADCC) is the most common form of inherited cataracts and accounts for one-third of congenital cataracts. Heterozygous null mutations in the crystallin genes are the major cause of the ADCC. This study aims to detect the mutational spectrum of four crystallin genes, CRYBA1/A3, CRYBB1, CRYBB2 and CRYGD in an Iranian family. Genomic DNA was isolated from whole blood cells from theproband and other family members. The coding regions and flanking intronicsequences of crystalline genes were analyzed by Sanger sequencing in aproband with ADCC. The identified mutation was further evaluated in available family members. To predict the potential protein partners of CRYBA1/A3, we also used an in-silico analysis. A de novo heterozygous deletion (c.272-274delGAG, p.G91del) in exon 4 of CRYBA1/A3 gene, leading to a deletion of Glycine at codon 91 was found. This genetic variation did not change the reading frame of CRYBA1 protein. In conclusion, we identified a de novo in-frame 3-bp deletion in the proband with an autosomal dominant congenital cataract, but not in her parents, in an Iranian family. This mutation has occurred de novo on a paternal gamete during spermatogenesis. The in-silico results predicted the interaction of CRYBA1 protein with the other CRY as well as proteins responsible for eye cell signaling.
[Mh] Termos MeSH primário: Catarata/genética
Genes Dominantes/genética
Linhagem
Deleção de Sequência/genética
Cadeia A de beta-Cristalina/genética
[Mh] Termos MeSH secundário: Adulto
Grupo com Ancestrais do Continente Asiático/genética
Sequência de Bases
Catarata/sangue
Criança
Códon/genética
Análise Mutacional de DNA
Feminino
Variação Genética
Glicina/genética
Seres Humanos
Irã (Geográfico)
Masculino
Dados de Sequência Molecular
Mutação
Pais
Análise de Sequência de DNA/métodos
Cadeia A de beta-Cristalina/sangue
Cadeia B de beta-Cristalina/sangue
Cadeia B de beta-Cristalina/genética
gama-Cristalinas/sangue
gama-Cristalinas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRYBA1 protein, human); 0 (CRYBB1 protein, human); 0 (CRYGD protein, human); 0 (Codon); 0 (beta-Crystallin A Chain); 0 (beta-Crystallin B Chain); 0 (beta-crystallin B2); 0 (gamma-Crystallins); TE7660XO1C (Glycine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170126
[St] Status:MEDLINE


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[PMID]:27666820
[Au] Autor:Gao Q; Ren H; Chen M; Niu Z; Tao H; Jia Y; Zhang J; Li W
[Ad] Endereço:Department of Laboratory Diagnosis, Changhai Hospital, The Second Military Medical University, Shanghai 200433, P.R. China.
[Ti] Título:Long non-coding RNAs regulate effects of ß-crystallin B2 on mouse ovary development.
[So] Source:Mol Med Rep;14(5):4223-4231, 2016 Nov.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:ß-crystallin B2 (CRYBB2) knockout mice exhibit morphological and functional abnormalities in the ovary. Long non­coding RNAs (lncRNAs) regulate gene transcription and translation, and epigenetic modification of genomic DNA. The present study investigated the role of lncRNAs in mediating the effects of CRYBB2 in the regulation of ovary development in mice. In the current study, ovary tissues from wild­type (WT) and CRYBB2 knockout mice were subjected to lncRNA and mRNA microarray profiling. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses were performed to group the differentially expressed lncRNAs into regulated gene pathways and functions. The correlation matrix method was used to establish a network of lncRNA and mRNA co­expression. Quantitative reverse transcription-polymerase chain reaction (RT­qPCR) was used to verify expression of a number of these differentially expressed lncRNAs and mRNAs. There were 157 differentially expressed lncRNAs and 1,085 differentially expressed mRNAs between ovary tissues from WT and CRYBB2 knockout mice. The GO and KEGG analyses indicated that these differentially expressed lncRNAs and mRNAs were important in Ca2+ signaling and ligand and receptor interactions. The correlation matrix method established an lncRNA and mRNA co­expression network, consisting of 53 lncRNAs and 45 mRNAs with 98 nodes and 75 connections. RT­qPCR confirmed downregulation of lncRNA A­30­P01019163 expression, which further downregulated its downstream gene purinergic receptor P2X, ligand­gated ion channel, 7 (P2rx7) expression in ovary tissues from CRYBB2 knockout mice. In conclusion, CRYBB2 regulates expression of different lncRNAs to influence ovary development. lncRNA A­30­P01019163 may affect ovarian cell cycle and proliferation by regulating P2rx7 expression in the ovary.
[Mh] Termos MeSH primário: Ovário/metabolismo
RNA Longo não Codificante/genética
Receptores Purinérgicos P2X7/genética
Cadeia B de beta-Cristalina/biossíntese
[Mh] Termos MeSH secundário: Animais
Feminino
Perfilação da Expressão Gênica
Regulação da Expressão Gênica no Desenvolvimento
Redes Reguladoras de Genes/genética
Camundongos
Análise de Sequência com Séries de Oligonucleotídeos
Ovário/crescimento & desenvolvimento
RNA Longo não Codificante/biossíntese
RNA Mensageiro/biossíntese
RNA Mensageiro/genética
Receptores Purinérgicos P2X7/biossíntese
Transdução de Sinais
Cadeia B de beta-Cristalina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Long Noncoding); 0 (RNA, Messenger); 0 (Receptors, Purinergic P2X7); 0 (beta-Crystallin B Chain); 0 (beta-crystallin B2)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170410
[Lr] Data última revisão:
170410
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160927
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2016.5761


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[PMID]:27326458
[Au] Autor:Jiao X; Kabir F; Irum B; Khan AO; Wang Q; Li D; Khan AA; Husnain T; Akram J; Riazuddin S; Hejtmancik JF; Riazuddin SA
[Ad] Endereço:Ophthalmic Genetics and Visual Function Branch, National Eye Institute, National Institutes of Health, Bethesda, MD, 20892, United States of America.
[Ti] Título:A Common Ancestral Mutation in CRYBB3 Identified in Multiple Consanguineous Families with Congenital Cataracts.
[So] Source:PLoS One;11(6):e0157005, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: This study was performed to investigate the genetic determinants of autosomal recessive congenital cataracts in large consanguineous families. METHODS: Affected individuals underwent a detailed ophthalmological examination and slit-lamp photographs of the cataractous lenses were obtained. An aliquot of blood was collected from all participating family members and genomic DNA was extracted from white blood cells. Initially, a genome-wide scan was performed with genomic DNAs of family PKCC025 followed by exclusion analysis of our familial cohort of congenital cataracts. Protein-coding exons of CRYBB1, CRYBB2, CRYBB3, and CRYBA4 were sequenced bidirectionally. A haplotype was constructed with SNPs flanking the causal mutation for affected individuals in all four families, while the probability that the four familial cases have a common founder was estimated using EM and CHM-based algorithms. The expression of Crybb3 in the developing murine lens was investigated using TaqMan assays. RESULTS: The clinical and ophthalmological examinations suggested that all affected individuals had nuclear cataracts. Genome-wide linkage analysis localized the causal phenotype in family PKCC025 to chromosome 22q with statistically significant two-point logarithm of odds (LOD) scores. Subsequently, we localized three additional families, PKCC063, PKCC131, and PKCC168 to chromosome 22q. Bidirectional Sanger sequencing identified a missense variation: c.493G>C (p.Gly165Arg) in CRYBB3 that segregated with the disease phenotype in all four familial cases. This variation was not found in ethnically matched control chromosomes, the NHLBI exome variant server, or the 1000 Genomes or dbSNP databases. Interestingly, all four families harbor a unique disease haplotype that strongly suggests a common founder of the causal mutation (p<1.64E-10). We observed expression of Crybb3 in the mouse lens as early as embryonic day 15 (E15), and expression remained relatively steady throughout development. CONCLUSION: Here, we report a common ancestral mutation in CRYBB3 associated with autosomal recessive congenital cataracts identified in four familial cases of Pakistani origin.
[Mh] Termos MeSH primário: Catarata/congênito
Catarata/genética
Consanguinidade
Mutação/genética
Cadeia B de beta-Cristalina/genética
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Cromossomos Humanos Par 22/genética
Família
Feminino
Perfilação da Expressão Gênica
Marcadores Genéticos
Haplótipos/genética
Seres Humanos
Cristalino/embriologia
Cristalino/metabolismo
Escore Lod
Masculino
Camundongos
Repetições de Microssatélites/genética
Linhagem
Polimorfismo de Nucleotídeo Único/genética
Lâmpada de Fenda
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRYBB3 protein, human); 0 (Genetic Markers); 0 (beta-Crystallin B Chain)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160622
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0157005


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[PMID]:27318838
[Au] Autor:Qi LB; Hu LD; Liu H; Li HY; Leng XY; Yan YB
[Ad] Endereço:State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
[Ti] Título:Cataract-causing mutation S228P promotes ßB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain.
[So] Source:Protein Cell;7(7):501-15, 2016 Jul.
[Is] ISSN:1674-8018
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:ß/γ-Crystallins are predominant structural proteins in the cytoplasm of lens fiber cells and share a similar fold composing of four Greek-key motifs divided into two domains. Numerous cataract-causing mutations have been identified in various ß/γ-crystallins, but the mechanisms underlying cataract caused by most mutations remains uncharacterized. The S228P mutation in ßB1-crystallin has been linked to autosomal dominant congenital nuclear cataract. Here we found that the S228P mutant was prone to aggregate and degrade in both of the human and E. coli cells. The intracellular S228P aggregates could be redissolved by lanosterol. The S228P mutation modified the refolding pathway of ßB1-crystallin by affecting the formation of the dimeric intermediate but not the monomeric intermediate. Compared with native ßB1-crystallin, the refolded S228P protein had less packed structures, unquenched Trp fluorophores and increased hydrophobic exposure. The refolded S228P protein was prone to aggregate at the physiological temperature and decreased the protective effect of ßB1-crystallin on ßA3-crystallin. Molecular dynamic simulation studies indicated that the mutation decreased the subunit binding energy and modified the distribution of surface electrostatic potentials. More importantly, the mutation separated two interacting loops in the C-terminal domain, which shielded the hydrophobic core from solvent in native ßB1-crystallin. These two interacting loops are highly conserved in both of the N- and C-terminal domains of all ß/γ-crystallins. We propose that these two interacting loops play an important role in the folding and structural stability of ß/γ-crystallin domains by protecting the hydrophobic core from solvent access.
[Mh] Termos MeSH primário: Catarata
Simulação de Dinâmica Molecular
Mutação de Sentido Incorreto
Agregação Patológica de Proteínas
Proteólise
Cadeia B de beta-Cristalina
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Catarata/genética
Catarata/metabolismo
Células HeLa
Seres Humanos
Agregação Patológica de Proteínas/genética
Agregação Patológica de Proteínas/metabolismo
Domínios Proteicos
Estrutura Secundária de Proteína
Cadeia B de beta-Cristalina/química
Cadeia B de beta-Cristalina/genética
Cadeia B de beta-Cristalina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRYBB1 protein, human); 0 (beta-Crystallin B Chain)
[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:160620
[St] Status:MEDLINE
[do] DOI:10.1007/s13238-016-0284-3


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[PMID]:27256633
[Au] Autor:Trkova M; Hynek M; Dudakova L; Becvarova V; Hlozanek M; Raskova D; Vincent AL; Liskova P
[Ad] Endereço:Gennet, Centre for Fetal Medicine and Reproductive Genetics, Prague, Czech Republic.
[Ti] Título:Early detection of bilateral cataracts in utero may represent a manifestation of severe congenital disease.
[So] Source:Am J Med Genet A;170(7):1843-8, 2016 Jul.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We observed bilateral cataracts on second trimester ultrasound, in two consecutive pregnancies, with no other structural defects detected. The parents were unrelated and had no family history for the disease. The first pregnancy was terminated in week 22. Copy number variation analysis revealed, in both the aborted fetus and the mother, a 495 kb duplication at 22q11.23 encompassing CRYBB3 and CRYBB2, and not present in variation databases. In the second pregnancy, lens hyperechogenicity was detected by ultrasound at week 13 and 4 days. The identical duplication at 22q11.23 was found in the fetus and considered as possibly pathogenic. At weeks 22 and 30, smaller orbit measurements were elucidated on ultrasound, raising concerns as to the underlying molecular genetic cause, necessitating further investigation. Whole-exome sequencing, using DNA of the first fetus, was performed shortly after the birth of a male child, and two truncating RAB3GAP1 mutations were detected: c.538G>T; p. (Glu180*) and c.943C>T; p. (Arg315*). Neither mutation has been previously reported to be disease-causing; however, evaluation in the context of previously published literature indicated their deleterious nature, implying a clinical diagnosis of Warburg micro syndrome or Martsolf syndrome. Sanger sequencing confirmed segregation of the two mutations within the family, consistent with autosomal recessive inheritance. The child born from the second pregnancy showed features typical of Warburg micro syndrome, with the exception of microcephaly, at age 31 months. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Anormalidades Múltiplas/genética
Catarata/congênito
Catarata/genética
Córnea/anormalidades
Hipogonadismo/genética
Deficiência Intelectual/genética
Microcefalia/genética
Atrofia Óptica/genética
Cadeia B de beta-Cristalina/genética
Proteínas rab3 de Ligação ao GTP/genética
[Mh] Termos MeSH secundário: Anormalidades Múltiplas/diagnóstico
Anormalidades Múltiplas/fisiopatologia
Feto Abortado/fisiopatologia
Catarata/diagnóstico
Catarata/fisiopatologia
Córnea/fisiopatologia
Variações do Número de Cópias de DNA/genética
Éxons/genética
Feminino
Seres Humanos
Hipogonadismo/diagnóstico
Hipogonadismo/fisiopatologia
Lactente
Recém-Nascido
Deficiência Intelectual/diagnóstico
Deficiência Intelectual/fisiopatologia
Masculino
Microcefalia/diagnóstico
Microcefalia/fisiopatologia
Mutação
Atrofia Óptica/diagnóstico
Atrofia Óptica/fisiopatologia
Linhagem
Gravidez
Análise de Sequência de DNA
Ultrassonografia Pré-Natal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRYBB3 protein, human); 0 (beta-Crystallin B Chain); 0 (beta-crystallin B2); EC 3.6.5.2 (RAB3GAP1 protein, human); EC 3.6.5.2 (rab3 GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160604
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.37685



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