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Pesquisa : D12.776.503.140 [Categoria DeCS]
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[PMID]:26912787
[Au] Autor:Bastounis E; Álvarez-González B; del Álamo JC; Lasheras JC; Firtel RA
[Ad] Endereço:Section of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093-0380.
[Ti] Título:Cooperative cell motility during tandem locomotion of amoeboid cells.
[So] Source:Mol Biol Cell;27(8):1262-71, 2016 Apr 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Streams of migratory cells are initiated by the formation of tandem pairs of cells connected head to tail to which other cells subsequently adhere. The mechanisms regulating the transition from single to streaming cell migration remain elusive, although several molecules have been suggested to be involved. In this work, we investigate the mechanics of the locomotion ofDictyosteliumtandem pairs by analyzing the spatiotemporal evolution of their traction adhesions (TAs). We find that in migrating wild-type tandem pairs, each cell exerts traction forces on stationary sites (∼80% of the time), and the trailing cell reuses the location of the TAs of the leading cell. Both leading and trailing cells form contractile dipoles and synchronize the formation of new frontal TAs with ∼54-s time delay. Cells not expressing the lectin discoidin I or moving on discoidin I-coated substrata form fewer tandems, but the trailing cell still reuses the locations of the TAs of the leading cell, suggesting that discoidin I is not responsible for a possible chemically driven synchronization process. The migration dynamics of the tandems indicate that their TAs' reuse results from the mechanical synchronization of the leading and trailing cells' protrusions and retractions (motility cycles) aided by the cell-cell adhesions.
[Mh] Termos MeSH primário: Dictyostelium/citologia
[Mh] Termos MeSH secundário: Fenômenos Biomecânicos
Adesão Celular
Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Movimento Celular/fisiologia
Dictyostelium/genética
Discoidinas/genética
Discoidinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Discoidins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160226
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-12-0836


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[PMID]:26812435
[Au] Autor:Bush M; Setiaputra D; Yip CK; Molday RS
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada.
[Ti] Título:Cog-Wheel Octameric Structure of RS1, the Discoidin Domain Containing Retinal Protein Associated with X-Linked Retinoschisis.
[So] Source:PLoS One;11(1):e0147653, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RS1, also known as retinoschisin, is a disulphide-linked, discoidin domain containing homo-oligomeric protein that plays a crucial role in maintaining the cellular and synaptic organization of the retina. This is highlighted by the finding that over 130 mutations in RS1 cause X-linked retinoschisis, a retinal degenerative disease characterized by the splitting of the retinal cell layers, disruption of the photoreceptor-bipolar synapses, degeneration of photoreceptors, and severe loss in central vision. In this study, we investigated the arrangement of the RS1 subunits within the oligomer complex using single particle electron microscopy. RS1 was seen as two stacked rings with each ring displaying a symmetrical cog wheel-like structure with eight teeth or projections corresponding to the RS1 subunits. Three dimensional reconstruction and molecular modelling indicated that the discoidin domain, the principal functional unit of RS1, projects outward, and the Rs1 domain and C-terminal segment containing intermolecular disulphide bonds are present in the inner ring to form the core octameric structure. These studies provide a basis for further understanding the role of the novel core RS1 octameric complex in retinal cell biology and X-linked retinoschisis.
[Mh] Termos MeSH primário: Proteínas do Olho/química
Modelos Moleculares
Retina/metabolismo
[Mh] Termos MeSH secundário: Cromatografia em Gel
Discoidinas
Eletroforese em Gel de Poliacrilamida
Proteínas do Olho/genética
Proteínas do Olho/metabolismo
Seres Humanos
Lectinas/química
Microscopia Eletrônica
Mutagênese
Estrutura Quaternária de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas de Protozoários/química
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Retinosquise/genética
Retinosquise/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Discoidins); 0 (Eye Proteins); 0 (Lectins); 0 (Protein Subunits); 0 (Protozoan Proteins); 0 (RS1 protein, human); 0 (Recombinant Proteins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160127
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0147653


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[PMID]:26449461
[Au] Autor:Garige M; Walters E
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Howard University College of Medicine, Washington, DC, USA.
[Ti] Título:Curcumin inhibits development and cell adhesion in Dictyostelium discoideum: Implications for YakA signaling and GST enzyme function.
[So] Source:Biochem Biophys Res Commun;467(2):275-81, 2015 Nov 13.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The molecular basis for nutraceutical properties of the polyphenol curcumin (Curcuma longa, Turmeric) is complex, affecting multiple factors that regulate cell signaling and homeostasis. Here, we report the effect of curcumin on cellular and developmental mechanisms in the eukaryotic model, Dictyostelium discoideum. Dictyostelium proliferation was inhibited in the presence of curcumin, which also suppressed the prestarvation marker, discoidin I, members of the yakA-mediated developmental signaling pathway, and expression of the extracellular matrix/cell adhesion proteins (DdCAD and csA). This resulted in delayed chemotaxis, adhesion, and development of the organism. In contrast to the inhibitory effects on developmental genes, curcumin induced gstA gene expression, overall GST activity, and generated production of reactive oxygen species. These studies expand our knowledge of developmental and biochemical signaling influenced by curcumin, and lends greater consideration of GST enzyme function in eukaryotic cell signaling, development, and differentiation.
[Mh] Termos MeSH primário: Curcumina/farmacologia
Dictyostelium/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Glutationa Transferase/genética
Proteínas Quinases/genética
[Mh] Termos MeSH secundário: Adesão Celular/efeitos dos fármacos
Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Proliferação Celular/efeitos dos fármacos
Quimiotaxia/efeitos dos fármacos
Dictyostelium/genética
Dictyostelium/crescimento & desenvolvimento
Dictyostelium/metabolismo
Discoidinas
Regulação da Expressão Gênica no Desenvolvimento
Glutationa Transferase/metabolismo
Lectinas/genética
Lectinas/metabolismo
Proteínas Quinases/metabolismo
Proteínas de Protozoários/genética
Proteínas de Protozoários/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Discoidins); 0 (Enzyme Inhibitors); 0 (Lectins); 0 (Protozoan Proteins); 0 (Reactive Oxygen Species); 0 (cell cohesion molecule, Dictyostelium); EC 2.5.1.18 (Glutathione Transferase); EC 2.7.- (Protein Kinases); EC 2.7.1.- (YakA protein, Dictyostelium discoideum); IT942ZTH98 (Curcumin)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151010
[St] Status:MEDLINE


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[PMID]:25372678
[Au] Autor:Kim KH; Hong SK; Hwang KY; Kim EE
[Ad] Endereço:Biomedical Research Institute, Korea Institute of Science and Technology, Hwarang-ro 14-gil 5, Seongbuk-gu, Seoul 136-791, Republic of Korea.
[Ti] Título:Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association.
[So] Source:Acta Crystallogr D Biol Crystallogr;70(Pt 11):2863-74, 2014 Nov.
[Is] ISSN:1399-0047
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 Šresolution, which reveals a distorted eight-stranded ß-barrel with two short α-helices at one end of the barrel. Interestingly, the N- and C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/química
Peptídeos e Proteínas de Sinalização Intracelular/química
Lectinas/química
Proteínas de Protozoários/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Moléculas de Adesão Celular/metabolismo
Cristalografia por Raios X
Discoidinas
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Lectinas/metabolismo
Camundongos
Modelos Moleculares
Dados de Sequência Molecular
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas de Protozoários/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Discoidins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Lectins); 0 (Mkln1 protein, mouse); 0 (Protozoan Proteins)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141106
[St] Status:MEDLINE
[do] DOI:10.1107/S139900471401894X


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[PMID]:23291776
[Au] Autor:Song J; Imanaka H; Imamura K; Minoda M; Yamaguchi S; Nakanishi K
[Ad] Endereço:Graduate School of Natural Science and Technology, Okayama University, Japan.
[Ti] Título:The discoidin domain of Bacillus circulans ß-galactosidase plays an essential role in repressing galactooligosaccharide production.
[So] Source:Biosci Biotechnol Biochem;77(1):73-9, 2013.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The recently cloned ß-galactosidase from Bacillus circulans ATCC 31382, designated BgaD, contains a multiple domain architecture including a F5/8 type C domain or a discoidin (DS) domain in the C-terminal peptide region. Here we report that the DS domain plays an essential role in repressing the production of galactooligosaccharides (GOSs). We prepared deletion mutants and point-mutated forms of rBgaD-A (deletion of the BgaD signal peptide) to compare their reaction behaviors. The yields of GOSs for all of the point-mutated forms as well as the deletion mutants of rBgaD-As increased as compared to rBgaD-A. In particular, W1540A mutant BgaD-A (rBgaD-A_W1540A) produced much more GOSs than rBgaD-A. Surface plasmon resonance experiments indicated that both the wild-type and the W1540A mutant DS domains showed high affinity for galactosyllactose. rBgaD-A, which has a wild-type DS domain, showed high hydrolytic activity toward galactosyllactose, while the hydrolytic activities of rBgaD-D, without a DS domain, and rBgaD-A_W1540A, with a mutant DS domain were extremely low. The findings obtained in this study indicate that the wild-type DS domain of rBgaD-A has a function that aids galactosyllactose molecules to be properly oriented within the active site, so that they can be hydrolyzed efficiently to produce galactose/glucose by inhibiting the accumulation of GOSs.
[Mh] Termos MeSH primário: Bacillus/enzimologia
Proteínas de Bactérias/metabolismo
Galactosídeos/biossíntese
beta-Galactosidase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Bacillus/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Discoidinas
Escherichia coli/genética
Galactose/biossíntese
Lactose/biossíntese
Lectinas/química
Lectinas/genética
Lectinas/metabolismo
Dados de Sequência Molecular
Mutação
Estrutura Terciária de Proteína
Proteínas de Protozoários/química
Proteínas de Protozoários/genética
Proteínas de Protozoários/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Relação Estrutura-Atividade
beta-Galactosidase/química
beta-Galactosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Discoidins); 0 (Galactosides); 0 (Lectins); 0 (Protozoan Proteins); 0 (Recombinant Proteins); EC 3.2.1.23 (beta-Galactosidase); J2B2A4N98G (Lactose); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130108
[St] Status:MEDLINE


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[PMID]:23084775
[Au] Autor:Guerriero G
[Ad] Endereço:Fungal Genetics and Genomics Unit, Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Science Vienna, University and Research Center Campus Tulln-Technopol, Tulln, Austria. gea.guerriero@boku.ac.at
[Ti] Título:Putative chitin synthases from Branchiostoma floridae show extracellular matrix-related domains and mosaic structures.
[So] Source:Genomics Proteomics Bioinformatics;10(4):197-207, 2012 Aug.
[Is] ISSN:2210-3244
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:The transition from unicellular to multicellular life forms requires the development of a specialized structural component, the extracellular matrix (ECM). In Metazoans, there are two main supportive systems, which are based on chitin and collagen/hyaluronan, respectively. Chitin is the major constituent of fungal cell walls and arthropod exoskeleton. However, presence of chitin/chitooligosaccharides has been reported in lower chordates and during specific stages of vertebrate development. In this study, the occurrence of chitin synthases (CHSs) was investigated with a bioinformatics approach in the cephalochordate Branchiostoma floridae, in which the presence of chitin was initially reported in the skeletal rods of the pharyngeal gill basket. Twelve genes coding for proteins containing conserved amino acid residues of processive glycosyltransferases from GT2 family were found and 10 of them display mosaic structures with novel domains never reported previously in a chitin synthase. In particular, the presence of a discoidin (DS) and a sterile alpha motif (SAM) domain was found in nine identified proteins. Sequence analyses and homology modelling suggest that these domains might interact with the extracellular matrix and mediate protein-protein interaction. The multi-domain putative chitin synthases from B. floridae constitute an emblematic example of the explosion of domain innovation and shuffling which predate Metazoans.
[Mh] Termos MeSH primário: Quitina Sintase/química
Quitina Sintase/genética
Cordados não Vertebrados/enzimologia
Cordados não Vertebrados/genética
Matriz Extracelular/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Evolução Biológica
Quitina/química
Quitina/metabolismo
Quitina Sintase/metabolismo
Biologia Computacional
Discoidinas
Matriz Extracelular/química
Glicosiltransferases/química
Glicosiltransferases/metabolismo
Lectinas
Modelos Moleculares
Dados de Sequência Molecular
Domínios e Motivos de Interação entre Proteínas
Estrutura Terciária de Proteína
Proteínas de Protozoários
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Discoidins); 0 (Lectins); 0 (Protozoan Proteins); 1398-61-4 (Chitin); EC 2.4.- (Glycosyltransferases); EC 2.4.1.16 (Chitin Synthase)
[Em] Mês de entrada:1306
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121023
[St] Status:MEDLINE


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[PMID]:22389384
[Au] Autor:Araki Y; Shimizu HD; Saeki K; Okamoto M; Yamada L; Ishida K; Sawada H; Urushihara H
[Ad] Endereço:Graduate School of Life and Environmental Sciences, University of Tsukuba, Tennodai, Tsukuba, Ibaraki, Japan.
[Ti] Título:A surface glycoprotein indispensable for gamete fusion in the social amoeba Dictyostelium discoideum.
[So] Source:Eukaryot Cell;11(5):638-44, 2012 May.
[Is] ISSN:1535-9786
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sexual reproduction is essential for the maintenance of species in a wide variety of multicellular organisms, and even unicellular organisms that normally proliferate asexually possess a sexual cycle because of its contribution to increased genetic diversity. Information concerning the molecules involved in fertilization is accumulating for many species of the metazoan, plant, and fungal lineages, and the evolutionary consideration of sexual reproduction systems is now an interesting issue. Macrocyst formation in the social amoeba Dictyostelium discoideum is a sexual process in which cells become sexually mature under dark and submerged conditions and fuse with complementary mating-type cells. In the present study, we isolated D. discoideum insertional mutants defective in sexual cell fusion and identified the relevant gene, macA, which encodes a highly glycosylated, 2,041-amino-acid membrane protein (MacA). Although its overall similarity is restricted to proteins of unknown function within dictyostelids, it contains LamGL and discoidin domains, which are implicated in cell adhesion. The growth and development of macA-null mutants were indistinguishable from those of the parental strain. The overexpression of macA using the V18 promoter in a macA-null mutant completely restored its sexual defects. Although the macA gene encoded exactly the same protein in a complementary mating-type strain, it was expressed at a much lower level. These results suggest that MacA is indispensable for gamete interactions in D. discoideum, probably via cell adhesion. There is a possibility that it is controlled in a mating-type-dependent manner.
[Mh] Termos MeSH primário: Dictyostelium/crescimento & desenvolvimento
Glicoproteínas de Membrana/química
Proteínas de Protozoários/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Adesão Celular
Membrana Celular/química
Sequência Conservada
Dictyostelium/genética
Dictyostelium/metabolismo
Discoidinas
Regulação da Expressão Gênica no Desenvolvimento
Genes de Protozoários
Glicosilação
Lectinas/química
Mutagênese Insercional/métodos
Regiões Promotoras Genéticas
Estrutura Terciária de Proteína
Reprodução
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Discoidins); 0 (Lectins); 0 (Membrane Glycoproteins); 0 (Protozoan Proteins)
[Em] Mês de entrada:1208
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120306
[St] Status:MEDLINE
[do] DOI:10.1128/EC.00028-12


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[PMID]:22292953
[Au] Autor:Wu JW; Liu HL
[Ad] Endereço:Institute of Biotechnology, National Taipei University of Technology, Taipei 10608, Taiwan.
[Ti] Título:In silico investigation of the disease-associated retinoschisin C110Y and C219G mutants.
[So] Source:J Biomol Struct Dyn;29(5):937-59, 2012.
[Is] ISSN:1538-0254
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The juvenile X-linked retinoschisis (XLRS) is a retinal disease caused by mutations in the secretory protein, retinoschisin (RS1). Majority of the disease is resulted from single point mutations on the RS1 discoidin domain with cysteine mutations being related to some of the more severe cases of XLRS. Previous studies have indicated that two mutations (C110Y and C219G), which involve cysteines that form intramolecular disulfide bonds in the native discoidin domain, resulted in different oligomerization states of the proteins and did not correlate with the degree of protein stability as calculated by the change in folding free energy. Through homology modeling, bioinformatics predictions, molecular dynamics (MD) and docking simulations, we attempt to investigate the effects of these two mutations on the structure of the RS1 discoidin domain in relevance to the discrepancy found between structural stability and aggregation propensity. Based on our findings, this discrepancy can be explained by the ability of C110Y mutant to establish suitable modules for initiating amorphous aggregation and to expand the aggregating mass through predominantly hydrophobic interactions. The low capability of C219G mutant to oligomerize, on the other hand, may be due to its greater structural instability and lesser hydrophobic tendency, two properties that may be unsupportive of aggregation. The results, altogether, indicate that aggregation propensity in the RS1 C110Y mutant is dependent upon the formation of suitable aggregating substrates for propagation of aggregation and not directly related to or determined by overall structural instability. As for the wildtype protein, the binding specificity of the spikes for biological function and the formation of octameric structure are contributed by important loop interactions, as well as evolved structural and sequence-based properties that prevent aggregation.
[Mh] Termos MeSH primário: Proteínas do Olho/química
Proteínas do Olho/genética
Modelos Moleculares
Mutação Puntual
Retinosquise/genética
[Mh] Termos MeSH secundário: Cisteína/química
Cisteína/genética
Discoidinas
Dissulfetos/química
Proteínas do Olho/metabolismo
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Lectinas/metabolismo
Simulação de Dinâmica Molecular
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Estrutura Terciária de Proteína
Proteínas de Protozoários/metabolismo
Reprodutibilidade dos Testes
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Discoidins); 0 (Disulfides); 0 (Eye Proteins); 0 (Lectins); 0 (Protozoan Proteins); 0 (RS1 protein, human); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1210
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120202
[St] Status:MEDLINE


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[PMID]:22245536
[Au] Autor:Molday RS; Kellner U; Weber BH
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Centre of Macular Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, B.C. V6T 1Z3, Canada. molday@mail.ubc.ca
[Ti] Título:X-linked juvenile retinoschisis: clinical diagnosis, genetic analysis, and molecular mechanisms.
[So] Source:Prog Retin Eye Res;31(3):195-212, 2012 May.
[Is] ISSN:1873-1635
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:X-linked juvenile retinoschisis (XLRS, MIM 312700) is a common early onset macular degeneration in males characterized by mild to severe loss in visual acuity, splitting of retinal layers, and a reduction in the b-wave of the electroretinogram (ERG). The RS1 gene (MIM 300839) associated with the disease encodes retinoschisin, a 224 amino acid protein containing a discoidin domain as the major structural unit, an N-terminal cleavable signal sequence, and regions responsible for subunit oligomerization. Retinoschisin is secreted from retinal cells as a disulphide-linked homo-octameric complex which binds to the surface of photoreceptors and bipolar cells to help maintain the integrity of the retina. Over 190 disease-causing mutations in the RS1 gene are known with most mutations occurring as non-synonymous changes in the discoidin domain. Cell expression studies have shown that disease-associated missense mutations in the discoidin domain cause severe protein misfolding and retention in the endoplasmic reticulum, mutations in the signal sequence result in aberrant protein synthesis, and mutations in regions flanking the discoidin domain cause defective disulphide-linked subunit assembly, all of which produce a non-functional protein. Knockout mice deficient in retinoschisin have been generated and shown to display most of the characteristic features found in XLRS patients. Recombinant adeno-associated virus (rAAV) mediated delivery of the normal RS1 gene to the retina of young knockout mice result in long-term retinoschisin expression and rescue of retinal structure and function providing a 'proof of concept' that gene therapy may be an effective treatment for XLRS.
[Mh] Termos MeSH primário: Proteínas do Olho/genética
Doenças Genéticas Ligadas ao Cromossomo X/genética
Retinosquise/genética
[Mh] Termos MeSH secundário: Animais
Diagnóstico Diferencial
Discoidinas
Eletrorretinografia
Proteínas do Olho/metabolismo
Doenças Genéticas Ligadas ao Cromossomo X/diagnóstico
Doenças Genéticas Ligadas ao Cromossomo X/metabolismo
Doenças Genéticas Ligadas ao Cromossomo X/terapia
Seres Humanos
Lectinas/metabolismo
Masculino
Camundongos
Proteínas de Protozoários/metabolismo
Retinosquise/diagnóstico
Retinosquise/metabolismo
Retinosquise/terapia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Discoidins); 0 (Eye Proteins); 0 (Lectins); 0 (Protozoan Proteins); 0 (RS1 protein, human)
[Em] Mês de entrada:1206
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120117
[St] Status:MEDLINE
[do] DOI:10.1016/j.preteyeres.2011.12.002


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[PMID]:20580724
[Au] Autor:Mathieu SV; Aragão KS; Imberty A; Varrot A
[Ad] Endereço:CERMAV-CNRS, 601 rue de la Chimie, BP53, F-38041 Grenoble Cedex 09, France.
[Ti] Título:Discoidin I from Dictyostelium discoideum and Interactions with oligosaccharides: specificity, affinity, crystal structures, and comparison with discoidin II.
[So] Source:J Mol Biol;400(3):540-54, 2010 Jul 16.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Discoidin I (DiscI) and discoidin II (DiscII) are N-acetylgalactosamine (GalNAc)-binding proteins from Dictyostelium discoideum. They consist of two domains: an N-terminal discoidin domain and a C-terminal H-type lectin domain. They were cloned and expressed in high yield in recombinant form in Escherichia coli. Although both lectins bind galactose (Gal) and GalNAc, glycan array experiments performed on the recombinant proteins displayed strong differences in their specificity for oligosaccharides. DiscI and DiscII bind preferentially to Gal/GalNAcbeta1-3Gal/GalNAc-containing and Gal/GalNAcbeta1-4GlcNAcbeta1-6Gal/GalNAc-containing glycans, respectively. The affinity of the interaction of DiscI with monosaccharides and disaccharides was evaluated using isothermal titration calorimetry experiments. The three-dimensional structures of native DiscI and its complexes with GalNAc, GalNAcbeta1-3Gal, and Galbeta1-3GalNAc were solved by X-ray crystallography. DiscI forms trimers with involvement of calcium at the monomer interface. The N-terminal discoidin domain presents a structural similarity to F-type lectins such as the eel agglutinin, where an amphiphilic binding pocket suggests possible carbohydrate-binding activity. In the C-terminal H-type lectin domain, the GalNAc residue establishes specific hydrogen bonds that explain the observed affinity (K(d)=3x10(-4) M). The different specificities of DiscI and DiscII for oligosaccharides were rationalized from the different structures obtained by either X-ray crystallography or molecular modeling.
[Mh] Termos MeSH primário: Dictyostelium/metabolismo
Lectinas/química
Lectinas/metabolismo
Monossacarídeos/metabolismo
Oligossacarídeos/metabolismo
Proteínas de Protozoários/química
Proteínas de Protozoários/metabolismo
[Mh] Termos MeSH secundário: Clonagem Molecular
Cristalografia por Raios X
Dictyostelium/química
Discoidinas
Escherichia coli/genética
Expressão Gênica
Cinética
Ligação Proteica
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Discoidins); 0 (Lectins); 0 (Monosaccharides); 0 (Oligosaccharides); 0 (Protozoan Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1007
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100629
[St] Status:MEDLINE
[do] DOI:10.1016/j.jmb.2010.05.042



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