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[PMID]: 28135340 [Au] Autor: Waiho K; Fazhan H; Shahreza MS; Moh JH; Noorbaiduri S; Wong LL; Sinnasamy S; Ikhwanuddin M [Ad] Endereço: Institute of Tropical Aquaculture, Universiti Malaysia Terengganu, Kuala Terengganu, Terengganu, Malaysia. [Ti] Título: Transcriptome Analysis and Differential Gene Expression on the Testis of Orange Mud Crab, Scylla olivacea, during Sexual Maturation. [So] Source: PLoS One;12(1):e0171095, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Adequate genetic information is essential for sustainable crustacean fisheries and aquaculture management. The commercially important orange mud crab, Scylla olivacea, is prevalent in Southeast Asia region and is highly sought after. Although it is a suitable aquaculture candidate, full domestication of this species is hampered by the lack of knowledge about the sexual maturation process and the molecular mechanisms behind it, especially in males. To date, data on its whole genome is yet to be reported for S. olivacea. The available transcriptome data published previously on this species focus primarily on females and the role of central nervous system in reproductive development. De novo transcriptome sequencing for the testes of S. olivacea from immature, maturing and mature stages were performed. A total of approximately 144 million high-quality reads were generated and de novo assembled into 160,569 transcripts with a total length of 142.2 Mb. Approximately 15-23% of the total assembled transcripts were annotated when compared to public protein sequence databases (i.e. UniProt database, Interpro database, Pfam database and Drosophila melanogaster protein database), and GO-categorised with GO Ontology terms. A total of 156,181 high-quality Single-Nucleotide Polymorphisms (SNPs) were mined from the transcriptome data of present study. Transcriptome comparison among the testes of different maturation stages revealed one gene (beta crystallin like gene) with the most significant differential expression-up-regulated in immature stage and down-regulated in maturing and mature stages. This was further validated by qRT-PCR. In conclusion, a comprehensive transcriptome of the testis of orange mud crabs from different maturation stages were obtained. This report provides an invaluable resource for enhancing our understanding of this species' genome structure and biology, as expressed and controlled by their gonads. [Mh] Termos MeSH primário: Braquiúros/genética Braquiúros/fisiologia Perfilação da Expressão Gênica/métodos Maturidade Sexual/genética Testículo/metabolismo [Mh] Termos MeSH secundário: Animais Análise por Conglomerados Ontologia Genética Masculino Anotação de Sequência Molecular Polimorfismo de Nucleotídeo Único/genética RNA Mensageiro/genética RNA Mensageiro/metabolismo Padrões de Referência Reprodutibilidade dos Testes Reprodução/genética Transcriptoma/genética beta-Cristalinas/genética beta-Cristalinas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (RNA, Messenger); 0 (beta-Crystallins) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170814 [Lr] Data última revisão: 170814 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170131 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0171095

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[PMID]: 28029780 [Au] Autor: Srivastava SS; Jamkhindikar AA; Raman R; Jobby MK; Chadalawada S; Sankaranarayanan R; Sharma Y [Ad] Endereço: CSIR-Centre for Cellular and Molecular Biology (CCMB) , Uppal Road, Hyderabad 500 007, India. [Ti] Título: A Transition Metal-Binding, Trimeric ßγ-Crystallin from Methane-Producing Thermophilic Archaea, Methanosaeta thermophila. [So] Source: Biochemistry;56(9):1299-1310, 2017 Mar 07. [Is] ISSN: 1520-4995 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: ßγ-Crystallins are important constituents of the vertebrate eye lens, whereas in microbes, they are prevalent as Ca -binding proteins. In archaea, ßγ-crystallins are conspicuously confined to two methanogens, viz., Methanosaeta and Methanosarcina. One of these, i.e., M-crystallin from Methanosarcina acetivorans, has been shown to be a typical Ca -binding ßγ-crystallin. Here, with the aid of a high-resolution crystal structure and isothermal titration calorimetry, we report that "Methallin", a ßγ-crystallin from Methanosaeta thermophila, is a trimeric, transition metal-binding protein. It binds Fe, Ni, Co, or Zn ion with nanomolar affinity, which is consistent even at 55 °C, the optimal temperature for the methanogen's growth. At the center of the protein trimer, the metal ion is coordinated by six histidines, two from each protomer, leading to an octahedral geometry. Small-angle X-ray scattering analysis confirms that the trimer seen in the crystal lattice is a biological assembly; this assembly dissociates to monomers upon removal of the metal ion. The introduction of two histidines (S17H/S19H) into a homologous ßγ-crystallin, Clostrillin, allows it to bind nickel at the introduced site, though with micromolar affinity. However, because of the lack of a compatible interface, nickel binding could not induce trimerization, affirming that Methallin is a naturally occurring trimer for high-affinity transition metal binding. While ßγ-crystallins are known to bind Ca and form homodimers and oligomers, the transition metal-binding, trimeric Methallin is a new paradigm for ßγ-crystallins. The distinct features of Methallin, such as nickel or iron binding, are also possible imprints of biogeochemical changes during the period of its origin. [Mh] Termos MeSH primário: Archaea/metabolismo Multimerização Proteica Elementos de Transição/metabolismo beta-Cristalinas/química beta-Cristalinas/metabolismo gama-Cristalinas/química gama-Cristalinas/metabolismo [Mh] Termos MeSH secundário: Metano/biossíntese Modelos Moleculares Estrutura Quaternária de Proteína Temperatura Ambiente [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Transition Elements); 0 (beta-Crystallins); 0 (gamma-Crystallins); OP0UW79H66 (Methane) [Em] Mês de entrada: 1705 [Cu] Atualização por classe: 170508 [Lr] Data última revisão: 170508 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161229 [St] Status: MEDLINE [do] DOI: 10.1021/acs.biochem.6b00985

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[PMID]: 27992995 [Au] Autor: Kozlyuk N; Sengupta S; Bierma JC; Martin RW [Ad] Endereço: Department of Chemistry, University of California , Irvine, California 92697-2025, United States. [Ti] Título: Calcium Binding Dramatically Stabilizes an Ancestral Crystallin Fold in Tunicate ßγ-Crystallin. [So] Source: Biochemistry;55(50):6961-6968, 2016 Dec 20. [Is] ISSN: 1520-4995 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The tunicate (Ciona intestinalis) ßγ-crystallin represents an intermediate case between the calcium-binding proteins ancestral to the vertebrate ßγ-crystallin fold and the vertebrate structural crystallins. Unlike the structural ßγ-crystallins in the vertebrate eye lens, this ßγ-crystallin strongly binds Ca . Furthermore, Ca binding greatly stabilizes the protein, an effect that has previously been observed in microbial ßγ-crystallins but not in those of vertebrates. This relationship between binding and protein stabilization makes the tunicate ßγ-crystallin an interesting model for studying the evolution of the human ßγ-crystallin. We also compare and contrast the binding sites of tunicate ßγ-crystallin with those of other ßγ-crystallins to develop hypotheses about the functional origin of the lack of Ca -binding sites in human crystallins. [Mh] Termos MeSH primário: Cálcio/metabolismo Ciona intestinalis/metabolismo Cristalino/metabolismo beta-Cristalinas/química gama-Cristalinas/química [Mh] Termos MeSH secundário: Sequência de Aminoácidos Animais Sítios de Ligação Dicroísmo Circular Evolução Molecular Seres Humanos Modelos Moleculares Conformação Proteica Homologia de Sequência de Aminoácidos Espectrometria de Fluorescência beta-Cristalinas/metabolismo gama-Cristalinas/metabolismo [Pt] Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE [Nm] Nome de substância: 0 (beta-Crystallins); 0 (gamma-Crystallins); SY7Q814VUP (Calcium) [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170427 [Lr] Data última revisão: 170427 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161221 [St] Status: MEDLINE

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[PMID]: 27752786 [Au] Autor: Dai J; Zhou J; Liu H; Huang K [Ad] Endereço: Hubei Key Laboratory of Bioinorganic Chemistry and Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, 1037 Luoyu Road, Hongshan, Wuhan, Hubei, 430074, People's Republic of China. [Ti] Título: Selenite and ebselen supplementation attenuates D-galactose-induced oxidative stress and increases expression of SELR and SEP15 in rat lens. [So] Source: J Biol Inorg Chem;21(8):1037-1046, 2016 Dec. [Is] ISSN: 1432-1327 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: Selenite and ebselen supplementation has been shown to possess anti-cataract potential in some experimental animal models of cataract, however, the underlying mechanisms remain unclear. The present study was designed to evaluate the anti-cataract effects and the underlying mechanisms of selenite and ebselen supplementation on galactose induced cataract in rats, a common animal model of sugar cataract. Transmission electron microscopy images of lens fiber cells (LFC) and lens epithelial cells (LEC) were observed in D-galactose-induced experimental cataractous rats treated with or without selenite and ebselen, also redox homeostasis and expression of proteins such as selenoprotein R (SELR), 15kD selenoprotein (SEP15), superoxide dismutase 1 (SOD1), catalase (CAT), ß-crystallin protein, aldose reductase (AR) and glucose-regulated protein 78 (GRP78) were estimated in the lenses. The results showed that D-galactose injection injured rat lens and resulted in cataract formation; however, selenite and ebselen supplementation markedly alleviated ultrastructural injury of LFC and LEC. Moreover, selenite and ebselen supplementation could mitigate the oxidative damage in rat lens and increase the protein expressions of SELR, SEP15, SOD1, CAT and ß-crystallin, as well as decrease the protein expressions of AR and GRP78. Taken together, these findings for the first time reveal the anti-cataract potential of selenite and ebselen in galactosemic cataract, and provide important new insights into the anti-cataract mechanisms of selenite and ebselen in sugar cataract. [Mh] Termos MeSH primário: Azóis/farmacologia Cristalino/efeitos dos fármacos Metionina Sulfóxido Redutases/metabolismo Compostos Organosselênicos/farmacologia Estresse Oxidativo/efeitos dos fármacos Ácido Selenioso/farmacologia Selenoproteínas/metabolismo [Mh] Termos MeSH secundário: Aldeído Redutase/metabolismo Animais Antioxidantes/administração & dosagem Antioxidantes/farmacologia Azóis/administração & dosagem Western Blotting Catalase/metabolismo Catarata/induzido quimicamente Catarata/metabolismo Catarata/prevenção & controle Suplementos Nutricionais Células Epiteliais/efeitos dos fármacos Células Epiteliais/metabolismo Células Epiteliais/ultraestrutura Galactose Glutationa Peroxidase/metabolismo Proteínas de Choque Térmico/metabolismo Cristalino/metabolismo Cristalino/patologia Masculino Microscopia Eletrônica de Transmissão Compostos Organosselênicos/administração & dosagem Ratos Sprague-Dawley Ácido Selenioso/administração & dosagem Superóxido Dismutase-1/metabolismo Oligoelementos/administração & dosagem Oligoelementos/farmacologia beta-Cristalinas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antioxidants); 0 (Azoles); 0 (Heat-Shock Proteins); 0 (Hspa5 protein, rat); 0 (Organoselenium Compounds); 0 (Selenoproteins); 0 (Sep15 protein, rat); 0 (Trace Elements); 0 (beta-Crystallins); 40X2P7DPGH (ebselen); EC 1.1.1.21 (Aldehyde Reductase); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Sod1 protein, rat); EC 1.15.1.1 (Superoxide Dismutase-1); EC 1.8.4.- (Methionine Sulfoxide Reductases); F6A27P4Q4R (Selenious Acid); X2RN3Q8DNE (Galactose) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 171013 [Lr] Data última revisão: 171013 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161019 [St] Status: MEDLINE

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[PMID]: 27234311 [Au] Autor: Yang J; Zhou S; Guo M; Li Y; Gu J [Ad] Endereço: State Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Center, Sun Yat-sen University, 54S Xianlie, Guangzhou, Guangdong, 510060, People's Republic of China. [Ti] Título: Different alpha crystallin expression in human age-related and congenital cataract lens epithelium. [So] Source: BMC Ophthalmol;16:67, 2016 May 28. [Is] ISSN: 1471-2415 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: BACKGROUND: The purpose of this study was to investigate the different expressions of αA-crystallin and αB-crystallin in human lens epithelium of age-related and congenital cataracts. METHODS: The central part of the human anterior lens capsule approximately 5 mm in diameter together with the adhering epithelial cells, were harvested and processed within 6 hours after cataract surgery from age-related and congenital cataract patients or from normal eyes of fresh cadavers. The mRNA and soluble protein levels of αA-crystallin and αB-crystallin in the human lens epithelium were detected by real-time PCR and western blots, respectively. RESULTS: The mRNA and soluble protein expressions of αA-crystallin and αB-crystallin in the lens epithelium were both reduced in age-related and congenital cataract groups when compared with the normal control group. However, the degree of α-crystallin loss in the lens epithelium was highly correlated with different cataract types. The α-crystallin expression of the lens epithelium was greatly reduced in the congenital cataract group but only moderately decreased in the age-related cataract group. The reduction of αA-crystallin soluble protein levels in the congenital cataract group was approximately 2.4 fold decrease compared with that of the age-related cataract group, while an mRNA fold change of 1.67 decrease was observed for the age-related cataract group. Similarly, the reduction of soluble protein levels of αB-crystallin in the congenital cataract group was approximately a 1.57 fold change compared with that of the age-related cataract group. A 1.75 fold change for mRNA levels compared with that of the age-related cataract group was observed. CONCLUSIONS: The results suggest that the differential loss of α-crystallin in the human lens epithelium could be associated with the different mechanisms of cataractogenesis in age-related versus congenital cataracts, subsequently resulting in different clinical presentations. [Mh] Termos MeSH primário: Catarata/metabolismo Cristalino/metabolismo alfa-Cristalinas/metabolismo beta-Cristalinas/metabolismo [Mh] Termos MeSH secundário: Idoso Análise de Variância Western Blotting Catarata/congênito Criança Pré-Escolar Epitélio/metabolismo Feminino Seres Humanos Lactente Masculino Meia-Idade RNA Mensageiro/metabolismo Reação em Cadeia da Polimerase em Tempo Real [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (RNA, Messenger); 0 (alpha-Crystallins); 0 (beta-Crystallins) [Em] Mês de entrada: 1701 [Cu] Atualização por classe: 170126 [Lr] Data última revisão: 170126 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160529 [St] Status: MEDLINE [do] DOI: 10.1186/s12886-016-0241-1

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[PMID]: 26145580 [Au] Autor: Mishra A; Krishnan B; Raman R; Sharma Y [Ad] Endereço: CSIR-Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad 500 007, India. [Ti] Título: Ca2+ and ßγ-crystallins: An affair that did not last? [So] Source: Biochim Biophys Acta;1860(1 Pt B):299-303, 2016 Jan. [Is] ISSN: 0006-3002 [Cp] País de publicação: Netherlands [La] Idioma: eng [Ab] Resumo: BACKGROUND: During the last three decades, lens ß- and γ-crystallins have found a huge number of kin from numerous taxonomical sources. Most of these proteins from invertebrates and microbes have been demonstrated or predicted to bind Ca2+ involving a distinct double-clamp motif, which is largely degenerated in lens homologues. SCOPE OF REVIEW: The various aspects of transformation of ßγ-crystallins from a quintessential Ca2+-binding protein into a primarily structural molecule have been reviewed. MAJOR CONCLUSIONS: In lens members of ßγ-crystallins, the residues involved in Ca2+ binding have diverged considerably from the classical consensus with consequent reduction in their Ca2+-binding properties. This evolutionary change is congenial to their new role as robust constituents of lens. The exact functions of the residual affinity for Ca2+ are yet to be established. GENERAL SIGNIFICANCE: This review highlights the significance of reduction in Ca2+-binding ability of the ßγ-crystallins for lens physiology and why this residual affinity may be functionally important. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease. [Mh] Termos MeSH primário: Cálcio/metabolismo Evolução Molecular Cristalino/metabolismo beta-Cristalinas/fisiologia gama-Cristalinas/fisiologia [Mh] Termos MeSH secundário: Animais Sítios de Ligação/genética Proteínas do Olho/genética Proteínas do Olho/metabolismo Seres Humanos Modelos Genéticos Ligação Proteica/genética [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW [Nm] Nome de substância: 0 (Eye Proteins); 0 (beta-Crystallins); 0 (gamma-Crystallins); SY7Q814VUP (Calcium) [Em] Mês de entrada: 1606 [Cu] Atualização por classe: 161126 [Lr] Data última revisão: 161126 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150707 [St] Status: MEDLINE

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[PMID]: 26145577 [Au] Autor: Lampi KJ; Murray MR; Peterson MP; Eng BS; Yue E; Clark AR; Barbar E; David LL [Ad] Endereço: Integrative Biosciences, Oregon Health & Science University, Portland, OR 97239-3098, United States. Electronic address: lampik@ohsu.edu. [Ti] Título: Differences in solution dynamics between lens ß-crystallin homodimers and heterodimers probed by hydrogen-deuterium exchange and deamidation. [So] Source: Biochim Biophys Acta;1860(1 Pt B):304-14, 2016 Jan. [Is] ISSN: 0006-3002 [Cp] País de publicação: Netherlands [La] Idioma: eng [Ab] Resumo: BACKGROUND: Lens transparency is due to the ordered arrangement of the major structural proteins, called crystallins. ßB2 crystallin in the lens of the eye readily forms dimers with other ß-crystallin subunits, but the resulting heterodimer structures are not known and were investigated in this study. METHODS: Structures of ßA3 and ßB2 crystallin homodimers and the ßA3/ßB2 crystallin heterodimers were probed by measuring changes in solvent accessibility using hydrogen-deuterium exchange with mass spectrometry. We further mimicked deamidation in ßB2 and probed the effect on the ßA3/ßB2 heterodimer. Results were confirmed with chemical crosslinking and NMR. RESULTS: Both ßA3 and ßB2 had significantly decreased deuterium levels in the heterodimer compared to their respective homodimers, suggesting that they had less solvent accessibility and were more compact in the heterodimer. The compact structure of ßB2 was supported by the identification of chemical crosslinks between lysines in ßB2 within the heterodimer that were inconsistent with ßB2's extended homodimeric structure. The compact structure of ßA3 was supported by an overall decrease in mobility of ßA3 in the heterodimer detected by NMR. In ßB2, peptides 70-84 and 121-134 were exposed in the homodimer, but buried in the heterodimer with ≥50% decreases in deuterium levels. Homologous peptides in ßA3, 97-109 and 134-149, had 25-50% decreases in deuterium levels in the heterodimer. These peptides are probable sites of interaction between ßB2 and ßA3 and are located at the predicted interface between subunits with bent linkers. Deamidation at Q184 in ßB2 at this predicted interface led to a less compact ßB2 in the heterodimer. The more compact structure of the ßA3/ßB2 heterodimer was also more heat stable than either of the homodimers. CONCLUSIONS: The major structural proteins in the lens, the ß-crystallins, are not static, but dynamic in solution, with differences in accessibility between the homo-and hetero-dimers. This structural flexibility, particularly of ßB2, may facilitate formation of different size higher-ordered structures found in the transparent lens. GENERAL SIGNIFICANCE: Understanding complex hetero-oligomer interactions between ß-crystallins in normal lens and how these interactions change during aging is fundamental to understanding the cause of cataracts. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease. [Mh] Termos MeSH primário: Amidas/química Medição da Troca de Deutério/métodos Cristalino/química Multimerização Proteica beta-Cristalinas/química beta-Cristalinas/ultraestrutura [Mh] Termos MeSH secundário: Sequência de Aminoácidos Animais Sítios de Ligação Dimerização Seres Humanos Técnicas de Sonda Molecular Dados de Sequência Molecular Ligação Proteica Conformação Proteica [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Amides); 0 (beta-Crystallins) [Em] Mês de entrada: 1606 [Cu] Atualização por classe: 170220 [Lr] Data última revisão: 170220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150707 [St] Status: MEDLINE

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[PMID]: 26518564 [Au] Autor: Yanshole LV; Yanshole VV; Snytnikova OA; Fursova AZh; Kolosova NG; Tsentalovich YP; Sagdeev RZ [Ad] Endereço: International Tomography Center of the Siberian Branch of Russian Academy of the Sciences, Novosibirsk, Russia. yura@tomo.nsc.ru. [Ti] Título: Effect of SkQ1 eye drops on the rat lens metabolomic composition and the chaperone activity of α-crystallin. [So] Source: Dokl Biochem Biophys;464:341-5, 2015. [Is] ISSN: 1608-3091 [Cp] País de publicação: Russia (Federation) [La] Idioma: eng [Ab] Resumo: The ability of SkQ1 eye drops to slow down the cataract development is demonstrated on the senescence-accelerated OXYS rats: the SkQ1 treatment leads to the considerable improvement of the lens condition as compared to the control group. The comparison of the chaperone activities of α-crystallins isolated from the rat lenses did not reveal significant difference between SkQ1-treated and control rats. The contents of major metabolites (23 compounds) in lenses of SkQ1-treated and untreated rats are also very similar, though the concentration of reduced glutathione (GSH) in lenses of SkQ1-treated rats is 12% lower. This difference may be attributed to the reduction of the oxidative stress under action of SkQ1 eye drops, and to the decreased requirement to produce high amounts of this antioxidant. [Mh] Termos MeSH primário: Catarata/tratamento farmacológico Catarata/metabolismo Depuradores de Radicais Livres/administração & dosagem Plastoquinona/análogos & derivados alfa-Cristalinas/metabolismo [Mh] Termos MeSH secundário: Envelhecimento/efeitos dos fármacos Envelhecimento/metabolismo Animais Modelos Animais de Doenças Glutationa/metabolismo Cinética Cristalino/efeitos dos fármacos Cristalino/metabolismo Soluções Oftálmicas Estresse Oxidativo/efeitos dos fármacos Estresse Oxidativo/fisiologia Plastoquinona/administração & dosagem Multimerização Proteica Ratos beta-Cristalinas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (10-(6'-plastoquinonyl)decyltriphenylphosphonium); 0 (Free Radical Scavengers); 0 (Ophthalmic Solutions); 0 (alpha-Crystallins); 0 (beta-Crystallins); GAN16C9B8O (Glutathione); OAC30J69CN (Plastoquinone) [Em] Mês de entrada: 1608 [Cu] Atualização por classe: 171019 [Lr] Data última revisão: 171019 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 151101 [St] Status: MEDLINE [do] DOI: 10.1134/S1607672915050191

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[PMID]: 26453637 [Au] Autor: Fan X; Zhou S; Wang B; Hom G; Guo M; Li B; Yang J; Vaysburg D; Monnier VM [Ad] Endereço: From the ‡Department of Pathology, xxf3@case.edu vmm3@case.edu. [Ti] Título: Evidence of Highly Conserved ß-Crystallin Disulfidome that Can be Mimicked by In Vitro Oxidation in Age-related Human Cataract and Glutathione Depleted Mouse Lens. [So] Source: Mol Cell Proteomics;14(12):3211-23, 2015 Dec. [Is] ISSN: 1535-9484 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Low glutathione levels are associated with crystallin oxidation in age-related nuclear cataract. To understand the role of cysteine residue oxidation, we used the novel approach of comparing human cataracts with glutathione-depleted LEGSKO mouse lenses for intra- versus intermolecular disulfide crosslinks using 2D-PAGE and proteomics, and then systematically identified in vivo and in vitro all disulfide forming sites using ICAT labeling method coupled with proteomics. Crystallins rich in intramolecular disulfides were abundant at young age in human and WT mouse lens but shifted to multimeric intermolecular disulfides at older age. The shift was ∼4x accelerated in LEGSKO lens. Most cysteine disulfides in ß-crystallins (except ßA4 in human) were highly conserved in mouse and human and could be generated by oxidation with H(2)O(2), whereas γ-crystallin oxidation selectively affected γC23/42/79/80/154, γD42/33, and γS83/115/130 in human cataracts, and γB79/80/110, γD19/109, γF19/79, γE19, γS83/130, and γN26/128 in mouse. Analysis based on available crystal structure suggests that conformational changes are needed to expose Cys42, Cys79/80, Cys154 in γC; Cys42, Cys33 in γD, and Cys83, Cys115, and Cys130 in γS. In conclusion, the ß-crystallin disulfidome is highly conserved in age-related nuclear cataract and LEGSKO mouse, and reproducible by in vitro oxidation, whereas some of the disulfide formation sites in γ-crystallins necessitate prior conformational changes. Overall, the LEGSKO mouse model is closely reminiscent of age-related nuclear cataract. [Mh] Termos MeSH primário: Envelhecimento/metabolismo Catarata/metabolismo Dissulfetos/química Glutationa/deficiência beta-Cristalinas/química beta-Cristalinas/isolamento & purificação [Mh] Termos MeSH secundário: Animais Linhagem Celular Cisteína/química Modelos Animais de Doenças Seres Humanos Técnicas In Vitro Cristalino/citologia Cristalino/metabolismo Camundongos Oxirredução Conformação Proteica Proteômica/métodos [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Disulfides); 0 (beta-Crystallins); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine) [Em] Mês de entrada: 1610 [Cu] Atualização por classe: 170220 [Lr] Data última revisão: 170220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 151011 [St] Status: MEDLINE [do] DOI: 10.1074/mcp.M115.050948

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[PMID]: 26188790 [Au] Autor: Takata T; Fujii N [Ad] Endereço: Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan. [Ti] Título: Effect of Asp 96 isomerization on the properties of a lens αB-crystallin-derived short peptide. [So] Source: J Pharm Biomed Anal;116:139-44, 2015 Dec 10. [Is] ISSN: 1873-264X [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: One of the major reasons for age-related cataract formation is an accumulation of insoluble lens proteins. In particular, higher-order α-crystallin aggregates, comprising αA and αB subunits, are insolubilized by the build up of various post-translational modifications over time. Although we previously found an exceptional amount of Asp96 isomerization in αB-crystallin from aged human lens, the biological effect remains unknown. To approximate the effect of Asp 96 isomerization in αB-crystallin, here residues 93-103 of αB-crystallin were chemically synthesized as peptides in which l-α-Asp was replaced with l-ß-Asp, D-α-Asp, or D-ß-Asp. The resulting peptides were then compared in a biological assay. The results showed that isomerization of Asp 96 altered both the local structure of peptide and its stability against enzymatic digestion. In addition, the synthesized peptides decreased the insoluble fraction of heated α-crystallin. The D-ß-Asp-containing peptide further decreased heat-induced precipitation of α-crystallin, and a chaperone assay based on heated alcohol dehydrogenase implied differential interaction of the peptides with substrate depending on the Asp isomer present in each. Our results suggest that the formation of Asp isomers is likely to affect the higher-order oligomer structure of α-crystallin and thereby its chaperone functions in aged lens. [Mh] Termos MeSH primário: Ácido Aspártico/química Cristalino/química Fragmentos de Peptídeos/química alfa-Cristalinas/química beta-Cristalinas/química [Mh] Termos MeSH secundário: Sequência de Aminoácidos Ácido Aspártico/genética Ácido Aspártico/metabolismo Cristalinas/química Cristalinas/genética Cristalinas/metabolismo Seres Humanos Isomerismo Cristalino/metabolismo Meia-Idade Dados de Sequência Molecular Fragmentos de Peptídeos/genética Fragmentos de Peptídeos/metabolismo alfa-Cristalinas/genética alfa-Cristalinas/metabolismo beta-Cristalinas/genética beta-Cristalinas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Crystallins); 0 (Peptide Fragments); 0 (alpha-Crystallins); 0 (beta-Crystallins); 30KYC7MIAI (Aspartic Acid) [Em] Mês de entrada: 1608 [Cu] Atualização por classe: 151020 [Lr] Data última revisão: 151020 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150720 [St] Status: MEDLINE

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