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Pesquisa : D12.776.395.550.200.250.325.200 [Categoria DeCS]
Referências encontradas : 240 [refinar]
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[PMID]:28358866
[Au] Autor:Bhattacharyya S; Bhakta M; Munshi NV
[Ad] Endereço:Department of Internal Medicine (Cardiology Division), UT Southwestern Medical Center, Dallas, TX, United States of America.
[Ti] Título:Phenotypically silent Cre recombination within the postnatal ventricular conduction system.
[So] Source:PLoS One;12(3):e0174517, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cardiac conduction system (CCS) is composed of specialized cardiomyocytes that initiate and maintain cardiac rhythm. Any perturbation to the normal sequence of electrical events within the heart can result in cardiac arrhythmias. To understand how cardiac rhythm is established at the molecular level, several genetically modified mouse lines expressing Cre recombinase within specific CCS compartments have been created. In general, Cre driver lines have been generated either by homologous recombination of Cre into an endogenous locus or Cre expression driven by a randomly inserted transgene. However, haploinsufficiency of the endogenous gene compromises the former approach, while position effects negatively impact the latter. To address these limitations, we generated a Cre driver line for the ventricular conduction system (VCS) that preserves endogenous gene expression by targeting the Contactin2 (Cntn2) 3' untranslated region (3'UTR). Here we show that Cntn23'UTR-IRES-Cre-EGFP/+ mice recombine floxed alleles within the VCS and that Cre expression faithfully recapitulates the spatial distribution of Cntn2 within the heart. We further demonstrate that Cre expression initiates after birth with preservation of native Cntn2 protein. Finally, we show that Cntn23'UTR-IRES-Cre-EGFP/+ mice maintain normal cardiac mechanical and electrical function. Taken together, our results establish a novel VCS-specific Cre driver line without the adverse consequences of haploinsufficiency or position effects. We expect that our new mouse line will add to the accumulating toolkit of CCS-specific mouse reagents and aid characterization of the cell-autonomous molecular circuitry that drives VCS maintenance and function.
[Mh] Termos MeSH primário: Arritmias Cardíacas/genética
Síndrome de Brugada/genética
Contactina 2/genética
Sistema de Condução Cardíaco
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Arritmias Cardíacas/fisiopatologia
Síndrome de Brugada/fisiopatologia
Doença do Sistema de Condução Cardíaco
Contactina 2/biossíntese
Modelos Animais de Doenças
Marcação de Genes
Haploinsuficiência/genética
Ventrículos do Coração/metabolismo
Ventrículos do Coração/fisiopatologia
Recombinação Homóloga/genética
Seres Humanos
Integrases/genética
Camundongos
Camundongos Transgênicos
Miócitos Cardíacos/metabolismo
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Cntn2 protein, mouse); 0 (Contactin 2); EC 2.7.7.- (Cre recombinase); EC 2.7.7.- (Integrases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174517


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[PMID]:27575893
[Au] Autor:Gandomi N; Varshochian R; Atyabi F; Ghahremani MH; Sharifzadeh M; Amini M; Dinarvand R
[Ad] Endereço:a Department of Pharmaceutics, Faculty of Pharmacy , Tehran University of Medical Sciences , Tehran , Iran.
[Ti] Título:Solid lipid nanoparticles surface modified with anti-Contactin-2 or anti-Neurofascin for brain-targeted delivery of medicines.
[So] Source:Pharm Dev Technol;22(3):426-435, 2017 May.
[Is] ISSN:1097-9867
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Multiple sclerosis (MS) is a chronic central nervous system (CNS) inflammation. Efficient drug delivery to brain is however hampered by blood-brain barrier (BBB). In order to have highly efficient and safe delivery of drugs to brain, solid lipid nanoparticles (SLNs) have indicated promising potentials as smart carriers that can pass the blood-brain barrier and deliver therapeutic biomolecules to the brain. In this study, PEGylated SLNs surface modified using anti-Contactin-2 or anti-Neurofascin, two axo-glial-glycoprotein antigens located in node of Ranvier, were prepared. These targeting moieties are considered as the main targets of autoimmune reaction in MS. The targeted SLNs were then characterized and their in vitro release profile together with their cell viability and uptake were studied. Their brain uptakes were also probed following injections in MS-induced mice. It was found that the targeted PEGylated SLNs had no significant cytotoxicity on U87MG cells although their cellular uptake was increased 4- and 8-fold when surface modified with anti-Contactin-2 or anti-Neurofascin, respectively, compared to control. Brain uptake results demonstrated higher uptake of surface-modified SLNs in the brain tissue compared with the PEGylated SLNs. The results of this report will help scientist to design more efficient nanocarriers for treatment of MS.
[Mh] Termos MeSH primário: Anti-Inflamatórios/administração & dosagem
Encéfalo/metabolismo
Moléculas de Adesão Celular/antagonistas & inibidores
Contactina 2/antagonistas & inibidores
Portadores de Fármacos/química
Metilprednisolona/administração & dosagem
Nanopartículas/química
Fatores de Crescimento Neural/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Anti-Inflamatórios/farmacocinética
Anti-Inflamatórios/uso terapêutico
Anticorpos Monoclonais/química
Encéfalo/efeitos dos fármacos
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Modelos Animais de Doenças
Endocitose/efeitos dos fármacos
Seres Humanos
Metilprednisolona/farmacocinética
Metilprednisolona/uso terapêutico
Camundongos Endogâmicos C57BL
Microscopia Confocal
Microscopia Eletrônica de Varredura
Esclerose Múltipla/tratamento farmacológico
Esclerose Múltipla/metabolismo
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Antibodies, Monoclonal); 0 (Cell Adhesion Molecules); 0 (Contactin 2); 0 (Drug Carriers); 0 (NFASC protein, human); 0 (Nerve Growth Factors); X4W7ZR7023 (Methylprednisolone)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170320
[Lr] Data última revisão:
170320
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160831
[St] Status:MEDLINE
[do] DOI:10.1080/10837450.2016.1226901


  3 / 240 MEDLINE  
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[PMID]:27621318
[Au] Autor:Lu Z; Reddy MV; Liu J; Kalichava A; Liu J; Zhang L; Chen F; Wang Y; Holthauzen LM; White MA; Seshadrinathan S; Zhong X; Ren G; Rudenko G
[Ad] Endereço:From the Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
[Ti] Título:Molecular Architecture of Contactin-associated Protein-like 2 (CNTNAP2) and Its Interaction with Contactin 2 (CNTN2).
[So] Source:J Biol Chem;291(46):24133-24147, 2016 Nov 11.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Contactin-associated protein-like 2 (CNTNAP2) is a large multidomain neuronal adhesion molecule implicated in a number of neurological disorders, including epilepsy, schizophrenia, autism spectrum disorder, intellectual disability, and language delay. We reveal here by electron microscopy that the architecture of CNTNAP2 is composed of a large, medium, and small lobe that flex with respect to each other. Using epitope labeling and fragments, we assign the F58C, L1, and L2 domains to the large lobe, the FBG and L3 domains to the middle lobe, and the L4 domain to the small lobe of the CNTNAP2 molecular envelope. Our data reveal that CNTNAP2 has a very different architecture compared with neurexin 1α, a fellow member of the neurexin superfamily and a prototype, suggesting that CNTNAP2 uses a different strategy to integrate into the synaptic protein network. We show that the ectodomains of CNTNAP2 and contactin 2 (CNTN2) bind directly and specifically, with low nanomolar affinity. We show further that mutations in CNTNAP2 implicated in autism spectrum disorder are not segregated but are distributed over the whole ectodomain. The molecular shape and dimensions of CNTNAP2 place constraints on how CNTNAP2 integrates in the cleft of axo-glial and neuronal contact sites and how it functions as an organizing and adhesive molecule.
[Mh] Termos MeSH primário: Contactina 2/química
Proteínas de Membrana/química
Modelos Moleculares
Proteínas do Tecido Nervoso/química
[Mh] Termos MeSH secundário: Contactina 2/genética
Contactina 2/metabolismo
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Ligação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CNTN2 protein, human); 0 (CNTNAP2 protein, human); 0 (Contactin 2); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160914
[St] Status:MEDLINE


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[PMID]:26996997
[Au] Autor:Wright S; Geerts AT; Jol-van der Zijde CM; Jacobson L; Lang B; Waters P; van Tol MJ; Stroink H; Neuteboom RF; Brouwer OF; Vincent A
[Ad] Endereço:Nuffield Department of Clinical Neurosciences, John Radcliffe University Hospital, University of Oxford, Oxford, United Kingdom.
[Ti] Título:Neuronal antibodies in pediatric epilepsy: Clinical features and long-term outcomes of a historical cohort not treated with immunotherapy.
[So] Source:Epilepsia;57(5):823-31, 2016 May.
[Is] ISSN:1528-1167
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: In autoimmune encephalitis the etiologic role of neuronal cell-surface antibodies is clear; patients diagnosed and treated early have better outcomes. Neuronal antibodies have also been described in patients with pediatric epilepsy without encephalitis. The aim was to assess whether antibody presence had any effect on long-term outcomes in these patients. METHODS: Patients (n = 178) were recruited between 1988 and 1992 as part of the prospective Dutch Study of Epilepsy in Childhood; none received immunotherapy. Healthy age-matched bone-marrow donors served as controls (n = 112). All sera were tested for serum N-methyl-d-aspartate receptor (NMDAR), alpha amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor, leucine rich glioma inactivated 1, contactin associated protein like 2 (CASPR2), contactin-2, glutamic acid decarboxylase, and voltage gated potassium channel (VGKC)-complex antibodies by standard techniques. No cerebrospinal fluid (CSF) samples were available. Results were correlated with clinical data collected over 15 years. RESULTS: Seventeen patients (9.5%) were positive for VGKC complex (n = 3), NMDAR (n = 7), CASPR2 (n = 4), and contactin-2 (n = 3), compared to three (3/112; 2.6%) healthy controls (VGKC complex [n = 1], NMDAR [n = 2]; p = 0.03; Fisher's exact test). Titers were relatively low (≤1:100 for cell-surface antibodies), but 8 (47%) of the 17 positive samples bound to the surface of live hippocampal neurons consistent with a potential pathogenic antibody. Preexisting cognitive impairment was more frequent in antibody-positive patients (9/17 vs. 33/161; p = 0.01). Fourteen antibody-positive patients were treated with standard antiepileptic drugs (AEDs); three (17%) became intractable but this was not different from the 16 (10%) of 161 antibody-negative patients. In 96 patients with available follow-up samples at 6 and/or 12 months, 6 of 7 positive antibodies had disappeared and, conversely, antibodies had appeared for the first time in a further 7 patients. SIGNIFICANCE: Neuronal antibodies were found at low levels in 9.5% of patients with new-onset pediatric epilepsy but did not necessarily persist over time, and the development of antibodies de novo in later samples suggests they could be due to a secondary response to neuronal damage or inflammation. Moreover, as the response to standard AEDs and the long-term outcome did not differ from those of antibody-negative pediatric patients, these findings suggest that routine neuronal antibody testing is unlikely to be helpful in pediatric epilepsy. However, the higher incidence of preexisting cognitive problems in the antibody-positive group, the CASPR2 and contactin-2 antibodies in 7 of 17 patients, and the binding of 8 of 17 of serum samples to live hippocampal neurons suggest that neuronal antibodies, even if secondary, could contribute to the comorbidities of pediatric epilepsy.
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Epilepsia/sangue
Epilepsia/diagnóstico
Proteínas do Tecido Nervoso/imunologia
[Mh] Termos MeSH secundário: Adolescente
Criança
Pré-Escolar
Estudos de Coortes
Contactina 2/imunologia
Epilepsia/classificação
Feminino
Glutamato Descarboxilase/imunologia
Seres Humanos
Lactente
Recém-Nascido
Masculino
Proteínas de Membrana/imunologia
Países Baixos
Canais de Potássio de Abertura Dependente da Tensão da Membrana/imunologia
Receptores de N-Metil-D-Aspartato/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (CNTNAP2 protein, human); 0 (Contactin 2); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (Potassium Channels, Voltage-Gated); 0 (Receptors, N-Methyl-D-Aspartate); EC 4.1.1.15 (Glutamate Decarboxylase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160322
[St] Status:MEDLINE
[do] DOI:10.1111/epi.13356


  5 / 240 MEDLINE  
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[PMID]:26840208
[Au] Autor:Hivert B; Pinatel D; Labasque M; Tricaud N; Goutebroze L; Faivre-Sarrailh C
[Ad] Endereço:Aix-Marseille Université, CNRS, Centre de Recherche en Neurobiologie et Neurophysiologie de Marseille-UMR7286, Marseille, France.
[Ti] Título:Assembly of juxtaparanodes in myelinating DRG culture: Differential clustering of the Kv1/Caspr2 complex and scaffolding protein 4.1B.
[So] Source:Glia;64(5):840-52, 2016 May.
[Is] ISSN:1098-1136
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The precise distribution of ion channels at the nodes of Ranvier is essential for the efficient propagation of action potentials along myelinated axons. The voltage-gated potassium channels Kv1.1/1.2 are clustered at the juxtaparanodes in association with the cell adhesion molecules, Caspr2 and TAG-1 and the scaffolding protein 4.1B. In the present study, we set up myelinating cultures of DRG neurons and Schwann cells to look through the formation of juxtaparanodes in vitro. We showed that the Kv1.1/Kv1.2 channels were first enriched at paranodes before being restricted to distal paranodes and juxtaparanodes. In addition, the Kv1 channels displayed an asymmetric expression enriched at the distal juxtaparanodes. Caspr2 was strongly co-localized with Kv1.2 whereas the scaffolding protein 4.1B was preferentially recruited at paranodes while being present at juxtaparanodes too. Kv1.2/Caspr2 but not 4.1B, also transiently accumulated within the nodal region both in myelinated cultures and developing sciatic nerves. Studying cultures and sciatic nerves from 4.1B KO mice, we further showed that 4.1B is required for the proper targeting of Caspr2 early during myelination. Moreover, using adenoviral-mediated expression of Caspr-GFP and photobleaching experiments, we analyzed the stability of paranodal junctions and showed that the lateral stability of paranodal Caspr was not altered in 4.1B KO mice indicating that 4.1B is not required for the assembly and stability of the paranodal junctions. Thus, developing an adapted culture paradigm, we provide new insights into the dynamic and differential distribution of Kv1 channels and associated proteins during myelination.
[Mh] Termos MeSH primário: Gânglios Espinais/citologia
Canal de Potássio Kv1.1/metabolismo
Proteínas dos Microfilamentos/metabolismo
Nós Neurofibrosos/metabolismo
Células de Schwann/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Contactina 2/metabolismo
Venenos Elapídicos/farmacocinética
Embrião de Mamíferos
Recuperação de Fluorescência Após Fotodegradação
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Canal de Potássio Kv1.1/genética
Canal de Potássio Kv1.2/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Proteínas dos Microfilamentos/genética
Modelos Biológicos
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Ligação Proteica
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CNTNAP2 protein, mouse); 0 (Cntn2 protein, mouse); 0 (Contactin 2); 0 (Elapid Venoms); 0 (Epb4.1l3 protein, mouse); 0 (Kv1.2 Potassium Channel); 0 (Membrane Proteins); 0 (Microfilament Proteins); 0 (Nerve Tissue Proteins); 147173-20-4 (Kv1.1 Potassium Channel); 147336-22-9 (Green Fluorescent Proteins); 74811-93-1 (dendrotoxin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160204
[St] Status:MEDLINE
[do] DOI:10.1002/glia.22968


  6 / 240 MEDLINE  
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[PMID]:26718491
[Au] Autor:Yan Y; Jiang Y
[Ad] Endereço:Department of Neurosurgery, The Second Xiangya Hospital of Central South University, Changsha, Hunan 410011, P.R. China.
[Ti] Título:RACK1 affects glioma cell growth and differentiation through the CNTN2-mediated RTK/Ras/MAPK pathway.
[So] Source:Int J Mol Med;37(1):251-7, 2016 Jan.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Receptor for activated C kinase 1 (RACK1) and contactin-2 (CNTN2) are known to be abnormally expressed in gliomas; however, the association between RACK1 and CNTN2, and the effects of RACK1 and CNTN2 on glioma cell differentiation and the related molecular mechanisms remain largely unknown. The present study aimed to investigate the interaction between RACK1 and CNTN2, and to examine whether RACK1/CNTN2/receptor tyrosine kinase (RTK)/Ras/mitogen-activated protein kinase (MAPK) axis plays a role in glioma growth and differentiation. The results from western blot analysis revealed that the protein expression levels of RACK1 and CNTN2 were higher in high­grade glioma tissues and cells, and lower in low-grade glioma tissues and cells. A co-immunoprecipitation assay demonstrated that RACK1 interacts with CNTN2, and RACK1 upregulated the expression of CNTN2. Gain-of­function and loss-of­function experiments indicated that both RACK1 and CNTN2 promoted glioma cell proliferation, inhibited glioma cell differentiation and activated the RTK/Ras/MAPK pathway. However, the effects of RACK1 on glioma cell proliferation, differentiation and the activation of the RTK/Ras/MAPK signaling pathway were abolished by the knockdown of CNTN2 using siRNA. In Therefore, the findings of this study firstly demonstrate that RACK1 interacts with CNTN2, and that the effects of RACK1 on glioma cell growth and differentiation are mediated by CNTN2. The RACK1/CNTN2/RTK/Ras/MAPK axis exists in glioma cells, and it may be a potential therapeutic target in gliomas.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/metabolismo
Encéfalo/patologia
Proliferação Celular
Contactina 2/metabolismo
Proteínas de Ligação ao GTP/metabolismo
Glioma/metabolismo
Proteínas de Neoplasias/metabolismo
Receptores de Superfície Celular/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Adulto
Idoso
Encéfalo/metabolismo
Neoplasias Encefálicas/patologia
Linhagem Celular Tumoral
Feminino
Glioma/patologia
Seres Humanos
Sistema de Sinalização das MAP Quinases
Masculino
Meia-Idade
Mapas de Interação de Proteínas
Receptores Proteína Tirosina Quinases/metabolismo
Receptores de Quinase C Ativada
Proteínas ras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CNTN2 protein, human); 0 (Contactin 2); 0 (Neoplasm Proteins); 0 (RACK1 protein, human); 0 (Receptors for Activated C Kinase); 0 (Receptors, Cell Surface); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.5.2 (ras Proteins)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160101
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2015.2421


  7 / 240 MEDLINE  
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[PMID]:26640242
[Au] Autor:Hashimoto K; Sakane F; Ikeda N; Akiyama A; Sugahara M; Miyamoto Y
[Ad] Endereço:Graduate School of Humanities and Sciences, Ochanomizu University, Otsuka 2-1-1, Bunkyo-ku, Tokyo 112-8610, Japan.
[Ti] Título:Vitronectin promotes the progress of the initial differentiation stage in cerebellar granule cells.
[So] Source:Mol Cell Neurosci;70:76-85, 2016 Jan.
[Is] ISSN:1095-9327
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vitronectin (VN), which is an extracellular matrix protein, is known to be involved in the proliferation and differentiation of primary cultured cerebellar granule cell precursors (CGCPs); however, the effect of VN is not fully understood. In this study, we analyzed the effects of VN loss on the proliferation and differentiation of CGCPs in VN knockout (VNKO) mice in vivo. First, immunohistochemistry showed that VN was distributed in the region from the inner external granule layer (iEGL) through the internal granule layer (IGL) in wild-type (WT) mice. Next, we observed the formation of the cerebellar cortex using sagittal sections of VNKO mice at postnatal days (P) 5, 8 and 11. Loss of VN suppressed the ratio of NeuN, a neuronal differentiation marker, to positive cerebellar granule cells (CGCs) in the external granule layer (EGL) and the ratio of CGCs in the IGL at P8, indicating that the loss of VN suppresses the differentiation into CGCs. However, the loss of VN did not significantly affect the proliferation of CGCPs. Next, the effect of VN loss on the initial differentiation stage of CGCPs was examined. The loss of VN increased the expression levels of Transient axonal glycoprotein 1 (TAG1), a marker of neurons in the initial differentiation stage, in the cerebella of VNKO mice at P5 and 8 and increased the ratio of TAG1-positive cells in the primary culture of VNKO-derived CGCPs, indicating that the loss of VN accumulates the CGCPs in the initial differentiation stage. Taken together, these results demonstrate that VN promotes the progress of the initial differentiation stage of CGCPs.
[Mh] Termos MeSH primário: Diferenciação Celular/fisiologia
Cerebelo/metabolismo
Neurônios/metabolismo
Vitronectina/metabolismo
[Mh] Termos MeSH secundário: Animais
Proliferação Celular/fisiologia
Cerebelo/citologia
Contactina 2/genética
Contactina 2/metabolismo
Camundongos
Camundongos Knockout
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Neurônios/citologia
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Vitronectina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contactin 2); 0 (Nerve Tissue Proteins); 0 (NeuN protein, mouse); 0 (Nuclear Proteins); 0 (Vitronectin)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151208
[St] Status:MEDLINE


  8 / 240 MEDLINE  
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[PMID]:26722394
[Au] Autor:Zhang YZ; Lou JY; Bai HY; Wang YL; Li JF; Yin HL
[Ad] Endereço:Department of Neurology, The Second Affiliated Hospital of Zhengzhou University Zhengzhou, P. R. China.
[Ti] Título:Protective effect of bone marrow mesenchymal stem cells on PC12 cells apoptosis mediated by TAG1.
[So] Source:Int J Clin Exp Pathol;8(10):12093-100, 2015.
[Is] ISSN:1936-2625
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: This study aims to explore the protection effect of bone marrow mesenchymal stem cells (BMSCs) on PC12 cells apoptosis mediated by transient axonal glycoprotein 1 (TAG1). METHODS: PC12 cells were divided into control group, Aß25-35 group and BMSCs + Aß25-35 group. The effects of BMSCs on PC12 cells treated by Aß25-35 were detected using MTT, Hoechst 33258 and Annexin V-FITC/PI staining methods. The expression levels of TAG1, ß-amyloid precursor protein (APP), AICD and p53 were determined by RT-PCR and Western blotting methods. The expression levels of Bax and Bcl-2 were determined by Western blotting method. The activity of Caspase 3 was detected by spectrophotometric method. RESULTS: MTT results showed that cell activity decreased after the treatment of 20 µM Aß25-35 for 48 h (P<0.01) while it increased in BMSCs + Aß25-35 group (P<0.01). Hoechst 33258 and Annexin V-FITC/PI staining results showed that Aß25-35 could induce the apoptosis of PC12 cells while the apoptosis of PC12 cells was inhibited in BMSCs + Aß25-35 group. RT-PCR and Western blotting methods showed that 20 µM Aß25-35 could increase the expression levels of TAG1, APP, AICD and p53 (P<0.01) while they decreased in BMSCs + Aß25-35 group (P<0.01). 20 µM Aß25-35 could increase the expression levels of Bax and decrease the expression levels of Bcl-2 (P<0.01), while the expression levels of Bax decreased and the expression levels of Bcl-2 increase in BMSCs + Aß25-35 group (P<0.01). 20 µM Aß25-35 could enhance Caspase 3 activity while it decreased in BMSCs + Aß25-35 group (P<0.01). Conclusions BMSCs with Aß25-35 could inhibit the apoptosis of PC12 cells, which maybe related with TAG1/APP/AICD signal pathway.
[Mh] Termos MeSH primário: Peptídeos beta-Amiloides/toxicidade
Apoptose/fisiologia
Contactina 2/metabolismo
Células Mesenquimais Estromais/metabolismo
Neurônios/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Western Blotting
Células da Medula Óssea/metabolismo
Técnicas de Cocultura
Citometria de Fluxo
Neurônios/metabolismo
Neurônios/patologia
Células PC12
Ratos
Ratos Sprague-Dawley
Reação em Cadeia da Polimerase em Tempo Real
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Peptides); 0 (Contactin 2)
[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:160102
[St] Status:MEDLINE


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[PMID]:26525675
[Au] Autor:Bastakis GG; Savvaki M; Stamatakis A; Vidaki M; Karagogeos D
[Ad] Endereço:Department of Basic Science, Faculty of Medicine, University of Crete and Institute of Molecular Biology and Biotechnology-FoRTH, Vassilika Vouton, Heraklion, Crete 71110, Greece.
[Ti] Título:Tag1 deficiency results in olfactory dysfunction through impaired migration of mitral cells.
[So] Source:Development;142(24):4318-28, 2015 Dec 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The olfactory system provides mammals with the abilities to investigate, communicate and interact with their environment. These functions are achieved through a finely organized circuit starting from the nasal cavity, passing through the olfactory bulb and ending in various cortical areas. We show that the absence of transient axonal glycoprotein-1 (Tag1)/contactin-2 (Cntn2) in mice results in a significant and selective defect in the number of the main projection neurons in the olfactory bulb, namely the mitral cells. A subpopulation of these projection neurons is reduced in Tag1-deficient mice as a result of impaired migration. We demonstrate that the detected alterations in the number of mitral cells are well correlated with diminished odor discrimination ability and social long-term memory formation. Reduced neuronal activation in the olfactory bulb and the corresponding olfactory cortex suggest that Tag1 is crucial for the olfactory circuit formation in mice. Our results underpin the significance of a numerical defect in the mitral cell layer in the processing and integration of odorant information and subsequently in animal behavior.
[Mh] Termos MeSH primário: Movimento Celular
Contactina 2/deficiência
Bulbo Olfatório/patologia
Bulbo Olfatório/fisiopatologia
[Mh] Termos MeSH secundário: Animais
Contagem de Células
Contactina 2/metabolismo
Camundongos Endogâmicos C57BL
Modelos Biológicos
Bulbo Olfatório/embriologia
Bulbo Olfatório/metabolismo
Neurônios Receptores Olfatórios/metabolismo
Neurônios Receptores Olfatórios/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Contactin 2)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:151216
[Lr] Data última revisão:
151216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151104
[St] Status:MEDLINE
[do] DOI:10.1242/dev.123943


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[PMID]:26070930
[Au] Autor:Kastriti ME; Sargiannidou I; Kleopa KA; Karagogeos D
[Ad] Endereço:Department of Basic Science, Faculty of Medicine, University of Crete, Heraklion, Greece; Institute of Molecular Biology & Biotechnology-FoRTH, Heraklion, Greece.
[Ti] Título:Differential modulation of the juxtaparanodal complex in Multiple Sclerosis.
[So] Source:Mol Cell Neurosci;67:93-103, 2015 Jul.
[Is] ISSN:1095-9327
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myelinated fibers are divided into discrete subdomains around the Nav-enriched nodes of Ranvier: the paranodes, where axoglial interactions occur, the juxtaparanodes, where voltage-gated potassium channels (VGKCs) are aggregated, and the internode. Perinodal changes have been reported in Multiple Sclerosis (MS) with functional consequences for the axon. Here we report on alterations of the juxtaparanodal proteins TAG-1, Caspr2 and VGKCs in normal appearing white matter (NAWM), perilesion and chronic lesion areas in post-mortem white matter tissue from MS patients compared to control white matter. We show that the molecular organization and maintenance of juxtaparanodes is affected in lesions, perilesions and NAWM in chronic MS through protein and mRNA expression as well as immunohistochemistry. The three molecules analyzed were differentially altered. TAG-1 clustering at juxtaparanodes was reduced in NAWM; TAG-1 and Caspr2 are diffused in perilesions and absent in lesion areas. VGKCs were no longer enriched at juxtaparanodes either at the NAWM or the perilesion and demyelinated plaques. While the protein levels of the three molecules showed only a tendency of reduction in the plaques, there was a significant upregulation of Caspr2 mRNA in the lesions accompanied by a transcriptional increase of paranodal Caspr, indicating an axonal homeostatic mechanism.
[Mh] Termos MeSH primário: Esclerose Múltipla/metabolismo
Nós Neurofibrosos/metabolismo
Substância Branca/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Axônios/metabolismo
Estudos de Casos e Controles
Contactina 2/genética
Contactina 2/metabolismo
Feminino
Seres Humanos
Masculino
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Meia-Idade
Esclerose Múltipla/patologia
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Neuroglia/metabolismo
Canais de Potássio de Abertura Dependente da Tensão da Membrana/genética
Canais de Potássio de Abertura Dependente da Tensão da Membrana/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Nós Neurofibrosos/patologia
Substância Branca/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CNTN2 protein, human); 0 (CNTNAP2 protein, human); 0 (Contactin 2); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (Potassium Channels, Voltage-Gated); 0 (RNA, Messenger)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150817
[Lr] Data última revisão:
150817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150614
[St] Status:MEDLINE



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