Base de dados : MEDLINE
Pesquisa : D08.811.277.352.650.775.400.200 [Categoria DeCS]
Referências encontradas : 430 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 43 ir para página                         

  1 / 430 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29348429
[Au] Autor:Goto-Ito S; Yamagata A; Sato Y; Uemura T; Shiroshima T; Maeda A; Imai A; Mori H; Yoshida T; Fukai S
[Ad] Endereço:Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
[Ti] Título:Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation.
[So] Source:Nat Commun;9(1):269, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPδ, PTPσ and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPδ-SALM2 and PTPδ-SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPδ, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPδ. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPδ-SALM5 requires the dimeric property of SALM5.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/química
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/química
Sinapses/metabolismo
Transmissão Sináptica
[Mh] Termos MeSH secundário: Animais
Moléculas de Adesão Celular Neuronais/genética
Moléculas de Adesão Celular Neuronais/metabolismo
Cristalografia por Raios X
Células HEK293
Seres Humanos
Modelos Moleculares
Mutação
Ligação Proteica
Domínios Proteicos
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Multimerização Proteica
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (Protein Isoforms); 0 (SALM5 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02417-z


  2 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29348579
[Au] Autor:Lin Z; Liu J; Ding H; Xu F; Liu H
[Ad] Endereço:State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China.
[Ti] Título:Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation.
[So] Source:Nat Commun;9(1):268, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:SALM5, a synaptic adhesion molecule implicated in autism, induces presynaptic differentiation through binding to the LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) that have been highlighted as presynaptic hubs for synapse formation. The mechanisms underlying SALM5/LAR-RPTP interaction remain unsolved. Here we report crystal structures of human SALM5 LRR-Ig alone and in complex with human PTPδ Ig1-3 (MeA ). Distinct from other LAR-RPTP ligands, SALM5 mainly exists as a dimer with LRR domains from two protomers packed in an antiparallel fashion. In the 2:2 heterotetrameric SALM5/PTPδ complex, a SALM5 dimer bridges two separate PTPδ molecules. Structure-guided mutations and heterologous synapse formation assays demonstrate that dimerization of SALM5 is prerequisite for its functionality in inducing synaptic differentiation. This study presents a structural template for the SALM family and reveals a mechanism for how a synaptic adhesion molecule directly induces cis-dimerization of LAR-RPTPs into higher-order signaling assembly.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
[Mh] Termos MeSH secundário: Baculoviridae
Dimerização
Células HEK293
Seres Humanos
Domínios de Imunoglobulina
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (SALM5 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02414-2


  3 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28637841
[Au] Autor:Nakamura F; Okada T; Shishikura M; Uetani N; Taniguchi M; Yagi T; Iwakura Y; Ohshima T; Goshima Y; Strittmatter SM
[Ad] Endereço:Department of Molecular Pharmacology and Neurobiology, Graduate School of Medicine, Yokohama City University, Yokohama, Kanagawa 236-0004, Japan, f-nakamura@umin.ac.jp stephen.strittmatter@yale.edu.
[Ti] Título:Protein Tyrosine Phosphatase δ Mediates the Sema3A-Induced Cortical Basal Dendritic Arborization through the Activation of Fyn Tyrosine Kinase.
[So] Source:J Neurosci;37(30):7125-7139, 2017 Jul 26.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Leukocyte common antigen-related (LAR) class protein tyrosine phosphatases (PTPs) are critical for axonal guidance; however, their relation to specific guidance cues is poorly defined. We here show that PTP-3, a LAR homolog in , is involved in axon guidance regulated by Semaphorin-2A-signaling. PTPδ, one of the vertebrate LAR class PTPs, participates in the Semaphorin-3A (Sema3A)-induced growth cone collapse response of primary cultured dorsal root ganglion neurons from embryos. , however, the contribution of PTPδ in Sema3A-regualted axon guidance was minimal. Instead, PTPδ played a major role in Sema3A-dependent cortical dendritic growth. δ and mutant mice exhibited poor arborization of basal dendrites of cortical layer V neurons. This phenotype was observed in both male and female mutants. The double-heterozygous mutants, δ , also showed a similar phenotype, indicating the genetic interaction. In δ brains, Fyn and Src kinases were hyperphosphorylated at their C-terminal Tyr527 residues. Sema3A-stimulation induced dephosphorylation of Tyr527 in the dendrites of wild-type cortical neurons but not of δ Arborization of cortical basal dendrites was reduced in as well as in δ double-heterozygous mutants. Collectively, PTPδ mediates Sema3A-signaling through the activation of Fyn by C-terminal dephosphorylation. The relation of leukocyte common antigen-related (LAR) class protein tyrosine phosphatases (PTPs) and specific axon guidance cues is poorly defined. We show that PTP-3, a LAR homolog in , participates in Sema2A-regulated axon guidance. PTPδ, a member of vertebrate LAR class PTPs, is involved in Sema3A-regulated cortical dendritic growth. In Sema3A signaling, PTPδ activates Fyn and Src kinases by dephosphorylating their C-terminal Tyr residues. This is the first evidence showing that LAR class PTPs participate in Semaphorin signaling .
[Mh] Termos MeSH primário: Córtex Cerebral/fisiologia
Dendritos/fisiologia
Plasticidade Neuronal/fisiologia
Proteínas Proto-Oncogênicas c-fyn/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
Semaforina-3A/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Córtex Cerebral/ultraestrutura
Dendritos/ultraestrutura
Ativação Enzimática
Feminino
Regulação Enzimológica da Expressão Gênica/fisiologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Proteínas Tirosina Quinases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sema3a protein, mouse); 0 (Semaphorin-3A); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 2.7.10.2 (Fyn protein, mouse); EC 2.7.10.2 (Proto-Oncogene Proteins c-fyn); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.2519-16.2017


  4 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28509371
[Au] Autor:Konze SA; Cajic S; Oberbeck A; Hennig R; Pich A; Rapp E; Buettner FFR
[Ad] Endereço:Institute of Clinical Biochemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625, Hannover, Germany.
[Ti] Título:Quantitative Assessment of Sialo-Glycoproteins and N-Glycans during Cardiomyogenic Differentiation of Human Induced Pluripotent Stem Cells.
[So] Source:Chembiochem;18(13):1317-1331, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Human induced pluripotent stem-cell-derived cardiomyocytes (hiPSC CMs) may be used in regenerative medicine for individualized tissue transplants in the future. For application in patients, the generated CMs have to be highly pure and well characterized. In order to overcome the prevalent scarcity of CM-specific markers, we quantitatively assessed cell-surface-exposed sialo-glycoproteins and N-glycans of hiPSCs, CM progenitors, and CMs. Applying a combination of metabolic labeling and specific sialo-glycoprotein capture, we could highly enrich and quantify membrane proteins during cardiomyogenic differentiation. Among them we identified a number of novel, putative biomarkers for hiPSC CMs. Analysis of the N-glycome by capillary gel electrophoresis revealed three novel structures comprising ß1,3-linked galactose, α2,6-linked sialic acid and complex fucosylation; these were highly specific for hiPSCs. Bisecting GlcNAc structures strongly increased during differentiation, and we propose that they are characteristic of early, immature CMs.
[Mh] Termos MeSH primário: Membrana Celular/química
Glicômica/métodos
Células-Tronco Pluripotentes Induzidas/química
Miócitos Cardíacos/química
Polissacarídeos/química
[Mh] Termos MeSH secundário: Acetilglucosamina/química
Acetilglucosamina/metabolismo
Sequência de Carboidratos
Diferenciação Celular
Membrana Celular/metabolismo
Subunidade alfa do Receptor do Fator Neutrófico Ciliar/genética
Subunidade alfa do Receptor do Fator Neutrófico Ciliar/metabolismo
Fucose/química
Fucose/metabolismo
Galactose/química
Galactose/metabolismo
Gastrinas/genética
Gastrinas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Células-Tronco Pluripotentes Induzidas/citologia
Células-Tronco Pluripotentes Induzidas/metabolismo
Laminina/genética
Laminina/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Miócitos Cardíacos/citologia
Miócitos Cardíacos/metabolismo
Polissacarídeos/metabolismo
Receptor EphA7/genética
Receptor EphA7/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
Receptores Acoplados a Proteínas-G/genética
Receptores Acoplados a Proteínas-G/metabolismo
Ácidos Siálicos/química
Ácidos Siálicos/metabolismo
Coloração e Rotulagem/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CNTFR protein, human); 0 (Ciliary Neurotrophic Factor Receptor alpha Subunit); 0 (Gastrins); 0 (HEPH protein, human); 0 (LGR4 protein, human); 0 (Laminin); 0 (Membrane Proteins); 0 (Polysaccharides); 0 (Receptors, G-Protein-Coupled); 0 (Sialic Acids); 151186-83-3 (laminin A); 28RYY2IV3F (Fucose); EC 2.7.10.1 (Receptor, EphA7); EC 3.1.3.48 (PTPRD protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2); V956696549 (Acetylglucosamine); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700100


  5 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28345455
[Au] Autor:Szaumkessel M; Wojciechowska S; Janiszewska J; Zemke N; Byzia E; Kiwerska K; Kostrzewska-Poczekaj M; Ustaszewski A; Jarmuz-Szymczak M; Grenman R; Wierzbicka M; Bartochowska A; Szyfter K; Giefing M
[Ad] Endereço:1 Institute of Human Genetics, Polish Academy of Sciences, Poznan, Poland.
[Ti] Título:Recurrent epigenetic silencing of the PTPRD tumor suppressor in laryngeal squamous cell carcinoma.
[So] Source:Tumour Biol;39(3):1010428317691427, 2017 Mar.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular processes like differentiation, mitotic cycle, and cell growth are regulated by tyrosine kinases with known oncogenic potential and tyrosine phosphatases that downmodulate the first. Therefore, tyrosine phosphatases are recurrent targets of gene alterations in human carcinomas. We and others suggested recently a tumor suppressor function of the PTPRD tyrosine phosphatase and reported homozygous deletions of the PTPRD locus in laryngeal squamous cell carcinoma. In this study, we investigated other gene-inactivating mechanisms potentially targeting PTPRD, including loss-of-function mutations and also epigenetic alterations like promoter DNA hypermethylation. We sequenced the PTPRD gene in eight laryngeal squamous cell carcinoma cell lines but did not identify any inactivating mutations. In contrast, by bisulfite pyrosequencing of the gene promoter region, we identified significantly higher levels of methylation (p = 0.001 and p = 0.0002, respectively) in 9/14 (64%) laryngeal squamous cell carcinoma cell lines and 37/79 (47%) of primary laryngeal squamous cell carcinoma tumors as compared to normal epithelium of the upper aerodigestive tract. There was also a strong correlation (p = 0.0001) between methylation and transcriptional silencing for the PTPRD gene observed in a cohort of 497 head and neck tumors from The Cancer Genome Atlas dataset suggesting that DNA methylation is the main mechanism of PTPRD silencing in these tumors. In summary, our data provide further evidence of the high incidence of PTPRD inactivation in laryngeal squamous cell carcinoma. We suggest that deletions and loss-of-function mutations are responsible for PTPRD loss only in a fraction of cases, whereas DNA methylation is the dominating mechanism of PTPRD inactivation.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/genética
Metilação de DNA/genética
Inativação Gênica
Neoplasias de Cabeça e Pescoço/genética
Neoplasias Laríngeas/genética
Regiões Promotoras Genéticas/genética
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Carcinoma de Células Escamosas/patologia
Linhagem Celular Tumoral
Feminino
Deleção de Genes
Neoplasias de Cabeça e Pescoço/patologia
Seres Humanos
Neoplasias Laríngeas/patologia
Masculino
Membrana Mucosa/citologia
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.3.48 (PTPRD protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170407
[Lr] Data última revisão:
170407
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170328
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317691427


  6 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28259897
[Au] Autor:Sun PH; Chen G; Mason M; Jiang WG; Ye L
[Ad] Endereço:Cardiff China Medical Research Collaborative Institute of Cancer and Genetics, Cardiff University School of Medicine, Cardiff, CF14 4XN, UK.
[Ti] Título:Dual roles of protein tyrosine phosphatase kappa in coordinating angiogenesis induced by pro-angiogenic factors.
[So] Source:Int J Oncol;50(4):1127-1135, 2017 Apr.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:A potential role may be played by receptor-type protein tyrosine phosphatase kappa (PTPRK) in angiogenesis due to its critical function in coordinating intracellular signal transduction from various receptors reliant on tyrosine phosphorylation. In the present study, we investigated the involvement of PTPRK in the cellular functions of vascular endothelial cells (HECV) and its role in angiogenesis using in vitro assays and a PTPRK knockdown vascular endothelial cell model. PTPRK knockdown in HECV cells (HECVPTPRKkd) resulted in a decrease of cell proliferation and cell-matrix adhesion; however, increased cell spreading and motility were seen. Reduced focal adhesion kinase (FAK) and paxillin protein levels were seen in the PTPRK knockdown cells which may contribute to the inhibitory effect on adhesion. HECVPTPRKkd cells were more responsive to the treatment of fibroblast growth factor (FGF) in their migration compared with the untreated control and cells treated with VEGF. Moreover, elevated c-Src and Akt1 were seen in the PTPRK knockdown cells. The FGF-promoted cell migration was remarkably suppressed by an addition of PLCγ inhibitor compared with other small inhibitors. Knockdown of PTPRK suppressed the ability of HECV cells to form tubules and also impaired the tubule formation that was induced by FGF and conditioned medium of cancer cells. Taken together, it suggests that PTPRK plays dual roles in coordinating angiogenesis. It plays a positive role in cell proliferation, adhesion and tubule formation, but suppresses cell migration, in particular, the FGF-promoted migration. PTPRK bears potential to be targeted for the prevention of tumour associated angiogenesis.
[Mh] Termos MeSH primário: Células Endoteliais/metabolismo
Neovascularização Patológica/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Adesão Celular
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Fatores de Crescimento de Fibroblastos/metabolismo
Quinase 1 de Adesão Focal/metabolismo
Técnicas de Silenciamento de Genes
Seres Humanos
Paxilina/metabolismo
Fosforilação
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Fator A de Crescimento do Endotélio Vascular/metabolismo
Quinases da Família src/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PXN protein, human); 0 (Paxillin); 0 (VEGFA protein, human); 0 (Vascular Endothelial Growth Factor A); 62031-54-3 (Fibroblast Growth Factors); EC 2.7.10.2 (CSK tyrosine-protein kinase); EC 2.7.10.2 (Focal Adhesion Kinase 1); EC 2.7.10.2 (PTK2 protein, human); EC 2.7.10.2 (src-Family Kinases); EC 2.7.11.1 (AKT1 protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.3.48 (PTPRK protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170306
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2017.3884


  7 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27697534
[Au] Autor:Naito Y; Lee AK; Takahashi H
[Ad] Endereço:Synapse Development and Plasticity, Institut de Recherches Cliniques de Montréal (IRCM), Montreal, Quebec H2W 1R7, Canada; Integrated Program in Neuroscience, McGill University, Montreal, Quebec H3A 2B4, Canada.
[Ti] Título:Emerging roles of the neurotrophin receptor TrkC in synapse organization.
[So] Source:Neurosci Res;116:10-17, 2017 Mar.
[Is] ISSN:1872-8111
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Tropomyosin-receptor-kinase (Trk) receptors have been extensively studied for their roles in kinase-dependent signaling cascades in nervous system development. Synapse organization is coordinated by trans-synaptic interactions of various cell adhesion proteins, a representative example of which is the neurexin-neuroligin complex. Recently, a novel role for TrkC as a synapse organizing protein has been established. Post-synaptic TrkC binds to pre-synaptic type-IIa receptor-type protein tyrosine phosphatase sigma (PTPσ). TrkC-PTPσ specifically induces excitatory synapses in a kinase domain-independent manner. TrkC has distinct extracellular domains for PTPσ- and NT-3-binding and thus may bind both ligands simultaneously. Indeed, NT-3 enhances the TrkC-PTPσ interaction, thus facilitating synapse induction at the pre-synaptic side and increasing pre-synaptic vesicle recycling in a kinase-independent fashion. A crystal structure study has revealed the detailed structure of the TrkC-PTPσ complex as well as competitive modulation of TrkC-mediated synaptogenesis by heparan sulfate proteoglycans (HSPGs), which bind the same domain of TrkC as PTPσ. Thus, there is strong evidence supporting a role for the TrkC-PTPσ complex in mechanisms underlying the fine turning of neural connectivity. Furthermore, disruption of the TrkC-PTPσ complex may be the underlying cause of certain psychiatric disorders caused by mutations in the gene encoding TrkC (NTRK3), supporting its role in cognitive functions.
[Mh] Termos MeSH primário: Receptor trkC/metabolismo
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Encéfalo/ultraestrutura
Técnicas de Cocultura
Fibroblastos/citologia
Fibroblastos/metabolismo
Seres Humanos
Neurônios/citologia
Neurônios/metabolismo
Neurotrofina 3/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
Receptores Pré-Sinápticos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Neurotrophin 3); 0 (Receptors, Presynaptic); EC 2.7.10.1 (Receptor, trkC); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170518
[Lr] Data última revisão:
170518
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161005
[St] Status:MEDLINE


  8 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28044141
[Au] Autor:Nakata M; Zhang B; Yang Y; Okada T; Shintani N; Hashimoto H; Yada T
[Ad] Endereço:Department of Physiology, Division of Integrative Physiology, Jichi Medical University School of Medicine, Shimotsuke, Tochigi 329-0498, Japan.
[Ti] Título:High-Fat Diet Augments VPAC1 Receptor-Mediated PACAP Action on the Liver, Inducing LAR Expression and Insulin Resistance.
[So] Source:J Diabetes Res;2016:9321395, 2016.
[Is] ISSN:2314-6753
[Cp] País de publicação:Egypt
[La] Idioma:eng
[Ab] Resumo:Pituitary adenylate cyclase-activating polypeptide (PACAP) acts on multiple processes of glucose and energy metabolism. PACAP potentiates insulin action in adipocytes and insulin release from pancreatic -cells, thereby enhancing glucose tolerance. Contrary to these effects at organ levels, PACAP null mice exhibit hypersensitivity to insulin. However, this apparent discrepancy remains to be solved. We aimed to clarify the mechanism underlying the antidiabetic phenotype of PACAP null mice. Feeding with high-fat diet (HFD) impaired insulin sensitivity and glucose tolerance in wild type mice, whereas these changes were prevented in PACAP null mice. HFD also impaired insulin-induced Akt phosphorylation in the liver in wild type mice, but not in PACAP null mice. Using GeneFishing method, HFD increased the leukocyte common antigen-related (LAR) protein tyrosine phosphatase in the liver in wild type mice. Silencing of LAR restored the insulin signaling in the liver of HFD mice. Moreover, the increased LAR expression by HFD was prevented in PACAP null mice. HFD increased the expression of VPAC1 receptor (VPAC1-R), one of three PACAP receptors, in the liver of wild type mice. These data indicate that PACAP-VPAC1-R signaling induces LAR expression and insulin resistance in the liver of HFD mice. Antagonism of VPAC1-R may prevent progression of HFD-induced insulin resistance in the liver, providing a novel antidiabetic strategy.
[Mh] Termos MeSH primário: Dieta Hiperlipídica/efeitos adversos
Resistência à Insulina
Fígado/metabolismo
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/farmacologia
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/fisiologia
[Mh] Termos MeSH secundário: Animais
Expressão Gênica/efeitos dos fármacos
Hipoglicemiantes
Fígado/química
Fígado/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos ICR
Camundongos Knockout
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/deficiência
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/genética
RNA Mensageiro/análise
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/antagonistas & inibidores
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hypoglycemic Agents); 0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (RNA, Messenger); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE
[do] DOI:10.1155/2016/9321395


  9 / 430 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27352860
[Au] Autor:Sarhan AR; Patel TR; Cowell AR; Tomlinson MG; Hellberg C; Heath JK; Cunningham DL; Hotchin NA
[Ad] Endereço:School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
[Ti] Título:LAR protein tyrosine phosphatase regulates focal adhesions through CDK1.
[So] Source:J Cell Sci;129(15):2962-71, 2016 Aug 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Focal adhesions are complex multi-molecular structures that link the actin cytoskeleton to the extracellular matrix through integrin adhesion receptors and play a key role in regulation of many cellular functions. LAR (also known as PTPRF) is a receptor protein tyrosine phosphatase that regulates PDGF signalling and localises to focal adhesions. We have observed that loss of LAR phosphatase activity in mouse embryonic fibroblasts results in reduced numbers of focal adhesions and decreased adhesion to fibronectin. To understand how LAR regulates cell adhesion we used phosphoproteomic data, comparing global phosphorylation events in wild-type and LAR phosphatase-deficient cells, to analyse differential kinase activity. Kinase prediction analysis of LAR-regulated phosphosites identified a node of cytoskeleton- and adhesion-related proteins centred on cyclin-dependent kinase-1 (CDK1). We found that loss of LAR activity resulted in reduced activity of CDK1, and that CDK1 activity was required for LAR-mediated focal adhesion complex formation. We also established that LAR regulates CDK1 activity through c-Abl and Akt family proteins. In summary, we have identified a new role for a receptor protein tyrosine phosphatase in regulating CDK1 activity and hence cell adhesion to the extracellular matrix.
[Mh] Termos MeSH primário: Proteína Quinase CDC2/metabolismo
Adesões Focais/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
[Mh] Termos MeSH secundário: Animais
Adesão Celular/efeitos dos fármacos
Fibronectinas/farmacologia
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Adesões Focais/efeitos dos fármacos
Camundongos
Modelos Biológicos
Fosforilação/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-abl/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibronectins); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); EC 2.7.10.2 (Proto-Oncogene Proteins c-abl); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.22 (CDC2 Protein Kinase); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160630
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.191379


  10 / 430 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27335277
[Au] Autor:Spina V; Khiabanian H; Messina M; Monti S; Cascione L; Bruscaggin A; Spaccarotella E; Holmes AB; Arcaini L; Lucioni M; Tabbò F; Zairis S; Diop F; Cerri M; Chiaretti S; Marasca R; Ponzoni M; Deaglio S; Ramponi A; Tiacci E; Pasqualucci L; Paulli M; Falini B; Inghirami G; Bertoni F; Foà R; Rabadan R; Gaidano G; Rossi D
[Ad] Endereço:Division of Hematology, Department of Translational Medicine, Amedeo Avogadro University of Eastern Piedmont, Novara, Italy;
[Ti] Título:The genetics of nodal marginal zone lymphoma.
[So] Source:Blood;128(10):1362-73, 2016 Sep 08.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nodal marginal zone lymphoma (NMZL) is a rare, indolent B-cell tumor that is distinguished from splenic marginal zone lymphoma (SMZL) by the different pattern of dissemination. NMZL still lacks distinct markers and remains orphan of specific cancer gene lesions. By combining whole-exome sequencing, targeted sequencing of tumor-related genes, whole-transcriptome sequencing, and high-resolution single nucleotide polymorphism array analysis, we aimed at disclosing the pathways that are molecularly deregulated in NMZL and we compare the molecular profile of NMZL with that of SMZL. These analyses identified a distinctive pattern of nonsilent somatic lesions in NMZL. In 35 NMZL patients, 41 genes were found recurrently affected in ≥3 (9%) cases, including highly prevalent molecular lesions of MLL2 (also known as KMT2D; 34%), PTPRD (20%), NOTCH2 (20%), and KLF2 (17%). Mutations of PTPRD, a receptor-type protein tyrosine phosphatase regulating cell growth, were enriched in NMZL across mature B-cell tumors, functionally caused the loss of the phosphatase activity of PTPRD, and were associated with cell-cycle transcriptional program deregulation and increased proliferation index in NMZL. Although NMZL shared with SMZL a common mutation profile, NMZL harbored PTPRD lesions that were otherwise absent in SMZL. Collectively, these findings provide new insights into the genetics of NMZL, identify PTPRD lesions as a novel marker for this lymphoma across mature B-cell tumors, and support the distinction of NMZL as an independent clinicopathologic entity within the current lymphoma classification.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/genética
Exoma/genética
Linfoma de Zona Marginal Tipo Células B/genética
Mutação/genética
Receptor Notch2/genética
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Neoplasias Esplênicas/genética
[Mh] Termos MeSH secundário: Sequenciamento de Nucleotídeos em Larga Escala/métodos
Seres Humanos
Linfoma de Zona Marginal Tipo Células B/patologia
Neoplasias Esplênicas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (NOTCH2 protein, human); 0 (Receptor, Notch2); EC 3.1.3.48 (PTPRD protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160624
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-02-696757



página 1 de 43 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