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[PMID]:29267504
[Au] Autor:Mendes GA; Haag T; Trott G; Rech CGSL; Ferreira NP; Oliveira MC; Kohek MB; Pereira-Lima JFS
[Ad] Endereço:Programa de Pós-Graduação em Patologia, Universidade Federal de Ciências da Saúde de Porto Alegre, Porto Alegre, RS, Brasil.
[Ti] Título:Expression of E-cadherin, Slug and NCAM and its relationship to tumor invasiveness in patients with acromegaly.
[So] Source:Braz J Med Biol Res;51(2):e6808, 2017 Dec 11.
[Is] ISSN:1414-431X
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:Pituitary adenomas account for 10-15% of primary intracranial tumors. Growth hormone (GH)-secreting adenomas account for 13% of all pituitary adenomas and cause acromegaly. These tumors can be aggressive, invade surrounding structures and are highly recurrent. The objective of this study was to evaluate E-cadherin, Slug and neural cell adhesion molecule (NCAM) expression in GH-secreting pituitary adenomas and its relationship to tumor invasiveness. A cross-sectional study of patients who underwent hypophysectomy due to GH-secreting pituitary adenoma from April 2007 to December 2014 was carried out. The medical records were reviewed to collect clinical data. Immediately after surgery, tumor samples were frozen in liquid nitrogen and stored in a biofreezer at -80°C for assessment of E-cadherin 1 (CDH1), SLUG (SNAI2), and NCAM (NCAM1) by real-time PCR. The samples were fixed in formalin and embedded in paraffin for immunohistochemical analysis of E-cadherin and NCAM. Thirty-five patients with acromegaly were included in the study. Of these, 65.7% had invasive tumors. Immunohistochemically, E-cadherin was expressed in 96.7% of patients, and NCAM in 80% of patients. There was no statistically significant relationship between tumor grade or invasiveness and immunohistochemical expression of these markers. Regarding gene expression, 50% of cases expressed CDH1, none expressed SNAI2, and 53.3% expressed NCAM1. There was no statistically significant relationship between tumor grade or invasiveness and gene expression of CDH1, SNAI2, and NCAM1. The absence of Slug overexpression and of E-cadherin and NCAM suppression suggests that expression of these markers is not associated with tumor invasiveness in GH-secreting pituitary adenomas.
[Mh] Termos MeSH primário: Acromegalia/patologia
Adenoma/patologia
Caderinas/análise
Moléculas de Adesão de Célula Nervosa/análise
Neoplasias Hipofisárias/patologia
Fatores de Transcrição da Família Snail/análise
[Mh] Termos MeSH secundário: Acromegalia/genética
Acromegalia/metabolismo
Adenoma/química
Adenoma/genética
Adolescente
Adulto
Idoso
Biomarcadores Tumorais/análise
Antígeno CD56/análise
Estudos Transversais
Feminino
Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Masculino
Meia-Idade
Gradação de Tumores
Invasividade Neoplásica
Neoplasias Hipofisárias/química
Neoplasias Hipofisárias/genética
Reação em Cadeia da Polimerase em Tempo Real
Estatísticas não Paramétricas
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CD56 Antigen); 0 (Cadherins); 0 (NCAM1 protein, human); 0 (Neural Cell Adhesion Molecules); 0 (SNAI1 protein, human); 0 (Snail Family Transcription Factors)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE


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[PMID]:29441926
[Au] Autor:Wei Z; Sun X; Xu Q; Zhang Y; Tian F; Sun H; Zheng H; Dai J
[Ti] Título:TAK-242 suppresses lipopolysaccharide-induced inflammation in human coronary artery endothelial cells.
[So] Source:Pharmazie;71(10):583-587, 2016 Oct 01.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:TAK-242 (resatorvid), a novel small-molecule cyclohexene derivative, inhibits TLR4 signaling selectively. TAK-242 blocked the Toll-like receptor (TLR) 4-triggered inflammatory signaling by binding directly to a specific amino acid Cys747 in the intracellular domain of TLR4. The present study was designed to examine the effects of TAK-242 on vascular inflammatory responses in human coronary artery endothelial cells (HCAECs) challenged by lipopolysaccharide (LPS, a TLR4 ligand). The results show that TAK-242 attenuated the LPS-induced expression of interleukin (IL)-6, IL-8 and monocyte chemoattractant protein 1 both at the transcription and translation levels in HCAECs. LPS-induced endothelial cell adhesion molecules, intercellular adhesion molecular-1 and vascular cell adhesion molecule-1 expressions were also reduced by treatment with TAK-242. In addition, coincubation with TAK-242 did not effect the expression of TLR4 in LPS-activated HCAECs. Furthermore, TAK-242 efficiently suppressed LPS-induced phosphorylation of nuclear factor κB (NF-κB) and IL-1 associated kinase-1 (IRAK-1) in HCAECs. These findings show that TAK-242 can suppress endothelial cell inflammation, suggesting that TAK-242 might be suitable for development as a therapeutic agent for inflammatory cardiovascular disease.
[Mh] Termos MeSH primário: Anti-Inflamatórios não Esteroides/farmacologia
Vasos Coronários/efeitos dos fármacos
Células Endoteliais/efeitos dos fármacos
Lipopolissacarídeos/antagonistas & inibidores
Sulfonamidas/farmacologia
[Mh] Termos MeSH secundário: Vasos Coronários/citologia
Citocinas/biossíntese
Citocinas/genética
Regulação da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Inflamação/induzido quimicamente
Inflamação/prevenção & controle
Quinases Associadas a Receptores de Interleucina-1/biossíntese
Quinases Associadas a Receptores de Interleucina-1/genética
NF-kappa B/efeitos dos fármacos
Moléculas de Adesão de Célula Nervosa/biossíntese
Moléculas de Adesão de Célula Nervosa/genética
RNA Mensageiro/biossíntese
Transdução de Sinais/efeitos dos fármacos
Receptor 4 Toll-Like/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Cytokines); 0 (Lipopolysaccharides); 0 (NF-kappa B); 0 (Neural Cell Adhesion Molecules); 0 (RNA, Messenger); 0 (Sulfonamides); 0 (TLR4 protein, human); 0 (Toll-Like Receptor 4); 0 (ethyl 6-(N-(2-chloro-4-fluorophenyl)sulfamoyl)cyclohex-1-ene-1-carboxylate); EC 2.7.11.1 (IRAK1 protein, human); EC 2.7.11.1 (Interleukin-1 Receptor-Associated Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6512


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[PMID]:29050943
[Au] Autor:Ma YC; Zhang L; Dai LL; Khan RU; Zou CG
[Ad] Endereço:State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, Yunnan 650091, China.
[Ti] Título:mir-67 regulates P. aeruginosa avoidance behavior in C. elegans.
[So] Source:Biochem Biophys Res Commun;494(1-2):120-125, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pathogen avoidance behaviors are found throughout the animal kingdom and are important for animal's survival in nature. As a free-living nematode, C. elegans is exposed to a variety of microorganisms, including toxic or pathogenic bacteria, in soil. C. elegans can develop efficient avoidance responses to pathogenic bacteria to minimize the infection risk. However, the role of microRNAs (miRNAs) in pathogen avoidance in C. elegans remains unclear. In this report, we showed that the miRNA mir-67 was involved in a behavioral avoidance response to P. aeruginosa PA14. Exposure to P. aeruginosa PA14 induced the expression of mir-67 in worms. mir-67(n4899) mutants exhibited a reduced ability to avoid P. aeruginosa PA14. By combining quantitative proteomic analysis with miRNA target prediction algorithms, we identified SAX-7/L1CAM, which is transmembrane cell adhesion receptor molecule, as the target of mir-67. Silencing of sax-7 by RNAi on mir-67 mutants rescued avoidance behavioral. Our data demonstrate that the mir-67-SAX-7 pathway modulate the behavioral avoidance response to pathogens, thus providing a new perspective in the role of miRNAs in host-microbe interactions.
[Mh] Termos MeSH primário: Caenorhabditis elegans/genética
Caenorhabditis elegans/fisiologia
MicroRNAs/genética
RNA de Helmintos/genética
[Mh] Termos MeSH secundário: Animais
Aprendizagem da Esquiva/fisiologia
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/fisiologia
Interações Hospedeiro-Patógeno/genética
Interações Hospedeiro-Patógeno/fisiologia
Moléculas de Adesão de Célula Nervosa/genética
Moléculas de Adesão de Célula Nervosa/fisiologia
Pseudomonas aeruginosa/patogenicidade
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (MicroRNAs); 0 (Neural Cell Adhesion Molecules); 0 (RNA, Helminth); 0 (SAX-7 protein, C elegans)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE


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[PMID]:29040270
[Au] Autor:Wylie T; Garg R; Ridley AJ; Conte MR
[Ad] Endereço:Randall Division of Cell and Molecular Biophysics, King's College London, Guy's Campus, London, United Kingdom.
[Ti] Título:Analysis of the interaction of Plexin-B1 and Plexin-B2 with Rnd family proteins.
[So] Source:PLoS One;12(10):e0185899, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Rnd family of proteins, Rnd1, Rnd2 and Rnd3, are atypical Rho family GTPases, which bind to but do not hydrolyse GTP. They interact with plexins, which are receptors for semaphorins, and are hypothesised to regulate plexin signalling. We recently showed that each Rnd protein has a distinct profile of interaction with three plexins, Plexin-B1, Plexin-B2 and Plexin-B3, in mammalian cells, although it is unclear which region(s) of these plexins contribute to this specificity. Here we characterise the binary interactions of the Rnd proteins with the Rho-binding domain (RBD) of Plexin-B1 and Plexin-B2 using biophysical approaches. Isothermal titration calorimetry (ITC) experiments for each of the Rnd proteins with Plexin-B1-RBD and Plexin-B2-RBD showed similar association constants for all six interactions, although Rnd1 displayed a small preference for Plexin-B1-RBD and Rnd3 for Plexin-B2-RBD. Furthermore, mutagenic analysis of Rnd3 suggested similarities in its interaction with both Plexin-B1-RBD and Plexin-B2-RBD. These results suggest that Rnd proteins do not have a clear-cut specificity for different Plexin-B-RBDs, possibly implying the contribution of additional regions of Plexin-B proteins in conferring functional substrate selection.
[Mh] Termos MeSH primário: Proteínas do Tecido Nervoso/metabolismo
Moléculas de Adesão de Célula Nervosa/metabolismo
Receptores de Superfície Celular/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Células COS
Calorimetria/métodos
Cercopithecus aethiops
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Mutação
Proteínas do Tecido Nervoso/genética
Moléculas de Adesão de Célula Nervosa/genética
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Receptores de Superfície Celular/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Termodinâmica
Proteínas rho de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nerve Tissue Proteins); 0 (Neural Cell Adhesion Molecules); 0 (PLXNB1 protein, human); 0 (PLXNB3 protein, human); 0 (RND1 protein, human); 0 (Receptors, Cell Surface); 0 (Recombinant Proteins); 0 (plexin B2 protein, human); EC 3.6.5.2 (RND2 protein, human); EC 3.6.5.2 (RND3 protein, human); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185899


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[PMID]:28969383
[Au] Autor:Zapiec B; Dieriks BV; Tan S; Faull RLM; Mombaerts P; Curtis MA
[Ad] Endereço:Max Planck Research Unit for Neurogenetics, Frankfurt, Germany.
[Ti] Título:A ventral glomerular deficit in Parkinson's disease revealed by whole olfactory bulb reconstruction.
[So] Source:Brain;140(10):2722-2736, 2017 Oct 01.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Olfactory dysfunction is common in Parkinson's disease and is an early symptom, but its pathogenesis remains poorly understood. Hindering progress in our mechanistic understanding of olfactory dysfunction in Parkinson's disease is the paucity of literature about the human olfactory bulb, both from normal and Parkinson's disease cases. Qualitatively it is well established that the neat arrangement of the glomerular array seen in the mouse olfactory bulb is missing in humans. But rigorous quantitative approaches to describe and compare the thousands of glomeruli in the human olfactory bulb are not available. Here we report a quantitative approach to describe the glomerular component of the human olfactory bulb, and its application to draw statistical comparisons between olfactory bulbs from normal and Parkinson's disease cases. We subjected horizontal 10 µm sections of olfactory bulbs from six normal and five Parkinson's disease cases to fluorescence immunohistochemistry with antibodies against vesicular glutamate transporter-2 and neural cell adhesion molecule. We scanned the immunostained sections with a fluorescence slide scanner, segmented the glomeruli, and generated 3D reconstructions of whole olfactory bulbs. We document the occurrence of atypical glomerular morphologies and glomerular-like structures deep in the olfactory bulb, both in normal and Parkinson's disease cases. We define a novel and objective parameter: the global glomerular voxel volume, which is the total volume of all voxels that are classified immunohistochemically as glomerular. We find that the global glomerular voxel volume in Parkinson's disease cases is half that of normal cases. The distribution of glomerular voxels along the dorsal-ventral dimension of the olfactory bulb in these series of horizontal sections is significantly altered in Parkinson's disease cases: whereas most glomerular voxels reside within the ventral half of olfactory bulbs from normal cases, glomerular voxels are more evenly spread among the ventral and dorsal halves of olfactory bulbs from Parkinson's disease cases. These quantitative whole-olfactory bulb analyses indicate a predominantly ventral deficit in the glomerular component in Parkinson's disease, consistent with the olfactory vector hypothesis for the pathogenesis of this neurodegenerative disease. The distribution of serine 129-phosphorylated α-synuclein immunoreactive voxels correlates with that of glomerular voxels. The higher the serine 129-phosphorylated α-synuclein load of an olfactory bulb from a Parkinson's disease case, the lower the global glomerular voxel volume. Our rigorous quantitative approach to the whole olfactory bulb will help understand the anatomy and histology of the normal human olfactory bulb and its pathological alterations in Parkinson's disease.
[Mh] Termos MeSH primário: Transtornos do Olfato/etiologia
Bulbo Olfatório/patologia
Doença de Parkinson/complicações
Doença de Parkinson/patologia
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Feminino
Imunofluorescência
Seres Humanos
Processamento de Imagem Assistida por Computador
Masculino
Meia-Idade
Moléculas de Adesão de Célula Nervosa/metabolismo
Bulbo Olfatório/metabolismo
Tirosina 3-Mono-Oxigenase
Proteína Vesicular 2 de Transporte de Glutamato/metabolismo
alfa-Sinucleína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neural Cell Adhesion Molecules); 0 (Vesicular Glutamate Transport Protein 2); 0 (alpha-Synuclein); EC 1.14.16.2 (Tyrosine 3-Monooxygenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1093/brain/awx208


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[PMID]:28939043
[Au] Autor:Sato Y; Suzuki S; Iijima Y; Iijima T
[Ad] Endereço:Institute of Innovative Science and Technology, Medical Division, Tokai University, Isehara City, Kanagawa, Japan; Department of Chemistry and Bioresource, Faculty of Engineering, Tokai University, Hiratsuka City, Kanagawa, Japan.
[Ti] Título:Neuroligin-induced presynaptic differentiation through SLM2-mediated splicing modifications of neurexin in cerebellar cultures.
[So] Source:Biochem Biophys Res Commun;493(2):1030-1036, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neurexins (NRXs) and neuroligins (NLs) play important roles in synapse specification. The alternatively spliced segment 4 (AS4) of NRX genes (Nrxn) is a critical element in selective trans-synaptic interactions. However, the role of splicing of NRXs and NLs in synapse specification is not fully understood. To investigate the exact role of splice-dependent NRX-NL interaction in the specification of glutamatergic and gamma-aminobutyric acid (GABA)-ergic synapses in the cerebellum, we evaluated the synaptogenic receptor activity of NL1/2/3 isoforms in a neuron-fibroblast co-culture system, in which the Nrxn AS4 segments are manipulated using SLM2, a selective and dominant regulator of AS4 splicing. We show that ectopic SLM2 expression (SLM2 E/E) causes marked skipping of exon 20 of AS4 in cerebellar neuron culture. Whereas NLs can induce VAMP2 presynaptic contacts from mainly glutamatergic neurons in both uninfected (control) and SLM2 E/E co-cultures, they induce VGAT GABAergic contacts in the control culture, but not properly in the SLM2 E/E culture. Furthermore, Nrxn3 is responsible for the NL-induced assembly of GABAergic synapses in co-culture. Importantly, lentivirus-based expression of Nrxn3 containing exon 20 restores the reduced NL-induced GABAergic contacts in the SLM2 E/E co-culture. Therefore, our findings may provide further insights into NRX-NL mediated synapse specification.
[Mh] Termos MeSH primário: Processamento Alternativo
Moléculas de Adesão Celular Neuronais/metabolismo
Cerebelo/citologia
Proteínas de Membrana/metabolismo
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Moléculas de Adesão Celular Neuronais/genética
Células Cultivadas
Cerebelo/metabolismo
Técnicas de Cocultura
Células HEK293
Seres Humanos
Camundongos Endogâmicos ICR
Moléculas de Adesão de Célula Nervosa/genética
Moléculas de Adesão de Célula Nervosa/metabolismo
Neurônios/citologia
Neurônios/metabolismo
Proteínas de Ligação a RNA/genética
Sinapses/metabolismo
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (Cntnap1 protein, mouse); 0 (Khdrbs3 protein, mouse); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (Neural Cell Adhesion Molecules); 0 (Nrxn1 protein, mouse); 0 (RNA-Binding Proteins); 0 (neurexin 3, mouse); 0 (neurexin II); 0 (neuroligin 1); 0 (neuroligin 2); 0 (neuroligin 3); 56-12-2 (gamma-Aminobutyric Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170924
[St] Status:MEDLINE


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[PMID]:28871037
[Au] Autor:Jiang W; Wei M; Liu M; Pan Y; Cao D; Yang X; Zhang C
[Ad] Endereço:Key Laboratory of Cognitive Science, Hubei Key Laboratory of Medical Information Analysis and Tumor Diagnosis and Treatment, Laboratory of Membrane Ion Channels and Medicine, College of Biomedical Engineering, South-Central University for Nationalities, Wuhan 430074, China.
[Ti] Título:Identification of Protein Tyrosine Phosphatase Receptor Type O (PTPRO) as a Synaptic Adhesion Molecule that Promotes Synapse Formation.
[So] Source:J Neurosci;37(41):9828-9843, 2017 Oct 11.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The proper formation of synapses-specialized unitary structures formed between two neurons-is critical to mediating information flow in the brain. Synaptic cell adhesion molecules (CAMs) are thought to participate in the initiation of the synapse formation process. However, functional analysis demonstrates that most well known synaptic CAMs regulate synaptic maturation and plasticity rather than synapse formation, suggesting that either CAMs work synergistically in the process of forming synapses or more CAMs remain to be found. By screening for unknown CAMs using a co-culture system, we revealed that protein tyrosine phosphatase receptor type O (PTPRO) is a potent CAM that induces the formation of artificial synapse clusters in co-cultures of human embryonic kidney 293 cells and hippocampal neurons cultured from newborn mice regardless of gender. PTPRO was enriched in the mouse brain and localized to postsynaptic sites at excitatory synapses. The overexpression of PTPRO in cultured hippocampal neurons increased the number of synapses and the frequency of miniature EPSCs (mEPSCs). The knock-down (KD) of PTPRO expression in cultured neurons by short hairpin RNA (shRNA) reduced the number of synapses and the frequencies of the mEPSCs. The effects of shRNA KD were rescued by expressing either full-length PTPRO or a truncated PTPRO lacking the cytoplasmic domain. Consistent with these results, the N-terminal extracellular domain of PTPRO was required for its synaptogenic activity in the co-culture assay. Our data show that PTPRO is a synaptic CAM that serves as a potent initiator of the formation of excitatory synapses. The formation of synapses is critical for the brain to execute its function and synaptic cell adhesion molecules (CAMs) play essential roles in initiating the formation of synapses. By screening for unknown CAMs using a co-culture system, we revealed that protein tyrosine phosphatase receptor type O (PTPRO) is a potent CAM that induces the formation of artificial synapse clusters. Using loss-of-function and gain-of-function approaches, we show that PTPRO promotes the formation of excitatory synapses. The N-terminal extracellular domain of PTPRO was required for its synaptogenic activity in cultured hippocampal neurons and the co-culture assay. Together, our data show that PTPRO is a synaptic CAM that serves as a potent initiator of synapse formation.
[Mh] Termos MeSH primário: Moléculas de Adesão de Célula Nervosa/fisiologia
Proteínas Tirosina Fosfatases Classe 3 Semelhantes a Receptores/fisiologia
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Técnicas de Cocultura
Potenciais Pós-Sinápticos Excitadores/fisiologia
Técnicas de Silenciamento de Genes
Células HEK293
Hipocampo/citologia
Hipocampo/crescimento & desenvolvimento
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Moléculas de Adesão de Célula Nervosa/genética
Técnicas de Patch-Clamp
Proteínas Tirosina Fosfatases Classe 3 Semelhantes a Receptores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neural Cell Adhesion Molecules); EC 3.1.3.48 (Ptpro protein, mouse); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 3)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.0729-17.2017


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[PMID]:28716979
[Au] Autor:Bustamante A; López-Cancio E; Pich S; Penalba A; Giralt D; García-Berrocoso T; Ferrer-Costa C; Gasull T; Hernández-Pérez M; Millan M; Rubiera M; Cardona P; Cano L; Quesada H; Terceño M; Silva Y; Castellanos M; Garces M; Reverté S; Ustrell X; Marés R; Baiges JJ; Serena J; Rubio F; Salas E; Dávalos A; Montaner J
[Ad] Endereço:From the Neurovascular Research Laboratory, Vall d'Hebron Institut de Recerca (VHIR), Hospital Universitari Vall d'Hebron, Universitat Autònoma de Barcelona, Spain (A.B., A.P., D.G., T.G.-B., J.M.); Stroke Unit, Hospital Universitari Germans Trias i Pujol, Barcelona, Spain (E.L.-C., M.H.-P., M.M., A
[Ti] Título:Blood Biomarkers for the Early Diagnosis of Stroke: The Stroke-Chip Study.
[So] Source:Stroke;48(9):2419-2425, 2017 Sep.
[Is] ISSN:1524-4628
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND PURPOSE: Stroke diagnosis could be challenging in the acute phase. We aimed to develop a blood-based diagnostic tool to differentiate between real strokes and stroke mimics and between ischemic and hemorrhagic strokes in the hyperacute phase. METHODS: The Stroke-Chip was a prospective, observational, multicenter study, conducted at 6 Stroke Centers in Catalonia. Consecutive patients with suspected stroke were enrolled within the first 6 hours after symptom onset, and blood samples were drawn immediately after admission. A 21-biomarker panel selected among previous results and from the literature was measured by immunoassays. Outcomes were differentiation between real strokes and stroke mimics and between ischemic and hemorrhagic strokes. Predictive models were developed by combining biomarkers and clinical variables in logistic regression models. Accuracy was evaluated with receiver operating characteristic curves. RESULTS: From August 2012 to December 2013, 1308 patients were included (71.9% ischemic, 14.8% stroke mimics, and 13.3% hemorrhagic). For stroke versus stroke mimics comparison, no biomarker resulted included in the logistic regression model, but it was only integrated by clinical variables, with a predictive accuracy of 80.8%. For ischemic versus hemorrhagic strokes comparison, NT-proBNP (N-Terminal Pro-B-Type Natriuretic Peptide) >4.9 (odds ratio, 2.40; 95% confidence interval, 1.55-3.71; <0.0001) and endostatin >4.7 (odds ratio, 2.02; 95% confidence interval, 1.19-3.45; =0.010), together with age, sex, blood pressure, stroke severity, atrial fibrillation, and hypertension, were included in the model. Predictive accuracy was 80.6%. CONCLUSIONS: The studied biomarkers were not sufficient for an accurate differential diagnosis of stroke in the hyperacute setting. Additional discovery of new biomarkers and improvement on laboratory techniques seem necessary for achieving a molecular diagnosis of stroke.
[Mh] Termos MeSH primário: Isquemia Encefálica/sangue
Hemorragia Cerebral/sangue
Acidente Vascular Cerebral/sangue
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Amina Oxidase (contendo Cobre)/sangue
Apolipoproteína C-III/sangue
Biomarcadores/sangue
Isquemia Encefálica/diagnóstico
Estudos de Casos e Controles
Caspase 3/sangue
Moléculas de Adesão Celular/sangue
Hemorragia Cerebral/diagnóstico
Quimiocina CXCL1/sangue
Endostatinas/sangue
Proteína Ligante Fas/sangue
Feminino
Produtos de Degradação da Fibrina e do Fibrinogênio/metabolismo
Fibronectinas/sangue
Proteínas de Choque Térmico HSC70/sangue
Seres Humanos
Proteína 3 de Ligação a Fator de Crescimento Semelhante à Insulina/sangue
Subunidade gama Comum de Receptores de Interleucina/sangue
Interleucina-17/sangue
Interleucina-6/sangue
Modelos Logísticos
Masculino
Metaloproteinase 9 da Matriz/sangue
Meia-Idade
Peptídeo Natriurético Encefálico/sangue
Fator de Crescimento Neural/sangue
Moléculas de Adesão de Célula Nervosa/sangue
Razão de Chances
Fragmentos de Peptídeos/sangue
Fosfopiruvato Hidratase/sangue
Estudos Prospectivos
Curva ROC
Receptores Tipo I de Fatores de Necrose Tumoral/sangue
Subunidade beta da Proteína Ligante de Cálcio S100/sangue
Acidente Vascular Cerebral/diagnóstico
Fator de von Willebrand/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Apolipoprotein C-III); 0 (Biomarkers); 0 (Cell Adhesion Molecules); 0 (Chemokine CXCL1); 0 (Endostatins); 0 (FASLG protein, human); 0 (Fas Ligand Protein); 0 (Fibrin Fibrinogen Degradation Products); 0 (Fibronectins); 0 (HSC70 Heat-Shock Proteins); 0 (HSPA8 protein, human); 0 (IGFBP3 protein, human); 0 (IL17A protein, human); 0 (IL2RG protein, human); 0 (IL6 protein, human); 0 (Insulin-Like Growth Factor Binding Protein 3); 0 (Interleukin Receptor Common gamma Subunit); 0 (Interleukin-17); 0 (Interleukin-6); 0 (NGF protein, human); 0 (Neural Cell Adhesion Molecules); 0 (Peptide Fragments); 0 (Receptors, Tumor Necrosis Factor, Type I); 0 (S100 Calcium Binding Protein beta Subunit); 0 (S100B protein, human); 0 (fibrin fragment D); 0 (pro-brain natriuretic peptide (1-76)); 0 (von Willebrand Factor); 114471-18-0 (Natriuretic Peptide, Brain); 9061-61-4 (Nerve Growth Factor); EC 1.4.3.21 (AOC3 protein, human); EC 1.4.3.21 (Amine Oxidase (Copper-Containing)); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (Caspase 3); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 4.2.1.11 (Phosphopyruvate Hydratase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1161/STROKEAHA.117.017076


  9 / 2685 MEDLINE  
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[PMID]:28641112
[Au] Autor:Gangwar SP; Zhong X; Seshadrinathan S; Chen H; Machius M; Rudenko G
[Ad] Endereço:Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555, USA; Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, USA.
[Ti] Título:Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges.
[So] Source:Neuron;94(6):1132-1141.e4, 2017 Jun 21.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuroligins and neurexins promote synapse development and validation by forming trans-synaptic bridges spanning the synaptic cleft. Select pairs promote excitatory and inhibitory synapses, with neuroligin 2 (NLGN2) limited to inhibitory synapses and neuroligin 1 (NLGN1) dominating at excitatory synapses. The cell-surface molecules, MAM domain-containing glycosylphosphatidylinositol anchor 1 (MDGA1) and 2 (MDGA2), regulate trans-synaptic adhesion between neurexins and neuroligins, impacting NLGN2 and NLGN1, respectively. We have determined the molecular mechanism of MDGA action. MDGA1 Ig1-Ig2 is sufficient to bind NLGN2 with nanomolar affinity; its crystal structure reveals an unusual locked rod-shaped array. In the crystal structure of the complex, two MDGA1 Ig1-Ig2 molecules each span the entire NLGN2 dimer. Site-directed mutagenesis confirms the observed interaction interface. Strikingly, Ig1 from MDGA1 binds to the same region on NLGN2 as neurexins do. Thus, MDGAs regulate the formation of neuroligin-neurexin trans-synaptic bridges by sterically blocking access of neurexins to neuroligins.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/metabolismo
Adesão Celular/genética
Proteínas do Tecido Nervoso/metabolismo
Moléculas de Adesão de Célula Nervosa/metabolismo
Sinapses/metabolismo
[Mh] Termos MeSH secundário: Animais
Moléculas de Adesão Celular Neuronais/genética
Linhagem Celular
Cristalografia
Seres Humanos
Mutagênese Sítio-Dirigida
Mutação
Proteínas do Tecido Nervoso/genética
Ligação Proteica
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (MDGA1 protein, human); 0 (NRXN1 protein, human); 0 (Nerve Tissue Proteins); 0 (Neural Cell Adhesion Molecules); 0 (neuroligin 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE


  10 / 2685 MEDLINE  
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[PMID]:28641111
[Au] Autor:Kim JA; Kim D; Won SY; Han KA; Park D; Cho E; Yun N; An HJ; Um JW; Kim E; Lee JO; Ko J; Kim HM
[Ad] Endereço:Graduate School of Nanoscience and Technology, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
[Ti] Título:Structural Insights into Modulation of Neurexin-Neuroligin Trans-synaptic Adhesion by MDGA1/Neuroligin-2 Complex.
[So] Source:Neuron;94(6):1121-1131.e6, 2017 Jun 21.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Membrane-associated mucin domain-containing glycosylphosphatidylinositol anchor proteins (MDGAs) bind directly to neuroligin-1 (NL1) and neuroligin-2 (NL2), thereby respectively regulating excitatory and inhibitory synapse development. However, the mechanisms by which MDGAs modulate NL activity to specify development of the two synapse types remain unclear. Here, we determined the crystal structures of human NL2/MDGA1 Ig1-3 complex, revealing their stable 2:2 arrangement with three interaction interfaces. Cell-based assays using structure-guided, site-directed MDGA1 mutants showed that all three contact patches were required for the MDGA's negative regulation of NL2-mediated synaptogenic activity. Furthermore, MDGA1 competed with neurexins for NL2 via its Ig1 domain. The binding affinities of both MDGA1 and MDGA2 for NL1 and NL2 were similar, consistent with the structural prediction of similar binding interfaces. However, MDGA1 selectively associated with NL2, but not NL1, in vivo. These findings collectively provide structural insights into the mechanism by which MDGAs negatively modulate synapse development governed by NLs/neurexins.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/metabolismo
Adesão Celular
Proteínas Ligadas por GPI/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Moléculas de Adesão de Célula Nervosa/metabolismo
Ligação Proteica
Sinapses/metabolismo
[Mh] Termos MeSH secundário: Animais
Células COS
Cercopithecus aethiops
Cristalografia
Células HEK293
Seres Humanos
Células L (Linhagem Celular)
Espectrometria de Massas
Camundongos
Inibição Neural
Neurogênese
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (GPI-Linked Proteins); 0 (MDGA1 protein, human); 0 (MDGA2 protein, human); 0 (NRXN1 protein, human); 0 (Nerve Tissue Proteins); 0 (Neural Cell Adhesion Molecules); 0 (neuroligin 1); 0 (neuroligin 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE



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