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Pesquisa : D08.811.277.352.650.775.400.500 [Categoria DeCS]
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[PMID]:29275231
[Au] Autor:Pastor M; Fernández-Calle R; Di Geronimo B; Vicente-Rodríguez M; Zapico JM; Gramage E; Coderch C; Pérez-García C; Lasek AW; Puchades-Carrasco L; Pineda-Lucena A; de Pascual-Teresa B; Herradón G; Ramos A
[Ad] Endereço:Departamento de Química y Bioquímica, Facultad de Farmacia, Universidad San Pablo-CEU, CEU Universities, Urbanización Montepríncipe, 28925, Alcorcón, Madrid, Spain.
[Ti] Título:Development of inhibitors of receptor protein tyrosine phosphatase ß/ζ (PTPRZ1) as candidates for CNS disorders.
[So] Source:Eur J Med Chem;144:318-329, 2018 Jan 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:A new series of blood-brain barrier permeable molecules designed to mimic the activity of Pleiotrophin in the CNS has been designed and synthesized. These compounds exert their action by interacting with the intracellular domain PD1 of the Protein Tyrosine-Phosphatase Receptor Z1 (PTPRZ1), and inhibiting its tyrosine phosphatase activity. The most potent compounds 10a and 12b (IC = 0,1 µM) significantly increase the phosphorylation of key tyrosine residues of PTPRZ1 substrates involved in neuronal survival and differentiation, and display protective effects against amphetamine-induced toxicity. Docking and molecular dynamics experiments have been used to analyze the binding mode and to explain the observed selectivity against PTP1B. An In vivo experiment has demonstrated that 10a can cross the BBB, thus promoting the possibility of moving forward these candidates for the development of drugs for the treatment of CNS disorders, such as drug addiction and neurodegenerative diseases.
[Mh] Termos MeSH primário: Anti-Inflamatórios não Esteroides/farmacologia
Proteínas de Transporte/farmacologia
Doenças do Sistema Nervoso Central/tratamento farmacológico
Citocinas/farmacologia
Inibidores Enzimáticos/farmacologia
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Anti-Inflamatórios não Esteroides/síntese química
Anti-Inflamatórios não Esteroides/química
Barreira Hematoencefálica/efeitos dos fármacos
Barreira Hematoencefálica/metabolismo
Proteínas de Transporte/síntese química
Proteínas de Transporte/química
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Doenças do Sistema Nervoso Central/metabolismo
Citocinas/síntese química
Citocinas/química
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Seres Humanos
Camundongos
Modelos Moleculares
Estrutura Molecular
Ratos
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Carrier Proteins); 0 (Cytokines); 0 (Enzyme Inhibitors); 134034-50-7 (pleiotrophin); EC 3.1.3.48 (PTPRZ1 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171225
[St] Status:MEDLINE


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[PMID]:28504721
[Au] Autor:Zeng AL; Yan W; Liu YW; Wang Z; Hu Q; Nie E; Zhou X; Li R; Wang XF; Jiang T; You YP
[Ad] Endereço:Department of Neurosurgery, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
[Ti] Título:Tumour exosomes from cells harbouring PTPRZ1-MET fusion contribute to a malignant phenotype and temozolomide chemoresistance in glioblastoma.
[So] Source:Oncogene;36(38):5369-5381, 2017 Sep 21.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Exosomes are carriers of pro-tumorigenic factors that participate in glioblastoma (GBM) progression, and many fusion genes are strong driver mutations in neoplasia and are involved in tumorigenesis. However, the ability of fusion genes to be transduced by exosomes is unknown. We characterized exosomes from GBM cells harbouring and not harbouring PTPRZ1-MET fusion (ZM fusion). We also determined the effect of the exosomes from ZM fusion cells (ZM exosomes) on pro-oncogenic secretions and showed that ZM exosomes are internalized by the recipient cells. In addition, we studied the effect of ZM exosome-mediated intercellular communication in the GBM microenvironment. MET proto-oncogene expression was higher in ZM exosomes. Moreover, phosphorylated MET was detected only in ZM exosomes and not in exosomes released by non-ZM fusion GBM cells. ZM exosomes transferred to non-ZM fusion GBM cells and normal human astrocytes altered gene expression and induced epithelial-mesenchymal transition. The uptake of ZM exosomes also induced an exosome-dependent phenotype defined by GBM cell migration and invasion, neurosphere growth and angiogenesis. In addition, ZM exosomes conferred temozolomide resistance to the GBM cells, and exosome-derived ZM fusion network proteins targeted multiple pro-oncogenic effectors in recipient cells within the GBM microenvironment. Our findings show that exosomes mediate the aggressive character of GBM and demonstrate the role of ZM fusion in the exacerbation of this effect. These findings have possible implications for the foundation of gene fusion-based therapy for managing GBM.
[Mh] Termos MeSH primário: Antineoplásicos Alquilantes/farmacologia
Dacarbazina/análogos & derivados
Exossomos/metabolismo
Glioblastoma/tratamento farmacológico
Proteínas de Fusão Oncogênicas/metabolismo
Proteínas Proto-Oncogênicas c-met/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
[Mh] Termos MeSH secundário: Animais
Comunicação Celular
Linhagem Celular Tumoral
Dacarbazina/farmacologia
Resistência a Medicamentos Antineoplásicos
Glioblastoma/genética
Glioblastoma/metabolismo
Glioblastoma/patologia
Seres Humanos
Masculino
Camundongos Endogâmicos BALB C
Camundongos Nus
Proteínas de Fusão Oncogênicas/genética
Fenótipo
Fosforilação
Proteínas Proto-Oncogênicas c-met/genética
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents, Alkylating); 0 (Oncogene Proteins, Fusion); 7GR28W0FJI (Dacarbazine); EC 2.7.10.1 (MET protein, human); EC 2.7.10.1 (Proto-Oncogene Proteins c-met); EC 3.1.3.48 (PTPRZ1 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5); YF1K15M17Y (temozolomide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2017.134


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[PMID]:27898738
[Au] Autor:Zwicker S; Bureik D; Bosma M; Martinez GL; Almer S; Boström EA
[Ad] Endereço:Department of Dental Medicine, Division of Periodontology, Karolinska Institutet, Huddinge, Sweden.
[Ti] Título:Receptor-Type Protein-Tyrosine Phosphatase ζ and Colony Stimulating Factor-1 Receptor in the Intestine: Cellular Expression and Cytokine- and Chemokine Responses by Interleukin-34 and Colony Stimulating Factor-1.
[So] Source:PLoS One;11(11):e0167324, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Differential intestinal expression of the macrophage growth factors colony stimulating factor-1 (CSF-1), interleukin (IL)-34, and their shared CSF-1 receptor (CSF-1R) in inflammatory bowel disease (IBD) has been shown. Diverse expression between CSF-1 and IL-34, suggest that IL-34 may signal via an alternate receptor. Receptor-type protein-tyrosine phosphatase ζ (PTPRZ1, RPTP-ζ), an additional IL-34 receptor, was recently identified. Here, we aimed to assess PTPRZ1 expression in IBD and non-IBD intestinal biopsies. Further, we aimed to investigate cellular PTPRZ1 and CSF-1R expression, and cytokine- and chemokine responses by IL-34 and CSF-1. The expression of PTPRZ1 was higher in non-IBD colon compared to ileum. PTPRZ1 expression was not altered with inflammation in IBD, however, correlated to IL34, CSF1, and CSF1R. The expression patterns of PTPRZ1 and CSF-1R differed in peripheral blood mononuclear cells (PBMCs), monocytes, macrophages, and intestinal epithelial cell line. PBMCs and monocytes of the same donors responded differently to IL-34 and CSF-1 with altered expression of tumor-necrosis factor α (TNF-α), IL-1ß, interferon γ (IFN-γ), IL-13, IL-8, and monocyte chemotactic protein-1 (MCP-1) levels. This study shows that PTPRZ1 was expressed in bowel tissue. Furthermore, CSF-1R protein was detected in an intestinal epithelial cell line and donor dependently in primary PBMCs, monocytes, and macrophages, and first hints also suggest an expression in these cells for PTPRZ1, which may mediate IL-34 and CSF-1 actions.
[Mh] Termos MeSH primário: Quimiocinas/metabolismo
Citocinas/metabolismo
Interleucinas/metabolismo
Intestinos/metabolismo
Fator Estimulador de Colônias de Macrófagos/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
Receptores de Fator Estimulador das Colônias de Granulócitos e Macrófagos/metabolismo
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Diferenciação Celular/efeitos dos fármacos
Células Cultivadas
Quimiocinas/análise
Quimiocinas/genética
Colo/metabolismo
Citocinas/análise
Citocinas/genética
Ensaio de Imunoadsorção Enzimática
Expressão Gênica/efeitos dos fármacos
Seres Humanos
Íleo/metabolismo
Doenças Inflamatórias Intestinais/metabolismo
Doenças Inflamatórias Intestinais/patologia
Interleucinas/farmacologia
Leucócitos Mononucleares/citologia
Leucócitos Mononucleares/efeitos dos fármacos
Leucócitos Mononucleares/metabolismo
Fator Estimulador de Colônias de Macrófagos/farmacologia
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Monócitos/citologia
Monócitos/efeitos dos fármacos
Monócitos/metabolismo
RNA Mensageiro/metabolismo
Receptores de Fator Estimulador das Colônias de Granulócitos e Macrófagos/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokines); 0 (Cytokines); 0 (Interleukins); 0 (RNA, Messenger); 0 (Receptors, Granulocyte-Macrophage Colony-Stimulating Factor); 0 (interleukin-34, human); 81627-83-0 (Macrophage Colony-Stimulating Factor); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0167324


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[PMID]:27748748
[Au] Autor:International Cancer Genome Consortium PedBrain Tumor Project
[Ti] Título:Recurrent MET fusion genes represent a drug target in pediatric glioblastoma.
[So] Source:Nat Med;22(11):1314-1320, 2016 Nov.
[Is] ISSN:1546-170X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pediatric glioblastoma is one of the most common and most deadly brain tumors in childhood. Using an integrative genetic analysis of 53 pediatric glioblastomas and five in vitro model systems, we identified previously unidentified gene fusions involving the MET oncogene in ∼10% of cases. These MET fusions activated mitogen-activated protein kinase (MAPK) signaling and, in cooperation with lesions compromising cell cycle regulation, induced aggressive glial tumors in vivo. MET inhibitors suppressed MET tumor growth in xenograft models. Finally, we treated a pediatric patient bearing a MET-fusion-expressing glioblastoma with the targeted inhibitor crizotinib. This therapy led to substantial tumor shrinkage and associated relief of symptoms, but new treatment-resistant lesions appeared, indicating that combination therapies are likely necessary to achieve a durable clinical response.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/genética
Glioblastoma/genética
Proteínas de Fusão Oncogênicas/genética
Proteínas Proto-Oncogênicas c-met/genética
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Anilidas/farmacologia
Animais
Neoplasias Encefálicas/tratamento farmacológico
Linhagem Celular Tumoral
Criança
Pré-Escolar
DNA de Neoplasias
Feminino
Glioblastoma/tratamento farmacológico
Seres Humanos
Lactente
Masculino
Camundongos
Camundongos SCID
Proteínas Associadas aos Microtúbulos/genética
Proteínas Quinases Ativadas por Mitógeno
Inibidores de Proteínas Quinases/farmacologia
Inibidores de Proteínas Quinases/uso terapêutico
Proteínas/genética
Proteínas Proto-Oncogênicas c-met/antagonistas & inibidores
Pirazóis/uso terapêutico
Piridinas/uso terapêutico
Quinolinas/farmacologia
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/genética
Análise de Sequência de DNA
Transdução de Sinais
Ensaios Antitumorais Modelo de Xenoenxerto
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anilides); 0 (DNA, Neoplasm); 0 (GSK 1363089); 0 (Microtubule-Associated Proteins); 0 (Oncogene Proteins, Fusion); 0 (Protein Kinase Inhibitors); 0 (Proteins); 0 (Pyrazoles); 0 (Pyridines); 0 (Quinolines); 0 (RNA, Messenger); 0 (TFG protein, human); 0 (cytoplasmic linker protein 115); 53AH36668S (crizotinib); EC 2.7.10.1 (Proto-Oncogene Proteins c-met); EC 2.7.11.24 (Mitogen-Activated Protein Kinases); EC 3.1.3.48 (PTPRZ1 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[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:161108
[St] Status:MEDLINE
[do] DOI:10.1038/nm.4204


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[PMID]:27693125
[Au] Autor:Papadimitriou E; Pantazaka E; Castana P; Tsalios T; Polyzos A; Beis D
[Ad] Endereço:Laboratory of Molecular Pharmacology, Department of Pharmacy, School of Health Sciences, University of Patras, GR26504 Patras, Greece. Electronic address: epapad@upatras.gr.
[Ti] Título:Pleiotrophin and its receptor protein tyrosine phosphatase beta/zeta as regulators of angiogenesis and cancer.
[So] Source:Biochim Biophys Acta;1866(2):252-265, 2016 12.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pleiotrophin (PTN) is a secreted heparin-binding growth factor that through its receptor protein tyrosine phosphatase beta/zeta (RPTPß/ζ) has a significant regulatory effect on angiogenesis and cancer. PTN and RPTPß/ζ are over-expressed in several types of human cancers and regulate important cancer cell functions in vitro and cancer growth in vivo. This review begins with a brief introduction of PTN and the regulation of its expression. PTN receptors are described with special emphasis on RPTPß/ζ, which also interacts with and/or affects the function of other important targets for cancer therapy, such as vascular endothelial growth factor A, α ß and cell surface nucleolin. PTN biological activities related to angiogenesis and cancer are extensively discussed. Finally, up to date approaches of targeting PTN or RPTPß/ζ for cancer treatment are presented. Insights into the regulatory role of PTN/RPTPß/ζ on angiogenesis will be extremely beneficial for future development of alternative anti-angiogenic approaches in cancer therapy.
[Mh] Termos MeSH primário: Proteínas de Transporte/fisiologia
Citocinas/fisiologia
Neoplasias/etiologia
Neovascularização Patológica/etiologia
Neovascularização Fisiológica
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/genética
Citocinas/genética
Regulação da Expressão Gênica
Seres Humanos
Neoplasias/irrigação sanguínea
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Cytokines); 134034-50-7 (pleiotrophin); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


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[PMID]:27548698
[Au] Autor:Mingo J; Erramuzpe A; Luna S; Aurtenetxe O; Amo L; Diez I; Schepens JT; Hendriks WJ; Cortés JM; Pulido R
[Ad] Endereço:Biomarkers in Cancer Unit, Biocruces Health Research Institute, Barakaldo, Spain.
[Ti] Título:One-Tube-Only Standardized Site-Directed Mutagenesis: An Alternative Approach to Generate Amino Acid Substitution Collections.
[So] Source:PLoS One;11(8):e0160972, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Site-directed mutagenesis (SDM) is a powerful tool to create defined collections of protein variants for experimental and clinical purposes, but effectiveness is compromised when a large number of mutations is required. We present here a one-tube-only standardized SDM approach that generates comprehensive collections of amino acid substitution variants, including scanning- and single site-multiple mutations. The approach combines unified mutagenic primer design with the mixing of multiple distinct primer pairs and/or plasmid templates to increase the yield of a single inverse-PCR mutagenesis reaction. Also, a user-friendly program for automatic design of standardized primers for Ala-scanning mutagenesis is made available. Experimental results were compared with a modeling approach together with stochastic simulation data. For single site-multiple mutagenesis purposes and for simultaneous mutagenesis in different plasmid backgrounds, combination of primer sets and/or plasmid templates in a single reaction tube yielded the distinct mutations in a stochastic fashion. For scanning mutagenesis, we found that a combination of overlapping primer sets in a single PCR reaction allowed the yield of different individual mutations, although this yield did not necessarily follow a stochastic trend. Double mutants were generated when the overlap of primer pairs was below 60%. Our results illustrate that one-tube-only SDM effectively reduces the number of reactions required in large-scale mutagenesis strategies, facilitating the generation of comprehensive collections of protein variants suitable for functional analysis.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Primers do DNA/genética
Mutagênese Sítio-Dirigida/métodos
Mutação
Reação em Cadeia da Polimerase/métodos
[Mh] Termos MeSH secundário: Primers do DNA/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Seres Humanos
PTEN Fosfo-Hidrolase/genética
PTEN Fosfo-Hidrolase/metabolismo
Plasmídeos/química
Plasmídeos/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/genética
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
Software
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Primers); EC 3.1.3.48 (PTPRZ1 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0160972


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[PMID]:27539848
[Au] Autor:Nikolaienko RM; Hammel M; Dubreuil V; Zalmai R; Hall DR; Mehzabeen N; Karuppan SJ; Harroch S; Stella SL; Bouyain S
[Ad] Endereço:From the Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110.
[Ti] Título:Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues.
[So] Source:J Biol Chem;291(41):21335-21349, 2016 Oct 07.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein-tyrosine phosphatase receptor type G (RPTPγ/PTPRG) interacts in vitro with contactin-3-6 (CNTN3-6), a group of glycophosphatidylinositol-anchored cell adhesion molecules involved in the wiring of the nervous system. In addition to PTPRG, CNTNs associate with multiple transmembrane proteins and signal inside the cell via cis-binding partners to alleviate the absence of an intracellular region. Here, we use comprehensive biochemical and structural analyses to demonstrate that PTPRG·CNTN3-6 complexes share similar binding affinities and a conserved arrangement. Furthermore, as a first step to identifying PTPRG·CNTN complexes in vivo, we found that PTPRG and CNTN3 associate in the outer segments of mouse rod photoreceptor cells. In particular, PTPRG and CNTN3 form cis-complexes at the surface of photoreceptors yet interact in trans when expressed on the surfaces of apposing cells. Further structural analyses suggest that all CNTN ectodomains adopt a bent conformation and might lie parallel to the cell surface to accommodate these cis and trans binding modes. Taken together, these studies identify a PTPRG·CNTN complex in vivo and provide novel insights into PTPRG- and CNTN-mediated signaling.
[Mh] Termos MeSH primário: Contactinas
Complexos Multiproteicos
Proteínas do Tecido Nervoso
Tecido Nervoso/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Animais
Contactinas/química
Contactinas/genética
Contactinas/metabolismo
Seres Humanos
Camundongos
Modelos Biológicos
Modelos Moleculares
Complexos Multiproteicos/química
Complexos Multiproteicos/genética
Complexos Multiproteicos/metabolismo
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/química
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/genética
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contactins); 0 (Multiprotein Complexes); 0 (Nerve Tissue Proteins); EC 3.1.3.48 (Ptprg protein, mouse); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE


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[PMID]:27511463
[Au] Autor:Boedtkjer E; Matchkov VV; Boedtkjer DM; Aalkjaer C
[Ad] Endereço:Department of Biomedicine, Aarhus University, Denmark;
[Ti] Título:Negative News: Cl- and HCO3- in the Vascular Wall.
[So] Source:Physiology (Bethesda);31(5):370-83, 2016 09.
[Is] ISSN:1548-9221
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cl(-) and HCO3 (-) are the most prevalent membrane-permeable anions in the intra- and extracellular spaces of the vascular wall. Outwardly directed electrochemical gradients for Cl(-) and HCO3 (-) permit anion channel opening to depolarize vascular smooth muscle and endothelial cells. Transporters and channels for Cl(-) and HCO3 (-) also modify vascular contractility and structure independently of membrane potential. Transport of HCO3 (-) regulates intracellular pH and thereby modifies the activity of enzymes, ion channels, and receptors. There is also evidence that Cl(-) and HCO3 (-) transport proteins affect gene expression and protein trafficking. Considering the extensive implications of Cl(-) and HCO3 (-) in the vascular wall, it is critical to understand how these ions are transported under physiological conditions and how disturbances in their transport can contribute to disease development. Recently, sensing mechanisms for Cl(-) and HCO3 (-) have been identified in the vascular wall where they modify ion transport and vasomotor function, for instance, during metabolic disturbances. This review discusses current evidence that transport (e.g., via NKCC1, NBCn1, Ca(2+)-activated Cl(-) channels, volume-regulated anion channels, and CFTR) and sensing (e.g., via WNK and RPTPγ) of Cl(-) and HCO3 (-) influence cardiovascular health and disease.
[Mh] Termos MeSH primário: Bicarbonatos/metabolismo
Cloretos/metabolismo
Transporte de Íons
Proteínas de Membrana Transportadoras/metabolismo
Músculo Liso Vascular/metabolismo
[Mh] Termos MeSH secundário: Animais
Canais de Cloreto/metabolismo
Regulador de Condutância Transmembrana em Fibrose Cística/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
Camundongos
Músculo Liso Vascular/enzimologia
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
Simportadores de Sódio-Bicarbonato/metabolismo
Membro 2 da Família 12 de Carreador de Soluto/metabolismo
Canais de Ânion Dependentes de Voltagem/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Bicarbonates); 0 (Chloride Channels); 0 (Chlorides); 0 (Membrane Transport Proteins); 0 (SLC4A7 protein, human); 0 (Sodium-Bicarbonate Symporters); 0 (Solute Carrier Family 12, Member 2); 0 (Voltage-Dependent Anion Channels); 126880-72-6 (Cystic Fibrosis Transmembrane Conductance Regulator); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170317
[Lr] Data última revisão:
170317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160812
[St] Status:MEDLINE
[do] DOI:10.1152/physiol.00001.2016


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[PMID]:27445335
[Au] Autor:Kuboyama K; Fujikawa A; Suzuki R; Tanga N; Noda M
[Ad] Endereço:From the Division of Molecular Neurobiology, National Institute for Basic Biology (NIBB) and.
[Ti] Título:Role of Chondroitin Sulfate (CS) Modification in the Regulation of Protein-tyrosine Phosphatase Receptor Type Z (PTPRZ) Activity: PLEIOTROPHIN-PTPRZ-A SIGNALING IS INVOLVED IN OLIGODENDROCYTE DIFFERENTIATION.
[So] Source:J Biol Chem;291(35):18117-28, 2016 08 26.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein-tyrosine phosphatase receptor type Z (PTPRZ) is predominantly expressed in the developing brain as a CS proteoglycan. PTPRZ has long (PTPRZ-A) and short type (PTPRZ-B) receptor forms by alternative splicing. The extracellular CS moiety of PTPRZ is required for high-affinity binding to inhibitory ligands, such as pleiotrophin (PTN), midkine, and interleukin-34; however, its functional significance in regulating PTPRZ activity remains obscure. We herein found that protein expression of CS-modified PTPRZ-A began earlier, peaking at approximately postnatal days 5-10 (P5-P10), and then that of PTN peaked at P10 at the developmental stage corresponding to myelination onset in the mouse brain. Ptn-deficient mice consistently showed a later onset of the expression of myelin basic protein, a major component of the myelin sheath, than wild-type mice. Upon ligand application, PTPRZ-A/B in cultured oligodendrocyte precursor cells exhibited punctate localization on the cell surface instead of diffuse distribution, causing the inactivation of PTPRZ and oligodendrocyte differentiation. The same effect was observed with the removal of CS chains with chondroitinase ABC but not polyclonal antibodies against the extracellular domain of PTPRZ. These results indicate that the negatively charged CS moiety prevents PTPRZ from spontaneously clustering and that the positively charged ligand PTN induces PTPRZ clustering, potentially by neutralizing electrostatic repulsion between CS chains. Taken altogether, these data indicate that PTN-PTPRZ-A signaling controls the timing of oligodendrocyte precursor cell differentiation in vivo, in which the CS moiety of PTPRZ receptors maintains them in a monomeric active state until its ligand binding.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Diferenciação Celular
Sulfatos de Condroitina/metabolismo
Citocinas/metabolismo
Células-Tronco Neurais/metabolismo
Oligodendroglia/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/genética
Sulfatos de Condroitina/genética
Citocinas/genética
Seres Humanos
Camundongos
Camundongos Mutantes
Células-Tronco Neurais/citologia
Oligodendroglia/citologia
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Cytokines); 134034-50-7 (pleiotrophin); 9007-28-7 (Chondroitin Sulfates); EC 3.1.3.48 (PTPRZ1 protein, human); EC 3.1.3.48 (Ptprz1 protein, mouse); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160723
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.742536


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[PMID]:27374750
[Au] Autor:Reinehr S; Reinhard J; Wiemann S; Stute G; Kuehn S; Woestmann J; Dick HB; Faissner A; Joachim SC
[Ad] Endereço:Experimental Eye Research Institute, University Eye Hospital, Ruhr-University Bochum, Bochum, Germany.
[Ti] Título:Early remodelling of the extracellular matrix proteins tenascin-C and phosphacan in retina and optic nerve of an experimental autoimmune glaucoma model.
[So] Source:J Cell Mol Med;20(11):2122-2137, 2016 Nov.
[Is] ISSN:1582-4934
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glaucoma is characterized by the loss of retinal ganglion cells (RGCs) and optic nerve fibres. Previous studies noted fewer RGCs after immunization with ocular antigens at 28 days. It is known that changes in extracellular matrix (ECM) components conduct retina and optic nerve degeneration. Here, we focused on the remodelling of tenascin-C and phosphacan/receptor protein tyrosine phosphatase ß/ζ in an autoimmune glaucoma model. Rats were immunized with optic nerve homogenate (ONA) or S100B protein (S100). Controls received sodium chloride (Co). After 14 days, no changes in RGC number were noted in all groups. An increase in GFAP mRNA expression was observed in the S100 group, whereas no alterations were noted via immunohistochemistry in both groups. Extracellular matrix remodelling was analyzed after 3, 7, 14 and 28 days. Tenascin-C and 473HD immunoreactivity in retinae and optic nerves was unaltered in both immunized groups at 3 days. At 7 days, tenascin-C staining increased in both tissues in the ONA group. Also, in the optic nerves of the S100 group, an intense tenascin-C staining could be shown. In the retina, an increased tenascin-C expression was also observed in ONA animals via Western blot. 473HD immunoreactivity was elevated in the ONA group in both tissues and in the S100 optic nerves at 7 days. At 14 days, tenascin-C and 473HD immunoreactivity was up-regulated in the ONA retinae, whereas phosphacan expression was up-regulated in both groups. We conclude that remodelling of tenascin-C and phosphacan occurred shortly after immunization, already before RGC loss. We assume that both ECM molecules represent early indicators of neurodegeneration.
[Mh] Termos MeSH primário: Doenças Autoimunes/metabolismo
Glaucoma/metabolismo
Nervo Óptico/metabolismo
Proteínas Tirosina Fosfatases Classe 5 Semelhantes a Receptores/metabolismo
Retina/metabolismo
Tenascina/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos/metabolismo
Doenças Autoimunes/patologia
Contagem de Células
Modelos Animais de Doenças
Glaucoma/patologia
Masculino
Neuroglia/metabolismo
Nervo Óptico/patologia
Ratos Endogâmicos Lew
Retina/patologia
Células Ganglionares da Retina/metabolismo
Células Ganglionares da Retina/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Tenascin); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160705
[St] Status:MEDLINE
[do] DOI:10.1111/jcmm.12909



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