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28 results on '"Garcia-Sierra, Francisco"'

1. A model of alcoholic liver disease based on different hepatotoxics leading to liver cancer

Author

Alarcón-Sánchez, Brisa Rodope, Idelfonso-García, Osiris Germán, Guerrero-Escalera, Dafne, Piña-Vázquez, Carolina, de Anda-Jáuregui, Guillermo, Pérez-Hernández, José Luis, de la Garza, Mireya, García-Sierra, Francisco, Sánchez-Pérez, Yesennia, Baltiérrez-Hoyos, Rafael, Vásquez-Garzón, Verónica Rocío, Muriel, Pablo, Pérez-Carreón, Julio Isael, Villa-Treviño, Saúl, and Arellanes-Robledo, Jaime

Published
2024
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2. IFN‐γ stimulates Paneth cell secretion through necroptosis mTORC1 dependent

Author

Encarnacion‐Garcia, Maria R., primary, De la Torre‐Baez, Raúl, additional, Hernandez‐Cueto, María A., additional, Velázquez‐Villegas, Laura A., additional, Candelario‐Martinez, Aurora, additional, Sánchez‐Argáez, Ana Beatriz, additional, Horta‐López, Perla H., additional, Montoya‐García, Armando, additional, Jaimes‐Ortega, Gustavo Alberto, additional, Lopez‐Bailon, Luis, additional, Piedra‐Quintero, Zayda, additional, Carrasco‐Torres, Gabriela, additional, De Ita, Marlon, additional, Figueroa‐Corona, María del Pilar, additional, Muñoz‐Medina, José Esteban, additional, Sánchez‐Uribe, Magdalena, additional, Ortiz‐Fernández, Arturo, additional, Meraz‐Ríos, Marco Antonio, additional, Silva‐Olivares, Angélica, additional, Betanzos, Abigail, additional, Baay‐Guzman, Guillermina Juliana, additional, Navarro‐Garcia, Fernando, additional, Villa‐Treviño, Saúl, additional, Garcia‐Sierra, Francisco, additional, Cisneros, Bulmaro, additional, Schnoor, Michael, additional, Ortíz‐Navarrete, Vianney F., additional, Villegas‐Sepúlveda, Nicolás, additional, Valle‐Rios, Ricardo, additional, Medina‐Contreras, Oscar, additional, Noriega, Lilia G., additional, and Nava, Porfirio, additional

Published
2024
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4. Paneth and Paneth-like cells undergoing necroptosis fuel intestinal epithelial cell proliferation following IFN-γ stimulation.

Author

Nava, Porfirio, primary, Encarnacion-Garcia, Maria R., additional, De la Torre-Baez, Raul, additional, Hernandez-Cueto, Maria A., additional, Velázquez-Villegas, Laura A., additional, Candelario-Martinez, Aurora, additional, Horta-López, Perla H., additional, Montoya-García, Armando, additional, Jaimes-Ortega, Gustavo Alberto, additional, Lopez-Bailon, Luis, additional, Piedra-Quintero, Zayda, additional, Carrasco-Torres, Gabriela, additional, De Ita, Marlon, additional, Figueroa-Corona, Maria del Pilar, additional, Muñoz-Medina, José Esteban, additional, Sánchez-Uribe, Magdalena, additional, Meraz-Ríos, Marco Antonio, additional, Villa-Treviño, Saúl, additional, Garcia-Sierra, Francisco, additional, Cisneros, Bulmaro, additional, Schnoor, Michael, additional, Ortíz-Navarrete, Vianney F., additional, Villegas-Sepúlveda, Nicolás, additional, Valle-Rios, Ricardo, additional, Medina-Contreras, Oscar, additional, and Noriega, Lilia G., additional

Published
2023
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9. Association of α-1-Antichymotrypsin Expression with the Development of Conformational Changes of Tau Protein in Alzheimer’s Disease Brain

Author

Horta-López, Perla H., primary, Mendoza-Franco, Graciela, additional, Rodríguez-Cruz, Fanny, additional, Torres-Cruz, Francisco M., additional, Hernández-Echeagaray, Elizabeth, additional, Jarero-Basulto, Jose J., additional, Rícny, Jan, additional, Florán Garduño, Benjamín, additional, and Garcia-Sierra, Francisco, additional

Published
2022
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11. Pathological Stages of Abnormally Processed Tau Protein During Its Aggregation into Fibrillary Structures in Alzheimer’s Disease

Author

Garcia-Sierra, Francisco, primary, Basurto-Islas, Gustavo, additional, Jarero-Basulto, Jaime, additional, C., Hugo, additional, Torres Cruz, Francisco M., additional, Cortes, Hernan, additional, Camarillo Rojas, Hector M., additional, Kristofikova, Zdena, additional, Ripova, Daniela, additional, Luna-Munoz, Jose, additional, Mena, Raul, additional, I., Lester, additional, and Mondragon-Rodriguez, Siddhartha, additional

Published
2011
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19. Cobalt ferrite nanowhiskers as T2 MRI contrast agent

Author

Ravichandran, M., primary, Oza, Goldie, additional, Velumani, S., additional, Ramirez, Jose Tapia, additional, Garcia-Sierra, Francisco, additional, Andrade, Norma Barragán, additional, Garza-Navarro, Marco A., additional, Garcia-Gutierrez, Domingo I., additional, Lara-Estrada, Rafael, additional, Sacristán-Rock, Emilio, additional, and Yi, Junsin, additional

Published
2015
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20. Lewy body variant of Alzheimer's disease: selective neocortical loss of t-SNARE proteins and loss of MAP2 and alpha-synuclein in medial temporal lobe

Author

Mukaetova-Ladinska, Elizabeta B., Xuereb, John H., Garcia-Sierra, Francisco, Hurt, Jenny, Gertz, Herman-J., Hills, Richard, Brayne, Carol, Huppert, Felicia A., Paykel, Eugene S., McGee, Magnus A., Jakes, Ross, Honer, William G., Harrington, Charles R., Wischik, Claude M., and CC75C Collaboration Group

Subjects
Male, Pathology, lcsh:Medicine, Neocortex, lcsh:Technology, chemistry.chemical_compound, tau, Phosphorylation, lcsh:Science, General Environmental Science, Aged, 80 and over, education.field_of_study, General Medicine, Temporal Lobe, medicine.anatomical_structure, alpha-Synuclein, Female, Alzheimer's disease, SNARE Proteins, dementia with Lewy bodies, Microtubule-Associated Proteins, Alzheimer’s disease, Braak staging, Research Article, Lewy Body Disease, medicine.medical_specialty, Article Subject, Population, Enzyme-Linked Immunosorbent Assay, tau Proteins, MAP2, t-SNARE complex, General Biochemistry, Genetics and Molecular Biology, α-synuclein, Alzheimer Disease, mental disorders, medicine, Dementia, Humans, education, Psychiatry, Aged, Alpha-synuclein, Lewy body, lcsh:T, business.industry, Dementia with Lewy bodies, lcsh:R, medicine.disease, chemistry, nervous system, lcsh:Q, Lewy Bodies, business, Synaptosomes
Abstract

Lewy bodies (LBs) appear in the brains of nondemented individuals and also occur in a range of neurodegenerative disorders, such as dementia with Lewy bodies (DLB) and Parkinson's disease. A number of people with a definite diagnosis of Alzheimer's disease (AD) also exhibit these intraneuronal inclusions in allo- and/or neocortical areas. The latter, referred to as Lewy body variant of AD (LBV), bears a clinical resemblance to AD in terms of age at onset, duration of illness, cognitive impairment, and illness severity. Since the presence of LBs is accompanied by neuronal cytoskeleton changes, it is possible that the latter may influence neuronal connectivity via alterations to the synaptic network. To address this, we examined the expression of synaptic proteins (synaptophysin, syntaxin, SNAP-25, and α-synuclein) and two cytoskeletal proteins (tau and MAP2) in the brain tissue of subjects enrolled in a population-based autopsy study (n = 47). They were divided into groups with no memory problems (control group, n = 15), LBV (n = 5), AD devoid of LBs (n = 17), cerebrovascular dementia (n = 3), and mixed dementia (n = 7). The LBV and AD groups had a similar degree of cognitive impairment and neuropathological staging in terms of Braak staging and CERAD score. In comparison with the control group and the dementia groups without LBs, the LBV group had significantly lower levels of syntaxin and SNAP-25 (23%) in the neocortex, and depletion of MAP2 (64%), SNAP-25 (34%), and α-synuclein (44%) proteins in the medial temporal lobes. These findings suggest that the t-SNARE complex deficit present in LBV may be associated with the presence of LB-related pathology and may explain the more profound cholinergic loss seen in these patients.

Published
2009

22. O4‐05‐05: Modeling familial danish dementia: Implications for the amyloid hypothesis of Alzheimer's disease

Author

Coomaraswamy, Janaky, primary, Kilger, Ellen, additional, Woelfing, Heidrun, additional, Schaefer, Claudia, additional, Kaeser, Stephan A., additional, Wegenast-Braun, Bettina, additional, Hefendehl, Jasmin K., additional, Wolburg, Hartwig, additional, Mazzella, Matthew, additional, Ghiso, Jorge, additional, Goedert, Michel, additional, Akiyama, Haruhiko, additional, Garcia-Sierra, Francisco, additional, Wolfer, David P., additional, Mathews, Paul M., additional, and Jucker, Mathias, additional

Published
2010
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25. Fisiopatología de la enfermedad de Alzheimer.

Author

Garcia-Sierra, Francisco, Luna-Muñoz, José, and Mena-López, Raúl

Subjects
*ALZHEIMER'S disease, *DEMENTIA, *NERVE fibers, *AMYLOID beta-protein, *HIPPOCAMPUS (Brain), *CEREBRAL cortex, *PROTEINS
Abstract

Alzheimer's disease (AD) is the comment cause of dementia in the elderly. Neuropathologically, AD is characterised by two pathological structures, namely neurofibrillary tangles and neuritic plaques. While tangles represent dense accumulation of abnormal filaments from tau protein, plaques are formed by fibrils of β amyloid. The physiopathogenesis of AD is related to a destructive process which is focused upon particular cortical areas and the hippocampus. These regions are directly related with the cognitive functioning and their state of degeneration correlates well with clinical degrees of dementia. Accordingly, the gradual accumulation of tangles has been proved to begin in transentorhinal and entorhinal cortical layer II and then invades the hippocampus follow up by other portions of cerebral cortex and specific sets of subcortical nuclei in a stererotyped fashion. The hierarchical accumulation of tangles in AD is predicted by the Braak's staging which is based on argentophilic labelled brain tissue. Since neurofibrillary tangles and not so plaques, correlate better with the cognitive disfunction in AD, the molecular mechanisms leading to their formation which involve abnormal tau protein processing are currently under intense research. [ABSTRACT FROM AUTHOR]

Published
2006

28. Association of α-1-Antichymotrypsin Expression with the Development of Conformational Changes of Tau Protein in Alzheimer's Disease Brain.

Author

Horta-López, Perla H., Mendoza-Franco, Graciela, Rodríguez-Cruz, Fanny, Torres-Cruz, Francisco M., Hernández-Echeagaray, Elizabeth, Jarero-Basulto, Jose J., Rícny, Jan, Florán Garduño, Benjamín, and Garcia-Sierra, Francisco

Subjects
*TAU proteins, *ALZHEIMER'S disease, *BRAIN diseases, *N-terminal residues, *NEUROFIBRILLARY tangles, *APOLIPOPROTEIN E4, *CHRONIC traumatic encephalopathy
Abstract

• α-1-antichymotrypsin is overexpressed in Alzheimer's disease-affected neurons. • α-1-antichymotrypsin colocalizes with Tau in diffuse granular deposits. • α-1-antichymotrypsin may promote conformational changes in truncated Tau. • Nuclear accumulation of α-1-antichymotrypsin was observed in neurons and astrocytes. In Alzheimer's disease (AD), two mutually exclusive amino-terminal-dependent conformations have been reported to occur during the aggregation of Tau protein into neurofibrillary tangles (NFTs). An early conformation of full-length Tau, involving the bending of the amino terminus over the third repeated domain, is recognized by the Alz-50 antibody, followed by a second conformation recognized by Tau-66 antibody that depends on the folding of the proline-rich region over the third repeated domain in a molecule partially truncated at the amino- and carboxyl-termini. α-1-antichymotrypsin (ACT) is an acute phase serum glycoprotein that accumulates abnormally in the brain of AD patients, and since it is considered to promote the in vitro and in vivo aggregation of amyloid-β, we here seek further evidence that ACT may also contribute to the abnormal aggregation of Tau in AD. By analyzing brain samples from a population of AD cases under immunofluorescence and high-resolution confocal microscopy, we demonstrate here the abundant expression of ACT in hippocampal neurons, visualized as a granular diffuse accumulation, frequently reaching the nuclear compartment. In a significant number of these neurons, intracellular NFTs composed of abnormally phosphorylated and truncated Tau at Asp421 were also observed to coexist in separated regions of the cytoplasm. However, we found strong colocalization between ACT and diffuse aggregates of Tau-66-positive granules, which was not observed with Alz-50 antibody. These results suggest that ACT may play a role during the development of Tau conformational changes facilitating its aggregation during the formation of the neurofibrillary pathology in AD. [ABSTRACT FROM AUTHOR]

Published
2023
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