Person: Fernández Aceñero, María Jesús
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First Name
María Jesús
Last Name
Fernández Aceñero
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Medicina
Department
Area
Anatomía Patológica
Identifiers
5 results
Search Results
Now showing 1 - 5 of 5
- Project number: 160
Item Aprendizaje flexible y personalizado para atender la diversidad en el aula, mediante la gamificación, a través del uso integrado de un sistema virtual de respuesta en el aula para dispositivos móviles con acceso a internet y una aplicación de screencasting(2018) Pino Sans, Javier Del; Martin Sopeña, Alejandra; López Salas, Alejandra; De Frías González, Mariano; Zeballos Deza, Gabriela; Moyano-Cires Ivanoff, Paula Viviana; García Sánchez, José Manuel; Frejo Moya, María Teresa; Anadón Baselga, María José; Capo Martí, Miguel Andrés; Díaz Plaza, María Jesús; Lobo Alonso, Margarita; García Lobo, Jimena; Pelayo Alarcón, Adela; Blanco Caneda, María Luisa; Peligros Gómez, María Isabel; Menárguez Palanca, Francisco Javier; López Varela, María Del Carmen; Ortega Medina, Luis; Rodríguez Gil, Yolanda; Agra Pujol, Carolina; Fernández Aceñero, María Jesús; Sola Vendrell, Emma Item Toward Liquid Biopsy: Determination of the Humoral Immune Response in Cancer Patients Using HaloTag Fusion Protein-Modified Electrochemical Bioplatforms(Analytical Chemistry, 2016) Garranzo Asensio, María; Guzmán Aránguez, Ana Isabel; Povés Francés, Carmen; Fernández Aceñero, María Jesús; Torrente Rodríguez, Rebeca Magnolia; Ruiz Valdepeñas Montiel, Víctor; Domínguez Muñóz, Gemma; San Frutos Llorente, Luis; Rodríguez Salas, Nuria; Villalba Díaz, María Teresa; Pingarrón Carrazón, José Manuel; Campuzano Ruiz, Susana; Barderas Manchado, RodrigoAutoantibodies raised against tumor-associated antigens have shown high promise as clinical biomarkers for reliable diagnosis, prognosis, and therapy monitoring of cancer. An electrochemical disposable biosensor for the specific and sensitive determination of p53-specific autoantibodies has been developed for the first time in this work. This biosensor involves the use of magnetic microcarriers (MBs) modified with covalently immobilized HaloTag fusion p53 protein as solid supports for the selective capture of specific autoantibodies. After magnetic capture of the modified MBs onto screen-printed carbon working electrodes, the amperometric signal using the system hydroquinone/H2O2 was related to the levels of p53-autoantibodies in the sample. The biosensor was applied for the analysis of sera from 24 patients with high-risk of developing colorectal cancer and 6 from patients already diagnosed with colorectal (4) and ovarian (2) cancer. The developed biosensor was able to determine p53 autoantibodies with a sensitivity higher than that of a commercial standard ELISA using a just-in-time produced protein in a simpler protocol with less sample volume and easily miniaturized and cost-effective instrumentation.Item The specific seroreactivity to ∆Np73 isoforms shows higher diagnostic ability in colorectal cancer patients than the canonical p73 protein(Scientific reports, 2019) Garranzo Asensio, María; Guzmán Aránguez, Ana Isabel; Povés Francés, Carmen; Fernández Aceñero, María Jesús; Montero Calle, Ana; Ceron, María Ángeles; Fernández Díez, Servando; Rodríguez Salas, Nuria; Gómez de Cedrón, Marta; Ramírez de Molina, Ana; Domínguez Muñóz, Gemma; Barderas Manchado, RodrigoThe p53-family is tightly regulated at transcriptional level. Due to alternative splicing, up to 40 different theoretical proteoforms have been described for p73 and at least 20 and 10 for p53 and p63, respectively. However, only the canonical proteins have been evaluated as autoantibody targets in cancer patients for diagnosis. In this study, we have cloned and expressed in vitro the most upregulated proteoforms of p73, ΔNp73α and ΔNp73β, for the analysis of their seroreactivity by a developed luminescence based immunoassay test using 145 individual plasma from colorectal cancer, premalignant individuals and healthy controls. ∆Np73α seroreactivity showed the highest diagnostic ability to discriminate between groups. The combination of ∆Np73α, ∆Np73β and p73 proteoforms seroreactivity were able to improve their individual diagnostic ability. Competitive inhibition experiments further demonstrated the presence of unique specific epitopes in ΔNp73 isoforms not present in p73, with several colorectal patients showing unique and specific seroreactivity to the ΔNp73 proteoforms. Overall, we have increased the complexity of the humoral immune response to the p53-family in cancer patients, showing that the proteoforms derived from the alternative splicing of p73 possess a higher diagnostic ability than the canonical protein, which might be extensive for p53 and p63 proteins.Item Rapid endoglin determination in serum samples using an amperometric magneto-actuated disposable immunosensing platform(Journal of Pharmaceutical and Biomedical Analysis, 2016) Torrente Rodríguez, Rebeca Magnolia; Campuzano Ruiz, Susana; Ruiz Valdepeñas Montiel, Víctor; Pedrero Muñoz, María; Fernández Aceñero, María Jesús; Barderas Manchado, Rodrigo; Pingarrón Carrazón, José ManuelA sensitive and rapid method for the determination of the clinically relevant biomarker human endoglin (CD105) in serum samples is presented, involving a magneto-actuated immunoassay and amperometric detection at disposable screen-printed carbon electrodes (SPCEs). Micro-sized magnetic particles were modified with a specific antibody to selectively capture the target protein which was further sandwiched with a secondary HRP-labeled antibody. The immunocomplexes attached to the magnetic carriers were amperometrically detected at SPCEs using the hydroquinone (HQ)/H2O2/HRP system. The magneto-actuated immunosensing platform was able to detect 5 pmoles of endoglin (in 25μL of sample, 0.2μM) in 30min providing statistically similar results to those obtained using a commercial ELISA kit for the determination of endogenous content of endoglin in human serum samples.Item CX3CL1–CX3CR1 Axis: A New Player in Coeliac Disease Pathogenesis(Nutrients, 2019) Fernández Prieto, Marta; Núñez, Concepción; Fernández Aceñero, María Jesús; López Palacios, Natalia; Bodas Pinedo, Andrés; Farrais, Sergio; Cuevas, David; Pascual, Virginia; Cerón Nieto, María Ángeles; Horta Herrera, Saúl; Espino Paisán, Laura; Salazar Mendoza, IsabelBackground: The CX3CL1–CX3CR1 axis has been related to numerous diseases. The aim of our study was to investigate its involvement in coeliac disease (CD) pathogenesis, particularly in the early phase of the disease. Methods: We collected peripheral blood from CD patients and controls, enrolled in a 3-day gluten challenge, to study soluble CX3CL1, I-TAC and MIG by Luminex, CX3CL1 and CX3CR1 gene expression by qPCR, and CX3CR1 protein expression in monocytes and CD8+, CD4+ and γδ+ T cells, by flow cytometry. We also analysed the expression of the CX3CL1 and CX3CR1 mRNA and protein in the duodenal biopsies of CD patients with active and treated disease, and in non-CD control individuals, by qPCR and immunohistochemistry. Results: After the gluten challenge, increased levels of CX3CL1, I-TAC and MIG proteins were observed in the peripheral blood of CD patients, with no changes in CX3CL1 mRNA, or CX3CR1 mRNA and protein. Regarding duodenal tissue, CX3CL1 was absent or barely present in the superficial and basal epithelium of CD patients, contrasting with the moderate to high levels present in controls. Conclusions: CX3CL1 seems to be involved in the appearance and progression of CD, and it appears to be a potential diagnostic biomarker. Its use as an alternative therapeutic target in CD deserves further research.