10 results on '"Aviles-Reyes A"'
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2. Intermittent hypoxia during sleep induces reactive gliosis and limited neuronal death in rats: implications for sleep apnea
- Author
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Aviles-Reyes, Rolando Xavier, Angelo, Maria Florencia, Villarreal, Alejandro, Rios, Hugo, Lazarowski, Alberto, and Ramos, Alberto Javier
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- 2010
- Full Text
- View/download PDF
3. The proinflammatory RAGE/NF-κB pathway is involved in neuronal damage and reactive gliosis in a model of sleep apnea by intermittent hypoxia
- Author
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Alberto Javier Ramos, Silvia Alvarez, Virginia Vanasco, Alejandra Inés Aguirre, Alejandro Villarreal, Diana Jerusalinsky, Philip A. Barker, Rolando Xavier Aviles Reyes, Maria Florencia Angelo, Matias Eliseo Melendez, Alberto L. Epstein, Jeronimo Lukin, Facultad de Medicina [Buenos Aires], Universidad de Buenos Aires [Buenos Aires] (UBA), Virus enveloppés, vecteurs et immunothérapie – Enveloped viruses, Vectors and Immuno-therapy (EVIR), Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centro de Estudios Farmacológicos y Botánicos [Buenos Aires] (CEFYBO), Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)-Facultad de Medicina [Buenos Aires], Universidad de Buenos Aires [Buenos Aires] (UBA)-Universidad de Buenos Aires [Buenos Aires] (UBA), Montreal Neurological Institute and Hospital, McGill University = Université McGill [Montréal, Canada], Centre International de Recherche en Infectiologie - UMR (CIRI), Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Male ,Receptor for Advanced Glycation End Products ,Wistar ,Hippocampus ,lcsh:Medicine ,Biochemistry ,RAGE (receptor) ,chemistry.chemical_compound ,Immunologic ,Receptors ,Gliosis ,Receptors, Immunologic ,Receptor ,lcsh:Science ,Hypoxia ,RAGE/NF-κB PATHWAY ,Neurons ,Multidisciplinary ,NF-kappa B ,Intermittent hypoxia ,Neurochemistry ,3. Good health ,Otras Ciencias Médicas ,medicine.anatomical_structure ,[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology ,[SDV.IMM]Life Sciences [q-bio]/Immunology ,purl.org/becyt/ford/3 [https] ,Research Article ,CIENCIAS MÉDICAS Y DE LA SALUD ,Neurite ,Central nervous system ,purl.org/becyt/ford/3.5 [https] ,Proinflammatory cytokine ,Sleep Apnea Syndromes ,medicine ,Animals ,Rats, Wistar ,Animal ,lcsh:R ,Biology and Life Sciences ,NF-κB ,[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology ,Rats ,Disease Models, Animal ,chemistry ,REACTIVE GLIOSIS ,Immunology ,Disease Models ,Cancer research ,NEURONAL DAMAGE ,lcsh:Q ,Molecular Neuroscience ,Neuroscience - Abstract
Sleep apnea (SA) causes long-lasting changes in neuronal circuitry, which persist even in patients successfully treated for the acute effects of the disease. Evidence obtained from the intermittent hypoxia (IH) experimental model of SA has shown neuronal death, impairment in learning and memory and reactive gliosis that may account for cognitive and structural alterations observed in human patients. However, little is known about the mechanism controlling these deleterious effects that may be useful as therapeutic targets in SA. The Receptor for Advanced Glycation End products (RAGE) and its downstream effector Nuclear Factor Kappa B (NF-κB) have been related to neuronal death and astroglial conversion to the pro-inflammatory neurodegenerative phenotype. RAGE expression and its ligand S100B were shown to be increased in experimental models of SA. We here used dissociated mixed hippocampal cell cultures and male Wistar rats exposed to IH cycles and observed that NF-κB is activated in glial cells and neurons after IH. To disclose the relative contribution of the S100B/RAGE/NF-κB pathway to neuronal damage and reactive gliosis after IH we performed sequential loss of function studies using RAGE or S100B neutralizing antibodies, a herpes simplex virus (HSV)-derived amplicon vector that induces the expression of RAGEΔcyto (dominant negative RAGE) and a chemical blocker of NF-κB. Our results show that NF-κB activation peaks 3 days after IH exposure, and that RAGE or NF-κB blockage during this critical period significantly improves neuronal survival and reduces reactive gliosis. Both in vitro and in vivo, S100B blockage altered reactive gliosis but did not have significant effects on neuronal survival. We conclude that both RAGE and downstream NF-κB signaling are centrally involved in the neuronal alterations found in SA models, and that blockage of these pathways is a tempting strategy for preventing neuronal degeneration and reactive gliosis in SA. Fil: Angelo, María Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia ; Argentina Fil: Aguirre, Alejandra Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia ; Argentina Fil: Aviles Reyes, Rolando Xavier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia ; Argentina Fil: Villarreal, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia ; Argentina Fil: Lukin, Jeronimo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia ; Argentina Fil: Melendez, Matías. Inserm; Francia. Centre National de la Recherche Scientifique; Francia. Université Claude Bernard Lyon 1; Francia Fil: Vanasco, Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina Fil: Barker, Philip A.. McGill University; Canadá Fil: Alvarez, Silvia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Bioquímica y Medicina Molecular; Argentina Fil: Epstein, Alberto Luis. Inserm; Francia. Centre National de la Recherche Scientifique; Francia. Université Claude Bernard Lyon 1; Francia Fil: Jerusalinsky, Diana Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia ; Argentina Fil: Ramos, Alberto Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia ; Argentina
- Published
- 2014
4. ASTROCYTIC OVEREXPRESSION OF NRF2 LEADS TO REDUCED DISEASE PROGRESSION IN APP/PS1 TRANSGENIC MICE
- Author
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Aviles-Reyes, Rolando Xavier, Jonhson, Delinda, and Johnson, Jeffrey
- Published
- 2018
- Full Text
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5. The role of clinical variables, neuropsychological performance and SLC6A4 and COMT gene polymorphisms on the prediction of early response to fluoxetine in major depressive disorder
- Author
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Gudayol-Ferré, Esteve, Herrera-Guzmán, Ixchel, Camarena, Beatriz, Cortés-Penagos, Carlos, Herrera-Abarca, Jorge E., Martínez-Medina, Patricia, Cruz, David, Hernández, Sandra, Genis, Alma, Carrillo-Guerrero, Mariana Y., Avilés Reyes, Rubén, and Guàrdia-Olmos, Joan
- Published
- 2010
- Full Text
- View/download PDF
6. S100B alters neuronal survival and dendrite extension via RAGE-mediated NF-κB signaling.
- Author
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Villarreal, Alejandro, Aviles Reyes, Rolando X., Angelo, Maria Florencia, Reines, Analia G., and Ramos, Alberto Javier
- Subjects
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NEUROLOGICAL research , *ASTROCYTES , *NEUROGLIA , *NERVOUS system , *ISCHEMIA , *BLOOD circulation disorders - Abstract
S100B is a soluble protein secreted by astrocytes that exerts pro-survival or pro-apoptotic effects depending on the concentration reached in the extracellular millieu. The S100B receptor termed RAGE (for receptor for advanced end glycation products) is highly expressed in the developing brain but is undetectable in normal adult brain. In this study, we show that RAGE expression is induced in cortical neurons of the ischemic penumbra. Increased RAGE expression was also observed in primary cortical neurons exposed to excitotoxic glutamate (EG). S100B exerts effects on survival pathways and neurite extension when the cortical neurons have been previously exposed to EG and these S100B effects were prevented by anti-RAGE blocking antibodies. Furthermore, nuclear factor kappa B (NF-κB) is activated by S100B in a dose- and RAGE-dependent manner and neuronal death induced by NF-κB inhibition was prevented by S100B that restored NF-κB activation levels. Together, these findings suggest that excitotoxic damage can induce RAGE expression in neurons from ischemic penumbra and demonstrate that cortical neurons respond to S100B through engagement of RAGE followed by activation of NF-κB signaling. In addition, basal NF-κB activity in neurons is crucial to modulate the extent of pro-survival or pro-death S100B effects. [ABSTRACT FROM AUTHOR]
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- 2011
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7. P1‐178: ASTROCYTIC OVEREXPRESSION OF NRF2 LEADS TO REDUCED DISEASE PROGRESSION IN APP/PS1 TRANSGENIC MICE.
- Author
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Aviles-Reyes, Rolando Xavier, Jonhson, Delinda, and Johnson, Jeffrey
- Published
- 2018
- Full Text
- View/download PDF
8. Simultaneous spatiotemporal mapping of in situ pH and bacterial activity within an intact 3D microcolony structure.
- Author
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Hwang, Geelsu, Liu, Yuan, Kim, Dongyeop, Sun, Victor, Aviles-Reyes, Alejandro, Kajfasz, Jessica K., Lemos, Jose A., and Koo, Hyun
- Published
- 2016
- Full Text
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9. Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.
- Author
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di Cologna, Nicholas M., Samaddar, Sandip, Valle, Carolina A., Vargas, Jonathan, Aviles-Reyes, Alejandro, Morales, Joyce, Ganguly, Tridib, Pileggi, Roberta, Brady, L. Jeannine, Lemos, José A., and Abranches, Jacqueline
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STREPTOCOCCUS mutans , *QUATERNARY structure , *COLONIZATION (Ecology) , *CONGO red (Staining dye) , *BINDING site assay , *HEART valves , *AMYLOID beta-protein , *AMYLOID - Abstract
The cnm gene, coding for the glycosylated collagen- and laminin-binding surface adhesin Cnm, is found in the genomes of approximately 20% of Streptococcus mutans clinical isolates and is associated with systemic infections and increased caries risk. Other surface-associated collagen-binding proteins of S. mutans, such as P1 and WapA, have been demonstrated to form an amyloid quaternary structure with functional implications within biofilms. In silico analysis predicted that the β-sheet-rich N-terminal collagen-binding domain (CBD) of Cnm has a propensity for amyloid aggregation, whereas the threonine-rich C-terminal domain was predicted to be disorganized. In this study, thioflavin-T fluorescence and electron microscopy were used to show that Cnm forms amyloids in either its native glycosylated or recombinant nonglycosylated form and that the CBD of Cnm is the main amyloidogenic unit of Cnm. We then performed a series of in vitro, ex vivo, and in vivo assays to characterize the amylogenic properties of Cnm. In addition, Congo red birefringence indicated that Cnm is a major amyloidogenic protein of S. mutans biofilms. Competitive binding assays using collagen-coated micro-titer plates and dental roots, a substrate rich in collagen, revealed that Cnm monomers inhibit S. mutans binding to collagenous substrates, whereas Cnm amyloid aggregates lose this property. Thus, while Cnm contributes to recognition and initial binding of S. mutans to collagen-rich surfaces, amyloid formation by Cnm might act as a negative regulatory mechanism to modulate collagen-binding activity within S. mutans biofilms and warrants further investigation. IMPORTANCE Streptococcus mutans is a keystone pathogen that promotes caries by acidifying the dental biofilm milieu. The collagen- and laminin-binding glycoprotein Cnm is a virulence factor of S. mutans. Expression of Cnm by S. mutans is hypothesized to contribute to niche expansion, allowing colonization of multiple sites in the body, including collagen-rich surfaces such as dentin and heart valves. Here, we suggest that Cnm function might be modulated by its aggregation status. As a monomer, its primary function is to promote attachment to collagenous substrates via its collagen-binding domain (CBD). However, in later stages of biofilm maturation, the same CBD of Cnm could self-assemble into amyloid fibrils, losing the ability to bind to collagen and likely becoming a component of the biofilm matrix. Our findings shed light on the role of functional amyloids in S. mutans pathobiology and ecology. [ABSTRACT FROM AUTHOR]
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- 2021
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10. Pro-inflammatory Analysis of Macrophages in Contact with Titanium Particles and Porphyromonas gingivalis.
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Dodo CG, Meirelles L, Aviles-Reyes A, Ruiz KGS, Abranches J, and Cury AADB
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- Cell Line, Cytokines genetics, Cytokines metabolism, Enzyme-Linked Immunosorbent Assay, Gene Expression, Humans, Inflammation Mediators metabolism, Macrophages metabolism, Microscopy, Electron, Scanning, O Antigens drug effects, Particle Size, Porphyromonas gingivalis immunology, Real-Time Polymerase Chain Reaction, Titanium chemistry, Dental Implants, Macrophages immunology, Porphyromonas gingivalis drug effects, Titanium pharmacology
- Abstract
During insertion of titanium dental implants, particles may shear from the implant to the periimplant region causing osteolysis, and their association with bacteria can exacerbate the inflammatory reaction. However, the association of a high invasive bacterium from the oral cavity, Porphyromonas gingivalis (Pg), and titanium particles remains unknown. This study evaluated pro-inflammatory reaction of human macrophages in contact with micro and nanoparticles of titanium associated with Porphyromonas gingivalis lipopolysaccharide (PgLPS). THP-1 cell were used and treated for 12, 24 and 48 h following 6 groups: Control(C), PgLPS (L); Microparticles (M); Nanoparticles (N); PgLPS and microparticles (LM); PgLPS and nanoparticles (LN). The following assays were carried out: i) cell viability using MTS, ii) cell morphology by SEM and iii) expression of tumor necrosis factor alpha (TNF-α), interleukin-1 beta (IL-1β) and interleukin-6 (IL-6) by qRT-PCR and ELISA. For statistics two-way ANOVA followed by Tukey's test was used (p<0.05). After treatment, cells presented similar viability and morphology demonstrating that the treatments were not able to induce cell death. Gene expression was significantly higher for TNF-α and IL1-β after 12 h, and for IL-6 after 24 h in the N and LN groups. Cytokine production over time was an ascending curve for TNF-α with the peak at 48 h and IL1-β and IL-6 had a straight line among the time points, although cells from N group presented a significant production of IL-6 at 48 h. In conclusion, these results suggest that titanium nanoparticles stimulate stronger pro-inflammatory response in macrophages, independent of their association with LPS from P.gingivalis.
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- 2017
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