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4 results on '"Araceli Hernandez-Flores"'

1. The constant domain of CRTAM is essential for high-affinity interaction with Nectin-like 2

Author

Juan Carlos Barragan-Galvez, Araceli Hernandez-Flores, Orestes Lopez-Ortega, Adriana A. Rodriguez-Alvarez, Jose Luis Maravillas-Montero, and Vianney Ortiz-Navarrete

Subjects
CRTAM, Nectin-like 2, Constant domain, CADM1, Affinity, Dimer, Biology (General), QH301-705.5, Biochemistry, QD415-436
Abstract

CRTAM (Class-I MHC restricted T cell-associated molecule) is a member of the Nectin-like family, composed of two extracellular domains, one constant domain (IgC) and another variable domain (IgV), expressed in activated CD8 T cells, epithelial cells, natural killer (NK) cells, and in a subpopulation of CD4 T cells. CRTAM recognizes the ligand Nectin-like 2 (Necl2) through the IgV domain. However, the role of the IgC domain during this ligand recognition has yet to be understood. In this study, we show the purification of soluble-folded Ig domains of CRTAM, and we demonstrate that the IgC domain forms a homodimer in solution via hydrophobic interactions. By surface plasmon resonance (SPR) analysis, we also demonstrate that CRTAM binds to Necl2 with an affinity of 2.16 nM. In conclusion, CRTAM's IgC is essential for a high-affinity interaction with Necl-2.

Published
2024
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2. A Patent-Pending Ointment Containing Extracts of Five Different Plants Showed Antinociceptive and Anti-Inflammatory Mechanisms in Preclinical Studies

Author

Juan Carlos Barragan-Galvez, Maria Leonor Gonzalez-Rivera, Juan C. Jiménez-Cruz, Araceli Hernandez-Flores, Guadalupe de la Rosa, Martha L. Lopez-Moreno, Eunice Yañez-Barrientos, Michelle Romero-Hernández, Martha Alicia Deveze-Alvarez, Pedro Navarro-Santos, Claudia Acosta-Mata, Mario Alberto Isiordia-Espinoza, and Angel Josabad Alonso-Castro

Subjects
ointment, analgesics, anti-inflammatory, plant extracts, inflammatory mediators, NF-κB pathway, Pharmacy and materia medica, RS1-441
Abstract

Background/Objectives: The antinociceptive and anti-inflammatory effects of a patent-pending ointment containing plant extracts from Eucalyptus globulus, Curcuma longa, Hamamelis virginiana, Echinacea purpurea, and Zingiber officinale were evaluated. Methods: Plant extracts were chemically characterized by gas chromatography–mass spectroscopy. The antinociceptive activity of the ointment was assessed using the hot plate, tail flick, and formalin tests, whereas the anti-inflammatory activity was measured using the acute and chronic TPA-induced ear edema tests. Mechanisms of action were evaluated using inhibitors from signaling pathways related to pain response and by using histological analysis and assessing the expression and activity of pro-inflammatory mediators. Results: The ointment showed antinociceptive and anti-inflammatory effects like those observed with diclofenac gel (1.16% v/v) and ketoprofen gel (2.5% v/v). The antinociceptive actions of the ointment are mediated by the possible participation of the opiodergic system and the nitric oxide pathway. The anti-inflammatory response was characterized by a decrease in myeloperoxidase (MPO) activity and by a reduction in ear swelling and monocyte infiltration in the acute inflammation model. In the chronic model, the mechanism of action relied on a decrease in pro-inflammatory mediators such as COX-2, IL-1β, TNF-α, and MPO. An in-silico study with myristic acid, one of the compounds identified in the ointment’s plant mixture, corroborated the in vivo results. Conclusions: The ointment showed antinociceptive activities mediated by the decrease in COX-2 and NO levels, and anti-inflammatory activity due to the reduction in IL-1β and TNFα levels, a reduction in MPO activity, and a decrease in NF-κB and COX-2 expression.

Published
2024
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3. A new nucleocytoplasmic RhoGAP protein contributes to control the pathogenicity ofEntamoeba histolyticaby regulating EhRacC and EhRacD activity

Author

Daniela Lozano-Amado, Arturo Rojo-Domínguez, Nancy Guillén, José Correa-Basurto, Eva Luna-Rivera, Miguel Angel Vargas, Rosaura Hernández-Rivas, Ma. de Jesús Almaraz-Barrera, Michael Schnoor, and Araceli Hernandez-Flores

Subjects
0301 basic medicine, chemistry.chemical_classification, 030102 biochemistry & molecular biology, biology, In silico, Immunology, Peptide, GTPase, Phosphatidic acid, biology.organism_classification, Microbiology, Erythrophagocytosis, Cell biology, 03 medical and health sciences, chemistry.chemical_compound, Entamoeba histolytica, 030104 developmental biology, chemistry, Biochemistry, Virology, Phosphatidylinositol, Actin
Abstract

Summary Small GTPases are signalling molecules that regulate important cellular processes. GTPases are deactivated by GTPase-activating proteins (GAPs). While human GAPs have been intensively studied, no GAP has yet been characterized in Entamoeba histolytica. In this study, we identified and characterized a novel nucleocytoplasmic RhoGAP in E. histolytica termed EhRhoGAPnc. In silico analyses of the domain structure revealed a previously undescribed peptide region within the carboxy-terminal region of EhRhoGAPnc capable of interacting with phosphatidic acid and phosphatidylinositol 3,5-bisphosphate. The full structural GAP domain showed increase GAP activity compared with the minimum region able to display GAP activity, as analysed both by experimental assays and molecular dynamics simulations. Furthermore, we identified amino acid residues that promote interactions between EhRhoGAPnc and its target GTPases EhRacC and EhRacD. Immunofluorescence studies revealed that EhRhoGAPnc colocalized with EhRacC and EhRacD during uroid formation but not during erythrophagocytosis. Interestingly, during erythrophagocytosis of red blood cells, EhRhoGAPnc colocalized with phosphatidic acid and phosphatidylinositol 3,5-bisphosphate. Overexpression of EhRhoGAPnc in E. histolytica led to inhibition of actin adhesion plate formation, migration, adhesion of E. histolytica to MDCK cells and consequently to an impairment of the cytopathic activity.

Published
2016
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4. A new nucleocytoplasmic RhoGAP protein contributes to control the pathogenicity of Entamoeba histolytica by regulating EhRacC and EhRacD activity

Author

Araceli, Hernandez-Flores, Ma de Jesus, Almaraz-Barrera, Daniela, Lozano-Amado, Jose, Correa-Basurto, Arturo, Rojo-Dominguez, Eva, Luna-Rivera, Michael, Schnoor, Nancy, Guillen, Rosaura, Hernandez-Rivas, and Miguel, Vargas

Subjects
Cell Nucleus, Cytoplasm, Binding Sites, Erythrocytes, Entamoeba histolytica, GTPase-Activating Proteins, Protozoan Proteins, Molecular Dynamics Simulation, rac GTP-Binding Proteins, Protein Transport, Phagocytosis, Humans, Amino Acid Sequence, Conserved Sequence
Abstract

Small GTPases are signalling molecules that regulate important cellular processes. GTPases are deactivated by GTPase-activating proteins (GAPs). While human GAPs have been intensively studied, no GAP has yet been characterized in Entamoeba histolytica. In this study, we identified and characterized a novel nucleocytoplasmic RhoGAP in E. histolytica termed EhRhoGAPnc. In silico analyses of the domain structure revealed a previously undescribed peptide region within the carboxy-terminal region of EhRhoGAPnc capable of interacting with phosphatidic acid and phosphatidylinositol 3,5-bisphosphate. The full structural GAP domain showed increase GAP activity compared with the minimum region able to display GAP activity, as analysed both by experimental assays and molecular dynamics simulations. Furthermore, we identified amino acid residues that promote interactions between EhRhoGAPnc and its target GTPases EhRacC and EhRacD. Immunofluorescence studies revealed that EhRhoGAPnc colocalized with EhRacC and EhRacD during uroid formation but not during erythrophagocytosis. Interestingly, during erythrophagocytosis of red blood cells, EhRhoGAPnc colocalized with phosphatidic acid and phosphatidylinositol 3,5-bisphosphate. Overexpression of EhRhoGAPnc in E. histolytica led to inhibition of actin adhesion plate formation, migration, adhesion of E. histolytica to MDCK cells and consequently to an impairment of the cytopathic activity.

Published
2015

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