Person:
Pastor Vargas, Carlos

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First Name
Carlos
Last Name
Pastor Vargas
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Ciencias Químicas
Department
Bioquímica y Biología Molecular
Area
Bioquímica y Biología Molecular
Identifiers
UCM identifierORCIDScopus Author IDWeb of Science ResearcherIDDialnet IDGoogle Scholar ID

Search Results

Now showing 1 - 10 of 74
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    Project number: 322
    La ciencia y tecnología químicas al servicio de la sociedad: actividad formativa para los alumnos del Máster en Ciencia y Tecnología Químicas
    (2023) Guzmán Solís, Eduardo; Guerrero Martínez, Andrés; Sánchez Benítez, Francisco Javier; Lobato Fernández, Álvaro; Barrio Redondo, Melissa del; Pradanas González, Fernando; Cano Rico, Israel; Castillo Martínez, Elisabet; Kayser González, Paula; Moya Cerero, Santiago de la; Gómez Gutiérrez, Julián; Palomares Gracia, Óscar; Pastor Vargas, Carlos; Encinas García, Noemí; García Martín, Gustavo; Lasanta Carrasco, María Isabel
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    Food Allergens: When Friends Become Foes—Caveats and Opportunities for Oral Immunotherapy Based on Deactivation Methods
    (Nutrients, 2023) Gil, Victoria M.; Fernández-Rivera, Nuria; Pastor Vargas, Carlos; Cintas, Pedro
    Food allergies represent a serious health concern and, since the 1990s, they have risen gradually in high-income countries. Unfortunately, the problem is complex because genetic, epigenetic, and environmental factors may be collectively involved. Prevention and diagnoses have not yet evolved into efficacious therapies. Identification and control of allergens present in edible substances hold promise for multi-purpose biomedical approaches, including oral immunotherapy. This review highlights recent studies and methods to modify the otherwise innocuous native proteins in most subjects, and how oral treatments targeting immune responses could help cancel out the potential risks in hypersensitive individuals, especially children. We have focused on some physical methods that can easily be conducted, along with chemo-enzymatic modifications of allergens by means of peptides and phytochemicals in particular. The latter, accessible from naturally-occurring substances, provide an added value to hypoallergenic matrices employing vegetal wastes, a point where food chemistry meets sustainable goals as well.
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    Targeting antigens to an invariant epitope of the MHC Class II DR molecule potentiates the immune response to subunit vaccines
    (Virus Research, 2011) Gil Dones, Félix; Pérez-Filgueira, Mariano; Barderas, María G.; Pastor Vargas, Carlos; Alonso, Covadonga; Vivanco, Fernando; Escribano, José M.
    Recombinant subunit and peptidic vaccines in general present a reduced immunogenicity in vaccinated individuals with respect to the whole pathogen from which they derived. The generation of strong immune responses to these vaccines requires the use of potent adjuvants, high antigen doses and repetitive vaccinations. In this report, we document the enhanced antibody response obtained against two recombinant subunit vaccines by means of targeting to antigen-presenting cells by a recombinant single chain antibody. This antibody, named APCH1, recognizes an epitope of MHC Class II DR molecule preserved in different animal species, including humans. We showed that vaccinal antigens translationally fused to APCH1 antibody and produced by recombinant baculoviruses in insect larvae (Trichoplusia ni), elicited an increased antibody response in comparison with the same antigens alone or fused to a carrier molecule. These results suggest that targeting of antigens to this invariant MHC Class II epitope has immunopotentiating effects that could circumvent the reduced potency of peptidic or subunit vaccines, opening the possibility of widespread application of APCH1 as a new adjuvant antibody of general use.
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    Occupational asthma due to tampico fiber from agave leaves
    (Allergy, 2008) Quirce, S; Fernández‐Nieto, M; Sastre, B.; Sastre, J.; Pastor Vargas, Carlos
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    Targeting antigens to an invariant epitope of the MHC Class II DR molecule potentiates the immune response to subunit vaccines
    (Virus Research, 2011) Pérez-Filgueira, Mariano; Barderas, María G.; Alonso, Covadonga; José M, Escribano; Gil Dones, Félix; Pastor Vargas, Carlos; Vivanco Martínez, Fernando
    Recombinant subunit and peptidic vaccines in general present a reduced immunogenicity in vaccinated individuals with respect to the whole pathogen from which they derived. The generation of strong immune responses to these vaccines requires the use of potent adjuvants, high antigen doses and repetitive vaccinations. In this report, we document the enhanced antibody response obtained against two recombinant subunit vaccines by means of targeting to antigen-presenting cells by a recombinant single chain antibody. This antibody, named APCH1, recognizes an epitope of MHC Class II DR molecule preserved in different animal species, including humans. We showed that vaccinal antigens translationally fused to APCH1 antibody and produced by recombinant baculoviruses in insect larvae (Trichoplusia ni), elicited an increased antibody response in comparison with the same antigens alone or fused to a carrier molecule. These results suggest that targeting of antigens to this invariant MHC Class II epitope has immunopotentiating effects that could circumvent the reduced potency of peptidic or subunit vaccines, opening the possibility of widespread application of APCH1 as a new adjuvant antibody of general use.
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    Identification of vitellogenin as an allergen in Beluga caviar allergy
    (Allergy, 2008) Pérez‐Gordo, M.; Sánchez‐García, S.; Cases, B.; Cuesta‐Herranz, J.; Pastor Vargas, Carlos; Vivanco Martínez, Fernando
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    Occupational asthma caused by gerbil: purification and partial characterization of a new gerbil allergen
    (ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2010) de las Heras, Manuel; Cuesta-Herranz, Javier; Cases, Bárbara; de Miguel, Jaime; Fernández-Nieto, Mar; Sastre, Joaquin; Vivanco Martínez, Fernando; Pastor Vargas, Carlos
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    Allergy to Pumpkin With Cyclophilin as the Relevant Allergen
    (ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2010) González de Olano, David; González-Mancebo, Eloina; Santos Macadán, Sara; Gandolfo Cano, Mar; Pérez-Gordo, Marina; Cases Ortega, Bárbara; Vivanco Martínez, Fernando; Pastor Vargas, Carlos
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    Identification of potential allergens involved in systemic reactions to melon and watermelon
    (Annals of allergy, asthma & immunology, 2010) González-Mancebo, Eloina; López-Torrejón, Gema; González de Olano, David; Cembellín Santos, Sara; Gandolfo-Cano, Mar; Meléndez, Amaya; Salcedo, Gabriel; Cuesta-Herranz, Javier; Vivanco Martínez, Fernando; Pastor Vargas, Carlos
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    Expression of endothelial nitric oxide synthase in human peritoneal tissue: regulation by escherichia coli lipopolysaccharide
    (Journal of the American Society of Nephrology, 2000) Arriero, María M.; Rodríguez-Feo, Juan A.; Celdrán, Ángel; Sánchez de Miguel, Lourdes; González Fernández, Fernando; Fortes, José; Reyero, Ana; Frieyro, Octavio; Pinta, Juan C de la; Franco, Ángeles; Casado, Santos; López Farre, Antonio José; Pastor Vargas, Carlos
    Changes in the expression of endothelial nitric oxide synthase (eNOS) in the peritoneum could be involved in the peritoneal dysfunction associated with peritoneal inflammation. Demonstrated recently in bovine endothelial cells was the existence of cytosolic proteins that bind to the 3′-untranslated region (3′-UTR) of eNOS mRNA and could be implicated in eNOS mRNA stabilization. The present work demonstrates that eNOS protein is expressed in human endothelial and mesothelial peritoneal cells. Escherichia coli lipopolysaccharide shortened the half-life of eNOS message, reducing eNOS protein expression in peritoneal mesothelial and endothelial cells. Moreover, under basal conditions, human peritoneal samples expressed cytosolic proteins that bind to the 3′-UTR of eNOS mRNA. The cytosolic proteins that directly bind to 3′-UTR were identified as a 60-kD protein. After incubation of human peritoneal samples with lipopolysaccharide, the binding activity of the cytosolic 60-kD protein increased in a time-dependent manner. Studies are now necessary to determine the involvement of this 60-kD protein in the regulation of eNOS expression in peritoneal cells and particularly its involvement in the peritoneal dysfunction associated with inflammatory reactions.