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Pesquisa : D12.776.543.750.590 [Categoria DeCS]
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[PMID]:28236974
[Au] Autor:Álvarez-Aznar A; Muhl L; Gaengel K
[Ad] Endereço:Rudbeck Laboratory, Uppsala University, Uppsala, Sweden.
[Ti] Título:VEGF Receptor Tyrosine Kinases: Key Regulators of Vascular Function.
[So] Source:Curr Top Dev Biol;123:433-482, 2017.
[Is] ISSN:1557-8933
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vascular endothelial growth factor receptor (VEGFR) tyrosine kinases are key regulators of vascular development in vertebrates. Their activation is regulated through a family of secreted glycoproteins, the vascular endothelial growth factors (VEGFs). Expression, proteolytic processing, and diffusion range of VEGF proteins need to be tightly regulated, due to their crucial roles in development. While some VEGFs form concentration gradients across developing tissues and act as morphogenes, others function as inhibitors of receptor activation and downstream signaling. Ligand-induced receptor dimerization leads to activation of the intrinsic tyrosine kinase activity, which results in autophosphorylation of the receptors and in turn triggers the recruitment of interacting proteins as well as the initiation of downstream signaling. Although many biochemical details of VEGFR signaling have been revealed, the in vivo relevance of certain signaling aspects still remains to be demonstrated. Here, we highlight basic principles of VEGFR signaling and discuss its crucial role during development of the vascular system in mammals.
[Mh] Termos MeSH primário: Vasos Sanguíneos/fisiologia
Receptores de Fatores de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Animais
Evolução Molecular
Seres Humanos
Ligantes
Neuropilinas/metabolismo
Receptores de Fatores de Crescimento do Endotélio Vascular/química
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ligands); 0 (Neuropilins); EC 2.7.10.1 (Receptors, Vascular Endothelial Growth Factor)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170227
[St] Status:MEDLINE


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[PMID]:27906605
[Au] Autor:Meyer LA; Fritz J; Pierdant-Mancera M; Bagnard D
[Ad] Endereço:a INSERM U1109 - MN3T Lab, Fédération de Médecine Translationnelle, Labex Medalis, University of Strasbourg , France.
[Ti] Título:Current drug design to target the Semaphorin/Neuropilin/Plexin complexes.
[So] Source:Cell Adh Migr;10(6):700-708, 2016 Nov.
[Is] ISSN:1933-6926
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Semaphorin/Neuropilin/Plexin (SNP) complexes control a wide range of biological processes. Consistently, activity deregulation of these complexes is associated with many diseases. The increasing knowledge on SNP had in turn validated these molecular complexes as novel therapeutic targets. Targeting SNP activities by small molecules, antibodies and peptides or by soluble semaphorins have been proposed as new therapeutic approach. This review is focusing on the latest demonstration of this potential and discusses some of the key questions that need to be addressed before translating SNP targeting into clinically relevant approaches.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular/metabolismo
Desenho de Drogas
Proteínas do Tecido Nervoso/metabolismo
Neuropilinas/metabolismo
Semaforinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Bloqueadores/farmacologia
Seres Humanos
Bibliotecas de Moléculas Pequenas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antibodies, Blocking); 0 (Cell Adhesion Molecules); 0 (Nerve Tissue Proteins); 0 (Neuropilins); 0 (Semaphorins); 0 (Small Molecule Libraries); 0 (plexin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE


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[PMID]:27372370
[Au] Autor:Villoutreix BO; Miteva MA
[Ad] Endereço:Université Paris Diderot, Sorbonne Paris Cité, Molécules Thérapeutiques In Silico, Paris, France; Institut National de la Santé et de la Recherche Médicale (INSERM) Unité 973, Molécules Thérapeutiques In Silico, Paris, France. Electronic address: bruno.villoutreix@inserm.fr.
[Ti] Título:Discoidin Domains as Emerging Therapeutic Targets.
[So] Source:Trends Pharmacol Sci;37(8):641-59, 2016 Aug.
[Is] ISSN:1873-3735
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Discoidin (DS) domains are found in eukaryotic and prokaryotic extracellular and transmembrane multidomain proteins. These small domains play different functional roles and can interact with phospholipids, glycans, and proteins, including collagens. DS domain-containing proteins are often involved in cellular adhesion, migration, proliferation, and matrix-remodeling events, while some play a major role in blood coagulation. Mutations in DS domains have been associated with various disease conditions. This review provides an update on the structure, function, and modulation of the DS domains, with a special emphasis on two circulating blood coagulation cofactors, factor V and factor VIII, and the transmembrane neuropilin receptors that have been targeted for inhibition by biologics and small chemical compounds.
[Mh] Termos MeSH primário: Domínio Discoidina/fisiologia
Fator VIII/fisiologia
Fator V/fisiologia
Neuropilinas/fisiologia
[Mh] Termos MeSH secundário: Coagulação Sanguínea/efeitos dos fármacos
Coagulação Sanguínea/fisiologia
Fator V/antagonistas & inibidores
Fator V/química
Fator VIII/antagonistas & inibidores
Fator VIII/química
Seres Humanos
Modelos Moleculares
Terapia de Alvo Molecular
Neuropilinas/antagonistas & inibidores
Neuropilinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Neuropilins); 9001-24-5 (Factor V); 9001-27-8 (Factor VIII)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160704
[St] Status:MEDLINE


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[PMID]:27239104
[Au] Autor:Gao YL; Chai YF; Qi AL; Yao Y; Liu YC; Dong N; Wang LJ; Yao YM
[Ad] Endereço:Department of Emergency Medicine, Tianjin Medical University General Hospital, Tianjin 300052, China.
[Ti] Título:Neuropilin-1highCD4⁺CD25⁺ Regulatory T Cells Exhibit Primary Negative Immunoregulation in Sepsis.
[So] Source:Mediators Inflamm;2016:7132158, 2016.
[Is] ISSN:1466-1861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulatory T cells (Tregs) appear to be involved in sepsis-induced immune dysfunction; neuropilin-1 (Nrp-1) was identified as a surface marker for CD4(+)CD25(+)Tregs. In the current study, we investigated the negative immunoregulation of Nrp-1(high)CD4(+)CD25(+)Tregs and the potential therapeutic value of Nrp-1 in sepsis. Splenic CD4(+)CD25(+)Tregs from cecal ligation and puncture (CLP) mouse models were further segregated into Nrp-1(high)Tregs and Nrp-1(low)Tregs; they were cocultured with CD4(+)CD25(-) T cells. The expression of forkhead/winged helix transcription factor-3 (Foxp-3), cytotoxic T-lymphocyte associated antigen-4 (CTLA-4), membrane associated transforming growth factor-ß (TGF-ß(m+)), apoptotic rate, and secretive ability [including TGF-ß and interleukin-10 (IL-10)] for various types of Tregs, as well as the immunosuppressive ability of Tregs on CD4(+)CD25(-) T cells, were determined. Meanwhile, the impact of recombinant Nrp-1 polyclonal antibody on the demethylation of Foxp-3-TSDR (Treg-specific demethylated region) was measured in in vitro study. Sepsis per se markedly promoted the expression of Nrp-1 of CD4(+)CD25(+)Tregs. Foxp-3/CTLA-4/TGF-ß(m+) of Nrp-1(high)Tregs were upregulated by septic challenge. Nrp-1(high)Tregs showed strong resilience to apoptosis and secretive ability and the strongest immunosuppressive ability on CD4(+)CD25(-) T cells. In the presence of lipopolysaccharide (LPS), the recombinant Nrp-1 polyclonal antibody reduced the demethylation of Foxp-3-TSDR. Nrp-1(high)Tregs might reveal primary negative immunoregulation in sepsis; Nrp-1 could represent a new potential therapeutic target for the study of immune regulation in sepsis.
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos/metabolismo
Subunidade alfa de Receptor de Interleucina-2/metabolismo
Neuropilinas/metabolismo
Sepse/metabolismo
Linfócitos T Reguladores/metabolismo
[Mh] Termos MeSH secundário: Animais
Antígeno CTLA-4/metabolismo
Modelos Animais de Doenças
Fatores de Transcrição Forkhead/metabolismo
Interleucina-10/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Proteínas Repressoras/metabolismo
Sepse/imunologia
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CTLA-4 Antigen); 0 (Forkhead Transcription Factors); 0 (Foxp1 protein, mouse); 0 (IL10 protein, human); 0 (Interleukin-2 Receptor alpha Subunit); 0 (Neuropilins); 0 (Repressor Proteins); 0 (Transforming Growth Factor beta); 130068-27-8 (Interleukin-10)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170117
[Lr] Data última revisão:
170117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160531
[St] Status:MEDLINE
[do] DOI:10.1155/2016/7132158


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[PMID]:26921437
[Au] Autor:Li X; Jung JJ; Nie L; Razavian M; Zhang J; Samuel V; Sadeghi MM
[Ad] Endereço:Section of Cardiovascular Medicine and Cardiovascular Research Center, Yale School of Medicine, New Haven, Connecticut; Veterans Affairs Connecticut Healthcare System, West Haven, Connecticut; School of Pharmacy, Nanjing University of Chinese Medicine, Nanjing, China;
[Ti] Título:The neuropilin-like protein ESDN regulates insulin signaling and sensitivity.
[So] Source:Am J Physiol Heart Circ Physiol;310(9):H1184-93, 2016 May 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Insulin effects on cell metabolism, growth, and survival are mediated by its binding to, and activation of, insulin receptor. With increasing prevalence of insulin resistance and diabetes there is considerable interest in identifying novel regulators of insulin signal transduction. The transmembrane protein endothelial and smooth muscle cell-derived neuropilin-like protein (ESDN) is a novel regulator of vascular remodeling and angiogenesis. Here, we investigate a potential role of ESDN in insulin signaling, demonstrating that Esdn gene deletion promotes insulin-induced vascular smooth muscle cell proliferation and migration. This is associated with enhanced protein kinase B and mitogen-activated protein kinase activation as well as insulin receptor phosphorylation. Likewise, insulin signaling in the liver, muscle, and adipose tissue is enhanced in Esdn(-/-) mice, and these animals exhibit improved insulin sensitivity and glucose homeostasis in vivo. The effect of ESDN on insulin signaling is traced back to its interaction with insulin receptor, which alters the receptor interaction with regulatory adaptor protein-E3 ubiquitin ligase pairs, adaptor protein with pleckstrin homology and Src homology 2 domain-c-Cbl and growth factor receptor bound protein 10-neuronal precursor cell-expressed developmentally downregulated 4. In conclusion, our findings establish ESDN as an inhibitor of insulin receptor signal transduction through a novel regulatory mechanism. Loss of ESDN potentiates insulin's metabolic and mitotic effects and provides insights into a novel therapeutic avenue.
[Mh] Termos MeSH primário: Insulina/farmacologia
Músculo Liso Vascular/efeitos dos fármacos
Miócitos de Músculo Liso/efeitos dos fármacos
Neuropilinas/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Animais
Antígenos CD/metabolismo
Aorta Torácica/efeitos dos fármacos
Aorta Torácica/metabolismo
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Relação Dose-Resposta a Droga
Ativação Enzimática
Feminino
Proteína Adaptadora GRB10/metabolismo
Genótipo
Resistência à Insulina
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Músculo Liso Vascular/metabolismo
Miócitos de Músculo Liso/metabolismo
Neuropilinas/deficiência
Neuropilinas/genética
Fenótipo
Fosforilação
Proteínas Proto-Oncogênicas c-akt/metabolismo
Receptor de Insulina/agonistas
Receptor de Insulina/metabolismo
Fatores de Tempo
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Antigens, CD); 0 (Grb10 protein, mouse); 0 (Insulin); 0 (Neuropilins); 0 (Sh2b2 protein, mouse); 0 (endothelial and smooth muscle cell-derived neuropilin-like protein, mouse); 151441-47-3 (GRB10 Adaptor Protein); EC 2.7.10.1 (INSR protein, human); EC 2.7.10.1 (Receptor, Insulin); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[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:160228
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00782.2015


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[PMID]:26900851
[Au] Autor:Aung NY; Ohe R; Meng H; Kabasawa T; Yang S; Kato T; Yamakawa M
[Ad] Endereço:Department of Pathological Diagnostics, Yamagata University Faculty of Medicine, Yamagata, Japan.
[Ti] Título:Specific Neuropilins Expression in Alveolar Macrophages among Tissue-Specific Macrophages.
[So] Source:PLoS One;11(2):e0147358, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the immune system, neuropilins (NRPs), including NRP-1 and NRP-2, are expressed in thymocytes, dendritic cells, regulatory T cells and macrophages. Their functions on immune cells around the neoplastic cells vary into pro-angiogenesis, tumor progression and anti-angiogenesis according to their ligands. Even though NRPs expression on malignant tumors and immune system has studied, a PubMed-based literature query did not yield any articles describing NRPs expression on tissue-specific macrophages. The aims of this study were (i) to detect NRPs expression on tissue-specific macrophages in the brain, liver, spleen, lymph node and lung; (ii) to observe NRPs expression in classes of macrophages, including alveolar macrophages (AMs), bronchial macrophages (BMs), interstitial macrophages (IMs), intravascular macrophages (IVMs) and macrophage subsets (M1, M2 and Mox) in lung; and (iii) to detect the co-expression of NRPs and dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) in AMs. Both NRPs were specifically detected in AMs among tissue-specific macrophages by immunohistochemistry (IHC). NRPs mRNA expression levels were characterized in normal lung by reverse transcriptase polymerase chain reaction (RT-PCR) and in situ-polymerase chain reaction (in situ-PCR). The expression of both NRPs was detected in AMs, BMs and IVMs by IHC. The frequency of NRPs+ AMs in lung tissue adjacent to the cancer margin was significantly higher than the frequencies in inflamed and normal lung tissue. Double and triple IHC demonstrated that NRPs are expressed on all macrophage subsets in lung. Double IHC showed co-expression of DC-SIGN and NRPs in AMs. This study demonstrated for the first time the specific expression of both NRPs in AMs among tissue-specific macrophages and their expression on M1, M2 and Mox macrophages. Furthermore, the possible origin of AMs from blood monocytes could be suggested from a co-expression of NRPs and DC-SIGN.
[Mh] Termos MeSH primário: Macrófagos Alveolares/metabolismo
Macrófagos/metabolismo
Neuropilinas/metabolismo
[Mh] Termos MeSH secundário: Idoso
Encéfalo/metabolismo
Brônquios/metabolismo
Feminino
Seres Humanos
Imuno-Histoquímica
Fígado/metabolismo
Pulmão/metabolismo
Linfonodos/metabolismo
Masculino
Meia-Idade
Baço/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Neuropilins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160223
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0147358


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[PMID]:26405298
[Au] Autor:Saha S; Chakraborty PK; Xiong X; Dwivedi SK; Mustafi SB; Leigh NR; Ramchandran R; Mukherjee P; Bhattacharya R
[Ad] Endereço:*Peggy and Charles Stephenson Cancer Center, Department of Obstetrics and Gynecology, Department of Pathology, and Department of Cell Biology, University of Oklahoma Health Science Center, Oklahoma City, Oklahoma, USA; and Developmental Vascular Biology Program and Zebrafish Drug Screening Core, Dep
[Ti] Título:Cystathionine ß-synthase regulates endothelial function via protein S-sulfhydration.
[So] Source:FASEB J;30(1):441-56, 2016 Jan.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Deficiencies of the human cystathionine ß-synthase (CBS) enzyme are characterized by a plethora of vascular disorders and hyperhomocysteinemia. However, several clinical trials demonstrated that despite reduction in homocysteine levels, disease outcome remained unaffected, thus the mechanism of endothelial dysfunction is poorly defined. Here, we show that the loss of CBS function in endothelial cells (ECs) leads to a significant down-regulation of cellular hydrogen sulfide (H2S) by 50% and of glutathione (GSH) by 40%. Silencing CBS in ECs compromised phenotypic and signaling responses to the VEGF that were potentiated by decreased transcription of VEGF receptor (VEGFR)-2 and neuropilin (NRP)-1, the primary receptors regulating endothelial function. Transcriptional down-regulation of VEGFR-2 and NRP-1 was mediated by a lack in stability of the transcription factor specificity protein 1 (Sp1), which is a sulfhydration target of H2S at residues Cys68 and Cys755. Reinstating H2S but not GSH in CBS-silenced ECs restored Sp1 levels and its binding to the VEGFR-2 promoter and VEGFR-2, NRP-1 expression, VEGF-dependent proliferation, and migration phenotypes. Thus, our study emphasizes the importance of CBS-mediated protein S-sulfhydration in maintaining vascular health and function.-Saha, S., Chakraborty, P. K., Xiong, X., Dwivedi, S. K. D., Mustafi, S. B., Leigh, N. R., Ramchandran, R., Mukherjee, P., Bhattacharya, R. Cystathionine ß-synthase regulates endothelial function via protein S-sulfhydration.
[Mh] Termos MeSH primário: Cistationina beta-Sintase/metabolismo
Endotélio Vascular/metabolismo
Sulfeto de Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Movimento Celular
Proliferação Celular
Cistationina beta-Sintase/genética
Endotélio Vascular/efeitos dos fármacos
Endotélio Vascular/fisiologia
Glutationa/metabolismo
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/metabolismo
Células Endoteliais da Veia Umbilical Humana/fisiologia
Seres Humanos
Neuropilinas/genética
Neuropilinas/metabolismo
Sistemas do Segundo Mensageiro
Fator A de Crescimento do Endotélio Vascular/farmacologia
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/genética
Receptor 2 de Fatores de Crescimento do Endotélio Vascular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Neuropilins); 0 (Vascular Endothelial Growth Factor A); EC 2.7.10.1 (KDR protein, human); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-2); EC 4.2.1.22 (Cystathionine beta-Synthase); GAN16C9B8O (Glutathione); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170101
[Lr] Data última revisão:
170101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150926
[St] Status:MEDLINE
[do] DOI:10.1096/fj.15-278648


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[PMID]:26199980
[Au] Autor:Fonseca FP; Bingle L; Santos-Silva AR; Lopes MA; de Almeida OP; de Andrade BA; Mariano FV; Kowalski LP; Rangel AL; Martins MD; Meurer L; Speight PM; Vargas PA
[Ad] Endereço:Piracicaba Dental School and Faculty of Medicine, University of Campinas, Piracicaba, Brazil.
[Ti] Título:Semaphorins and neuropilins expression in salivary gland tumors.
[So] Source:J Oral Pathol Med;45(2):119-26, 2016 Feb.
[Is] ISSN:1600-0714
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Salivary gland tumors (SGT) account for 3-10% of all head and neck neoplasms, and little is known about their angiogenic properties. Despite semaphorins and neuropilins have been demonstrated to be prognostic determinants in many human cancers, they remain to be investigated in SGT. Therefore, the objective of this study was to analyze the clinical significance of the expression of class 3 semaphorins A (Sema3A) and B (Sema3B) and neuropilins-1 (Np-1) and neuropilins-2 (Np-2), in SGT. METHODS: Two hundred and forty-eight SGT were organized in tissue microarray paraffin blocks and expression of CD34, Sema3A, Sema3B, Np-1, and Np-2 was determined through immunohistochemistry. The immunoreactions were quantified using digital algorithms and the results correlated with clinicopathological parameters. RESULTS: Malignant tumors had an increased vascular density than their benign counterparts and their increased vascular area significantly correlated with recurrences (P < 0.05). Patients older than 40 years and the presence of recurrences determined an inferior survival rate (P = 0.0057 and P = 0.0303, respectively). In normal salivary glands, Np-1 and Np-2 expression was restricted to ductal cells, whereas Sema3A and Sema3B were positive in the serous acinar compartment. Tumors were positive for all markers and the co-expression of Np-1/Np-2 significantly correlated with the presence of paresthesia and advanced stages of the tumors (P = 0.01 and P = 0.04, respectively). CONCLUSION: Sema3A, Sema3B, Np-1, and Np-2 may be involved in the pathogenesis of SGT, but their expression did not present a statistically significant prognostic potential in this study.
[Mh] Termos MeSH primário: Neuropilinas/biossíntese
Neoplasias das Glândulas Salivares/metabolismo
Semaforinas/biossíntese
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Antígenos CD34/sangue
Biomarcadores Tumorais/genética
Biomarcadores Tumorais/metabolismo
Criança
Feminino
Seres Humanos
Imuno-Histoquímica
Masculino
Meia-Idade
Recidiva Local de Neoplasia/genética
Recidiva Local de Neoplasia/metabolismo
Recidiva Local de Neoplasia/patologia
Estadiamento de Neoplasias
Neuropilinas/genética
Prognóstico
Neoplasias das Glândulas Salivares/genética
Neoplasias das Glândulas Salivares/patologia
Semaforinas/genética
Taxa de Sobrevida
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD34); 0 (Biomarkers, Tumor); 0 (Neuropilins); 0 (Semaphorins)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:150723
[St] Status:MEDLINE
[do] DOI:10.1111/jop.12341


  9 / 188 MEDLINE  
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[PMID]:26451046
[Au] Autor:Guo HF; Vander Kooi CW
[Ad] Endereço:From the Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, Kentucky 40536.
[Ti] Título:Neuropilin Functions as an Essential Cell Surface Receptor.
[So] Source:J Biol Chem;290(49):29120-6, 2015 Dec 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Neuropilins (Nrps) are a family of essential cell surface receptors involved in multiple fundamental cellular signaling cascades. Nrp family members have key functions in VEGF-dependent angiogenesis and semaphorin-dependent axon guidance, controlling signaling and cross-talk between these fundamental physiological processes. More recently, Nrp function has been found in diverse signaling and adhesive functions, emphasizing their role as pleiotropic co-receptors. Pathological Nrp function has been shown to be important in aberrant activation of both canonical and alternative pathways. Here we review key recent insights into Nrp function in human health and disease.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Neuropilinas/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Axônios/metabolismo
Adesão Celular
Seres Humanos
Ligantes
Camundongos
Fenótipo
Ligação Proteica
Estrutura Terciária de Proteína
Transporte Proteico
Semaforinas/metabolismo
Transdução de Sinais
Fator A de Crescimento do Endotélio Vascular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Ligands); 0 (Neuropilins); 0 (Semaphorins); 0 (Vascular Endothelial Growth Factor A)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151010
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R115.687327


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[PMID]:26398657
[Au] Autor:Wu HB; Wang Z; Wang QS; Han YJ; Wang M; Zhou WL; Li HS
[Ad] Endereço:NanFang PET Center, Nanfang Hospital, Southern Medical University, Guangzhou, China.
[Ti] Título:Use of Labelled tLyP-1 as a Novel Ligand Targeting the NRP Receptor to Image Glioma.
[So] Source:PLoS One;10(9):e0137676, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Neuropilin (NRP) receptors are overexpressed in glioma tumor tissue, and therefore may be a potential target for imaging markers. We investigated whether labelled tLyP-1, an NRP targeting peptide, could be used as the targeting ligand for developing reagents for imaging glioma tumors. METHODS: The tLyP-1 peptide (CGNKRTR) was labeled with 5-carboxyfluorescein (FAM) or 18F-fluoride. A control peptide (MAQKTSH) was also labeled with FAM. The in vitro binding between FAM-tLyP-1 and U87MG cells and in vivo biodistribution of FAM-tLyP-1 in a U87MG glioblastoma xenograft model (nude mouse) were determined. The in vivo biodistribution of 18F-tLyP-1 was also determined by microPET/CT. RESULTS: In vitro, FAM-tLyP-1 was strongly taken up by U87MG cells at very low concentrations (1 µM). In vivo, FAM-tLyP-1 accumulated in glioma (U87MG) tumors, but uptake was minimal in the normal brain tissue 1 h after administration. The distribution of FAM-tLyP-1 in the tumor tissue was consistent with expression of NRP1. The tumor/brain fluorescence intensity ratio in mice treated with FAM-tLyP-1 was significantly higher than the control FAM-labeled peptide 1 h after administration (3.44 ± 0.83 vs. 1.32 ± 0.15; t = 5.547, P = 0.001). Uptake of FAM-tLyP-1 in glioma tumors could be blocked by administering an excess of non-conjugated tLyP-1 peptide. [Lys4] tLyP-1 was labeled with 18F to synthesis a PET (18F-tLyP-1). MicroPET/CT imaging showed the tumor was visualized clearly with a high tumor/brain radiolabel ratio at 60 min (2.69 ± 0.52) and 120 min (3.11 ± 0.25). CONCLUSION: Taken together, our results suggest that tLyP-1 could be developed as a novel fluorescent or radio labelled tracer for imaging glioma.
[Mh] Termos MeSH primário: Glioma/diagnóstico por imagem
Glioma/metabolismo
Neuropilinas/metabolismo
Peptídeos Cíclicos/metabolismo
Tomografia por Emissão de Pósitrons
Coloração e Rotulagem
Tomografia Computadorizada por Raios X
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Encéfalo/metabolismo
Neoplasias Encefálicas/metabolismo
Neoplasias Encefálicas/patologia
Linhagem Celular Tumoral
Feminino
Fluoresceínas/metabolismo
Radioisótopos de Flúor
Glioma/patologia
Seres Humanos
Ligantes
Masculino
Camundongos Endogâmicos BALB C
Dados de Sequência Molecular
Peptídeos Cíclicos/química
Distribuição Tecidual
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fluoresceins); 0 (Fluorine Radioisotopes); 0 (Ligands); 0 (LyP-1 peptide); 0 (Neuropilins); 0 (Peptides, Cyclic); 76823-03-5 (4-carboxyfluorescein)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150924
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0137676



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