Base de dados : MEDLINE
Pesquisa : D08.811.913.696.620.682.700.140 [Categoria DeCS]
Referências encontradas : 999 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 100 ir para página                         

  1 / 999 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27630263
[Au] Autor:Snowdon C; Johnston M
[Ad] Endereço:Department of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, CO 80045.
[Ti] Título:A novel role for yeast casein kinases in glucose sensing and signaling.
[So] Source:Mol Biol Cell;27(21):3369-3375, 2016 Nov 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Yeasts have sophisticated signaling pathways for sensing glucose, their preferred carbon source, to regulate its uptake and metabolism. One of these is the sensor/receptor-repressor (SRR) pathway, which detects extracellular glucose and transmits an intracellular signal that induces expression of HXT genes. The yeast casein kinases (Ycks) are key players in this pathway. Our model of the SRR pathway had the Ycks functioning downstream of the glucose sensors, transmitting the signal from the sensors to the Mth1 and Std1 corepressors that are required for repression of HXT gene expression. However, we found that overexpression of Yck1 fails to restore glucose signaling in a glucose sensor mutant. Conversely, overexpression of a glucose sensor suppresses the signaling defect of a yck mutant. These results suggest that the Ycks act upstream or at the level of the glucose sensors. Indeed, we found that the glucose sensor Rgt2 is phosphorylated on Yck consensus sites in its C-terminal tail in a Yck-dependent manner and that this phosphorylation is required for corepressor binding and ultimately HXT expression. This leads to a revised model of the SRR pathway in which the Ycks prime a site on the cytoplasmic tails of the glucose sensors to promote binding of the corepressors.
[Mh] Termos MeSH primário: Caseína Quinases/metabolismo
Proteínas Facilitadoras de Transporte de Glucose/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Caseína Quinase I/metabolismo
Proteínas de Ligação a DNA/metabolismo
Regulação Fúngica da Expressão Gênica/efeitos dos fármacos
Glucose/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas de Membrana/metabolismo
Proteínas de Transporte de Monossacarídeos/genética
Fosforilação
Saccharomyces cerevisiae/metabolismo
Transdução de Sinais/efeitos dos fármacos
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (DNA-Binding Proteins); 0 (Glucose Transport Proteins, Facilitative); 0 (Intracellular Signaling Peptides and Proteins); 0 (MTH1 protein, S cerevisiae); 0 (Membrane Proteins); 0 (Monosaccharide Transport Proteins); 0 (RGT2 protein, S cerevisiae); 0 (STD1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); EC 2.7.11.1 (Casein Kinase I); EC 2.7.11.1 (Casein Kinases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE


  2 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27513568
[Au] Autor:Peter T; Bissinger R; Lang F
[Ad] Endereço:Department of Cardiology, Vascular Medicine and Physiology, Eberhard-Karls-University of Tuebingen, Tuebingen, Germany.
[Ti] Título:Stimulation of Eryptosis by Caspofungin.
[So] Source:Cell Physiol Biochem;39(3):939-49, 2016.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: The echinocandin antifungal agent caspofungin has been shown to trigger apoptosis of fungal cells. Beyond that, caspofungin is toxic for host mitochondria. Even though lacking mitochondria, erythrocytes may enter apoptosis-like suicidal erythrocyte death or eryptosis, characterized by cell shrinkage and cell membrane scrambling with phosphatidylserine translocation to the erythrocyte surface. Signaling involved in triggering of eryptosis include increase of cytosolic Ca2+ activity ([Ca2+]i), oxidative stress, ceramide, caspase activation and/or activation of p38 kinase, protein kinase C, and casein kinase. The present study explored, whether caspofungin induces eryptosis and, if so, to shed some light on the cellular mechanisms involved. METHODS: Flow cytometry was employed to determine phosphatidylserine exposure at the cell surface from annexin-V-binding, cell volume from forward scatter, [Ca2+]i from Fluo3-fluorescence, ROS formation from DCFDA dependent fluorescence, and ceramide abundance utilizing specific antibodies. Hemolysis was quantified from hemoglobin concentration in the supernatant. RESULTS: A 48 hours exposure of human erythrocytes to caspofungin (≥ 30 µg/ml) significantly increased the percentage of annexin-V-binding cells, significantly decreased forward scatter, significantly enhanced hemolysis, but did not significantly increase Fluo3-fluorescence, DCFDA fluorescence or ceramide abundance. The effect of caspofungin on annexin-V-binding was not significantly blunted by removal of extracellular Ca2+, by inhibition of caspases with pancaspase inhibitor zVAD (10 µM), or by addition of the antioxidant N-acetyl-cysteine (1 mM), p38 kinase inhibitor SB203580 (2 µM) or protein kinase C inhibitor staurosporine (1 µM). The effect of caspofungin on annexin-V-binding was, however, significantly blunted in the presence of casein kinase inhibitor D4476 (10 µM). CONCLUSIONS: Caspofungin triggers cell shrinkage and phospholipid scrambling of the erythrocyte cell membrane, an effect possibly involving activation of casein kinase.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Cálcio/metabolismo
Equinocandinas/farmacologia
Eriptose/efeitos dos fármacos
Eritrócitos/efeitos dos fármacos
Lipopeptídeos/farmacologia
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Acetilcisteína/farmacologia
Compostos de Anilina
Anexina A5
Caseína Quinases/antagonistas & inibidores
Caseína Quinases/genética
Caseína Quinases/metabolismo
Caspases/genética
Caspases/metabolismo
Células Cultivadas
Ceramidas/metabolismo
Eritrócitos/química
Eritrócitos/citologia
Citometria de Fluxo
Fluoresceínas
Corantes Fluorescentes
Expressão Gênica
Hemólise/efeitos dos fármacos
Seres Humanos
Oligopeptídeos/farmacologia
Estresse Oxidativo
Fosfatidilserinas/metabolismo
Proteína Quinase C/antagonistas & inibidores
Proteína Quinase C/genética
Proteína Quinase C/metabolismo
Inibidores de Proteínas Quinases/farmacologia
Xantenos
Proteínas Quinases p38 Ativadas por Mitógeno/antagonistas & inibidores
Proteínas Quinases p38 Ativadas por Mitógeno/genética
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aniline Compounds); 0 (Annexin A5); 0 (Antifungal Agents); 0 (Ceramides); 0 (Echinocandins); 0 (Fluoresceins); 0 (Fluorescent Dyes); 0 (Lipopeptides); 0 (Oligopeptides); 0 (Phosphatidylserines); 0 (Protein Kinase Inhibitors); 0 (Reactive Oxygen Species); 0 (Xanthenes); 0 (benzyloxycarbonyl-valyl-alanyl-aspartic acid); 2044-85-1 (diacetyldichlorofluorescein); 23D4W0B50Y (Fluo-3); EC 2.7.11.1 (Casein Kinases); EC 2.7.11.13 (Protein Kinase C); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.4.22.- (Caspases); F0XDI6ZL63 (caspofungin); SY7Q814VUP (Calcium); WYQ7N0BPYC (Acetylcysteine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170202
[Lr] Data última revisão:
170202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160812
[St] Status:MEDLINE
[do] DOI:10.1159/000447802


  3 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
[PMID]:26617721
[Au] Autor:Chen H; Xu Y; Wang J; Zhao W; Ruan H
[Ad] Endereço:Department of Emergency, Shanghai Tenth People's Hospital, Tongji University School of Medicine 301 Yanchang Road, Shanghai 200072, China.
[Ti] Título:Baicalin ameliorates isoproterenol-induced acute myocardial infarction through iNOS, inflammation and oxidative stress in rat.
[So] Source:Int J Clin Exp Pathol;8(9):10139-47, 2015.
[Is] ISSN:1936-2625
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Baicalin belongs to glucuronic acid glycosides and after hydrolysis baicalein and glucuronic acid come into being. It has such effects as clearing heat and removing toxicity, anti-inflammation, choleresis, bringing high blood pressure down, diuresis, anti-allergic reaction and so on. In this study, we investigated whether baicalin ameliorates isoproterenol-induced acute myocardial infarction and its mechanism. Rat model of acute myocardial infarction was induced by isoproterenol. Casein kinase (CK), the MB isoenzyme of creatine kinase (CK-MB), lactate dehydrogenase (LDH), cardiac troponin T (cTnT) and infarct size measurement were used to measure the protective effect of baicalin on isoproterenol-induced acute myocardial infarction. iNOS protein expression in rat was analyzed using western blot analysis. Tumor necrosis factor-alpha (TNF-α), interleukin 6 (IL-6), malondialdehyde (MDA) and superoxide dismutase (SOD) and caspase-3 activation levels were explored using commercial ELISA kits. In the acute myocardial infarction experiment, baicalin effectively ameliorates the level of CK, CK-MB, LDH and cTnT, reduced infarct size in acute myocardial infarction rat model. Meanwhile, treatment with baicalin effectively decreased the iNOS protein expression, inflammatory factors and oxidative stresses in a rat model of acute myocardial infarction. However, baicalin emerged that anti-apoptosis activity and suppressed the activation of caspase-3 in a rat model of acute myocardial infarction. The data suggest that the protective effect of baicalin ameliorates isoproterenol-induced acute myocardial infarction through iNOS, inflammation and oxidative stress in rat.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/uso terapêutico
Flavonoides/uso terapêutico
Infarto do Miocárdio/tratamento farmacológico
Óxido Nítrico Sintase Tipo II/metabolismo
Estresse Oxidativo/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Caseína Quinases/sangue
Caspase 3/metabolismo
Creatina Quinase Forma MB/sangue
Inibidores Enzimáticos/farmacologia
Flavonoides/farmacologia
Inflamação/tratamento farmacológico
Inflamação/metabolismo
Interleucina-6/sangue
Isoproterenol
L-Lactato Desidrogenase/sangue
Masculino
Malondialdeído/sangue
Infarto do Miocárdio/induzido quimicamente
Infarto do Miocárdio/metabolismo
Ratos
Ratos Wistar
Superóxido Dismutase/sangue
Troponina T/metabolismo
Fator de Necrose Tumoral alfa/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Flavonoids); 0 (Interleukin-6); 0 (Troponin T); 0 (Tumor Necrosis Factor-alpha); 347Q89U4M5 (baicalin); 4Y8F71G49Q (Malondialdehyde); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.15.1.1 (Superoxide Dismutase); EC 2.7.11.1 (Casein Kinases); EC 2.7.3.2 (Creatine Kinase, MB Form); EC 3.4.22.- (Caspase 3); L628TT009W (Isoproterenol)
[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:151201
[St] Status:MEDLINE


  4 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26372956
[Au] Autor:Dick SA; Chang NC; Dumont NA; Bell RA; Putinski C; Kawabe Y; Litchfield DW; Rudnicki MA; Megeney LA
[Ad] Endereço:Regenerative Medicine Program, Sprott Center for Stem Cell Research, Ottawa Hospital Research Institute, Ottawa, ON, Canada K1H 8L6; Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON, Canada K1H 8L6;
[Ti] Título:Caspase 3 cleavage of Pax7 inhibits self-renewal of satellite cells.
[So] Source:Proc Natl Acad Sci U S A;112(38):E5246-52, 2015 Sep 22.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Compensatory growth and regeneration of skeletal muscle is dependent on the resident stem cell population, satellite cells (SCs). Self-renewal and maintenance of the SC niche is coordinated by the paired-box transcription factor Pax7, and yet continued expression of this protein inhibits the myoblast differentiation program. As such, the reduction or removal of Pax7 may denote a key prerequisite for SCs to abandon self-renewal and acquire differentiation competence. Here, we identify caspase 3 cleavage inactivation of Pax7 as a crucial step for terminating the self-renewal process. Inhibition of caspase 3 results in elevated Pax7 protein and SC self-renewal, whereas caspase activation leads to Pax7 cleavage and initiation of the myogenic differentiation program. Moreover, in vivo inhibition of caspase 3 activity leads to a profound disruption in skeletal muscle regeneration with an accumulation of SCs within the niche. We have also noted that casein kinase 2 (CK2)-directed phosphorylation of Pax7 attenuates caspase-directed cleavage. Together, these results demonstrate that SC fate is dependent on opposing posttranslational modifications of the Pax7 protein.
[Mh] Termos MeSH primário: Caspase 3/metabolismo
Músculo Esquelético/metabolismo
Fator de Transcrição PAX7/metabolismo
Células Satélites de Músculo Esquelético/citologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Caseína Quinases/metabolismo
Diferenciação Celular
Linhagem da Célula
Células Cultivadas
Imuno-Histoquímica
Camundongos
Camundongos Endogâmicos C57BL
Dados de Sequência Molecular
Fosforilação
Proteínas Recombinantes/metabolismo
Regeneração
Homologia de Sequência de Aminoácidos
Células-Tronco/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (PAX7 Transcription Factor); 0 (Pax7 protein, mouse); 0 (Recombinant Proteins); EC 2.7.11.1 (Casein Kinases); EC 3.4.22.- (Casp3 protein, mouse); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150916
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1512869112


  5 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25862939
[Au] Autor:Slone SR; Lavalley N; McFerrin M; Wang B; Yacoubian TA
[Ad] Endereço:Center for Neurodegeneration and Experimental Therapeutics, Department of Neurology, University of Alabama at Birmingham, Birmingham, AL, USA.
[Ti] Título:Increased 14-3-3 phosphorylation observed in Parkinson's disease reduces neuroprotective potential of 14-3-3 proteins.
[So] Source:Neurobiol Dis;79:1-13, 2015 Jul.
[Is] ISSN:1095-953X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:14-3-3 proteins are key regulators of cell survival. We have previously demonstrated that 14-3-3 levels are decreased in an alpha-synuclein (αsyn) mouse model of Parkinson's disease (PD), and that overexpression of certain 14-3-3 isoforms is protective in several PD models. Here we examine whether changes in 14-3-3 phosphorylation may contribute to the neurodegenerative process in PD. We examine three key 14-3-3 phosphorylation sites that normally regulate 14-3-3 function, including serine 58 (S58), serine 184 (S184), and serine/threonine 232 (S/T232), in several models of PD and in human PD brain. We observed that an increase in S232 phosphorylation is observed in rotenone-treated neuroblastoma cells, in cells overexpressing αsyn, and in human PD brains. Alterations in S58 phosphorylation were less consistent in these models, and we did not observe any phosphorylation changes at S184. Phosphorylation at S232 induced by rotenone is reduced by casein kinase inhibitors, and is not dependent on αsyn. Mutation of the S232 site affected 14-3-3θ's neuroprotective effects against rotenone and 1-methyl-4-phenylpyridinium (MPP(+)), with the S232D mutant lacking any protective effect compared to wildtype or S232A 14-3-3θ. The S232D mutant partially reduced the ability of 14-3-3θ to inhibit Bax activation in response to rotenone. Based on these findings, we propose that phosphorylation of 14-3-3s at serine 232 contributes to the neurodegenerative process in PD.
[Mh] Termos MeSH primário: Proteínas 14-3-3/metabolismo
Doença de Parkinson/metabolismo
Transtornos Parkinsonianos/metabolismo
[Mh] Termos MeSH secundário: 1-Metil-4-fenilpiridínio
Proteínas 14-3-3/genética
Animais
Caseína Quinases/antagonistas & inibidores
Caseína Quinases/metabolismo
Linhagem Celular Tumoral
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HEK293
Hipocampo/metabolismo
Seres Humanos
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Fosforilação/efeitos dos fármacos
Proteínas Serina-Treonina Quinases/metabolismo
Rotenona
Lobo Temporal/metabolismo
alfa-Sinucleína/genética
alfa-Sinucleína/metabolismo
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (14-3-3 Proteins); 0 (BAX protein, human); 0 (SNCA protein, human); 0 (alpha-Synuclein); 0 (bcl-2-Associated X Protein); 03L9OT429T (Rotenone); 147336-22-9 (Green Fluorescent Proteins); EC 2.7.11.1 (Casein Kinases); EC 2.7.11.1 (LRRK2 protein, human); EC 2.7.11.1 (Leucine-Rich Repeat Serine-Threonine Protein Kinase-2); EC 2.7.11.1 (Lrrk2 protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); R865A5OY8J (1-Methyl-4-phenylpyridinium)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150412
[St] Status:MEDLINE


  6 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24825444
[Au] Autor:Venerando A; Ruzzene M; Pinna LA
[Ti] Título:Casein kinase: the triple meaning of a misnomer.
[So] Source:Biochem J;460(2):141-56, 2014 Jun 01.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The term 'casein kinase' has been widely used for decades to denote protein kinases sharing the ability to readily phosphorylate casein in vitro. These fall into three main classes: two of them, later renamed as protein kinases CK1 (casein kinase 1, also known as CKI) and CK2 (also known as CKII), are pleiotropic members of the kinome functionally unrelated to casein, whereas G-CK, or genuine casein kinase, responsible for the phosphorylation of casein in the Golgi apparatus of the lactating mammary gland, has only been identified recently with Fam20C [family with sequence similarity 20C; also known as DMP-4 (dentin matrix protein-4)], a member of the four-jointed family of atypical protein kinases, being responsible for the phosphorylation of many secreted proteins. In hindsight, therefore, the term 'casein kinase' is misleading in every instance; in the case of CK1 and CK2, it is because casein is not a physiological substrate, and in the case of G-CK/Fam20C/DMP-4, it is because casein is just one out of a plethora of its targets, and a rather marginal one at that. Strikingly, casein kinases altogether, albeit representing a minimal proportion of the whole kinome, appear to be responsible for the generation of up to 40-50% of non-redundant phosphosites currently retrieved in human phosphopeptides database. In the present review, a short historical explanation will be provided accounting for the usage of the same misnomer to denote three unrelated classes of protein kinases, together with an update of our current knowledge of these pleiotropic enzymes, sharing the same misnomer while playing very distinct biological roles.
[Mh] Termos MeSH primário: Caseína Quinases/metabolismo
[Mh] Termos MeSH secundário: Caseína Quinase I
Caseína Quinase II/metabolismo
Caseína Quinases/classificação
Caseínas/metabolismo
Proteínas da Matriz Extracelular/metabolismo
Feminino
Complexo de Golgi/enzimologia
Seres Humanos
Lactação
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Caseins); 0 (Extracellular Matrix Proteins); EC 2.7.11.1 (Casein Kinase I); EC 2.7.11.1 (Casein Kinase II); EC 2.7.11.1 (Casein Kinases); EC 2.7.11.1 (FAM20C protein, human)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140515
[St] Status:MEDLINE
[do] DOI:10.1042/BJ20140178


  7 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24434535
[Au] Autor:Sfeir C; Fang PA; Jayaraman T; Raman A; Xiaoyuan Z; Beniash E
[Ad] Endereço:University of Pittsburgh, School of Dental Medicine, McGowan Institute of Regenerative Medicine, Center for Craniofacial Regeneration, 552 Salk Hall, 3501 Terrace St., Pittsburgh, PA 15261, USA. Electronic address: csfeir@pitt.edu.
[Ti] Título:Synthesis of bone-like nanocomposites using multiphosphorylated peptides.
[So] Source:Acta Biomater;10(5):2241-9, 2014 May.
[Is] ISSN:1878-7568
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:There is a great need for novel materials for mineralized tissue repair and regeneration. Two examples of such tissue, bone and dentin, are highly organized hierarchical nanocomposites in which mineral and organic phases interface at the molecular level. In contrast, current graft materials are either ceramic powders or physical blends of mineral and organic phases with mechanical properties far inferior to those of their target tissues. The objective of this study was to synthesize composite nanofibrils with highly integrated organic/inorganic phases inspired by the mineralized collagen fibrils of bone and dentin. Utilizing our understanding of bone and dentin biomineralization, we have first designed bioinspired peptides containing 3 Ser-Ser-Asp repeat motifs based on the highly phosphorylated protein, dentin phosphophoryn (DPP), found in dentin and alveolar bone. We demonstrate that up to 80% of serines in the peptide can be phosphorylated by casein kinases. We further tested the ability of these peptides to induce biomimetic calcium phosphate mineralization of collagen fibrils. Our mineralization studies have revealed that in the presence of these phosphorylated peptides, mineralized collagen fibrils structurally similar to the mineralized collagen fibrils of bone and dentin were formed. Our results demonstrate that using phosphorylated DPP-inspired peptides, we can successfully synthesize biomimetic composite nanofibrils with integrated organic and inorganic phases. These results provide the first step in the development of biomimetic nanostructured materials for mineralized tissue repair and regeneration using phosphopeptides.
[Mh] Termos MeSH primário: Osso e Ossos/metabolismo
Nanocompostos/química
Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Animais
Calcificação Fisiológica
Caseína Quinases/metabolismo
Elétrons
Colágenos Fibrilares/metabolismo
Cinética
Espectrometria de Massas
Dados de Sequência Molecular
Peptídeos/síntese química
Peptídeos/química
Fosforilação
Ratos
Tomografia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Fibrillar Collagens); 0 (Peptides); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.11.1 (Casein Kinases)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140118
[St] Status:MEDLINE


  8 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24148232
[Au] Autor:Halcsik E; Forni MF; Fujita A; Verano-Braga T; Jensen ON; Sogayar MC
[Ti] Título:New insights in osteogenic differentiation revealed by mass spectrometric assessment of phosphorylated substrates in murine skin mesenchymal cells.
[So] Source:BMC Cell Biol;14:47, 2013 Oct 22.
[Is] ISSN:1471-2121
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Bone fractures and loss represent significant costs for the public health system and often affect the patients quality of life, therefore, understanding the molecular basis for bone regeneration is essential. Cytokines, such as IL-6, IL-10 and TNFα, secreted by inflammatory cells at the lesion site, at the very beginning of the repair process, act as chemotactic factors for mesenchymal stem cells, which proliferate and differentiate into osteoblasts through the autocrine and paracrine action of bone morphogenetic proteins (BMPs), mainly BMP-2. Although it is known that BMP-2 binds to ActRI/BMPR and activates the SMAD 1/5/8 downstream effectors, little is known about the intracellular mechanisms participating in osteoblastic differentiation. We assessed differences in the phosphorylation status of different cellular proteins upon BMP-2 osteogenic induction of isolated murine skin mesenchymal stem cells using Triplex Stable Isotope Dimethyl Labeling coupled with LC/MS. RESULTS: From 150 µg of starting material, 2,264 proteins were identified and quantified at five different time points, 235 of which are differentially phosphorylated. Kinase motif analysis showed that several substrates display phosphorylation sites for Casein Kinase, p38, CDK and JNK. Gene ontology analysis showed an increase in biological processes related with signaling and differentiation at early time points after BMP2 induction. Moreover, proteins involved in cytoskeleton rearrangement, Wnt and Ras pathways were found to be differentially phosphorylated during all timepoints studied. CONCLUSIONS: Taken together, these data, allow new insights on the intracellular substrates which are phosphorylated early on during differentiation to BMP2-driven osteoblastic differentiation of skin-derived mesenchymal stem cells.
[Mh] Termos MeSH primário: Proteína Morfogenética Óssea 2/genética
Regulação da Expressão Gênica
Células Mesenquimais Estromais/metabolismo
Osteoblastos/metabolismo
Fosfoproteínas/genética
Pele/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteína Morfogenética Óssea 2/metabolismo
Caseína Quinases/genética
Caseína Quinases/metabolismo
Diferenciação Celular
Quinases Ciclina-Dependentes/genética
Quinases Ciclina-Dependentes/metabolismo
MAP Quinase Quinase 4/genética
MAP Quinase Quinase 4/metabolismo
Espectrometria de Massas
Células Mesenquimais Estromais/citologia
Camundongos
Osteoblastos/citologia
Fosfoproteínas/metabolismo
Fosforilação
Transdução de Sinais
Pele/citologia
Proteínas Wnt/genética
Proteínas Wnt/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/genética
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
Proteínas ras/genética
Proteínas ras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bmp2 protein, mouse); 0 (Bone Morphogenetic Protein 2); 0 (Phosphoproteins); 0 (Wnt Proteins); EC 2.7.11.1 (Casein Kinases); EC 2.7.11.22 (Cyclin-Dependent Kinases); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 2.7.12.2 (MAP Kinase Kinase 4); EC 3.6.5.2 (ras Proteins)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:150422
[Lr] Data última revisão:
150422
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131024
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2121-14-47


  9 / 999 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24120734
[Au] Autor:Zhou N; Zhang J; Feng L; Lu B; Wang Z; Sun R; Wu C; Bao J
[Ad] Endereço:School of Life Sciences & Key Laboratory of Bio-resources, Ministry of Education, Sichuan University, Chengdu 610064, China.
[Ti] Título:IntApop: a web service for predicting apoptotic protein interactions in humans.
[So] Source:Biosystems;114(3):238-44, 2013 Dec.
[Is] ISSN:1872-8324
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Apoptosis, a type of cell death, is necessary for maintaining tissue homeostasis and removing malignant cells. Interrupted apoptosis process contributes to carcinogenesis, developmental defects, autoimmune diseases and neurological disorders. Due to the complexity of the process, the molecular dynamics and relative interactions of individual proteins responsible for the activation or inhibition of apoptosis should be researched systematically. In this study, we integrate known protein interactions from databases DIP, IntAct, MINT, HPRD and BioGRID by Naïve Bayes classifier. The receiver operation characteristic (ROC) curve with the area under the ROC curve (AUC) of 0.797 indicates it has a good performance in prediction. Then, we predict the global human apoptotic protein interactions network. Within it, we not only identify the already known interactions of caspases (caspase-8/-10, caspase-9, caspase-3/-6/-7) and Bcl-2 family, but also reveal that Bid can interact with casein kinases (CSK21/22/2B, KC1A, KC1E); both of B2LA1 and B2CL2 can interact with Bid, Bax and Bak; caspase-8 interacts with autophagic proteins (MLP3B, MLP3A and LRRk2). Consequently, we make an initial step to develop the web service IntApop that provides an appropriate platform for apoptosis researchers, systems biologists and translational clinician scientists to predict apoptotic protein interactions in human. In addition, the interaction network can be visualized online, making it a widely applicable systems biology tool for apoptosis and cancer researchers.
[Mh] Termos MeSH primário: Proteínas Reguladoras de Apoptose/metabolismo
Apoptose/fisiologia
Mapas de Interação de Proteínas/fisiologia
Software
Biologia de Sistemas/métodos
[Mh] Termos MeSH secundário: Área Sob a Curva
Proteína Agonista de Morte Celular de Domínio Interatuante com BH3/metabolismo
Caseína Quinases/metabolismo
Caspases/metabolismo
Bases de Dados de Proteínas
Seres Humanos
Internet
Mapas de Interação de Proteínas/genética
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Curva ROC
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Apoptosis Regulatory Proteins); 0 (BH3 Interacting Domain Death Agonist Protein); 0 (BID protein, human); 0 (Proto-Oncogene Proteins c-bcl-2); EC 2.7.11.1 (Casein Kinases); EC 3.4.22.- (Caspases)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:131122
[Lr] Data última revisão:
131122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131015
[St] Status:MEDLINE


  10 / 999 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:23754375
[Au] Autor:Xiao J; Tagliabracci VS; Wen J; Kim SA; Dixon JE
[Ad] Endereço:Department of Pharmacology, University of California at San Diego, La Jolla, CA 92093, USA.
[Ti] Título:Crystal structure of the Golgi casein kinase.
[So] Source:Proc Natl Acad Sci U S A;110(26):10574-9, 2013 Jun 25.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The family with sequence similarity 20 (Fam20) kinases phosphorylate extracellular substrates and play important roles in biomineralization. Fam20C is the Golgi casein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Mutations in Fam20C cause Raine syndrome, an osteosclerotic bone dysplasia. Here we report the crystal structure of the Fam20C ortholog from Caenorhabditis elegans. The nucleotide-free and Mn/ADP-bound structures unveil an atypical protein kinase-like fold and highlight residues critical for activity. The position of the regulatory αC helix and the lack of an activation loop indicate an architecture primed for efficient catalysis. Furthermore, several distinct elements, including the presence of disulfide bonds, suggest that the Fam20 family diverged early in the evolution of the protein kinase superfamily. Our results reinforce the structural diversity of protein kinases and have important implications for patients with disorders of biomineralization.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/química
Caseína Quinases/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Caenorhabditis elegans/enzimologia
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Caseína Quinase I
Caseína Quinases/genética
Caseína Quinases/metabolismo
Cristalografia por Raios X
Proteínas da Matriz Extracelular/química
Proteínas da Matriz Extracelular/genética
Complexo de Golgi/enzimologia
Seres Humanos
Modelos Moleculares
Dados de Sequência Molecular
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Extracellular Matrix Proteins); EC 2.7.11.1 (Casein Kinase I); EC 2.7.11.1 (Casein Kinases); EC 2.7.11.1 (FAM20C protein, human)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130612
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1309211110



página 1 de 100 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde