Person:
López Rodríguez, Juan Carlos

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First Name
Juan Carlos
Last Name
López Rodríguez
URI
https://hdl.handle.net/20.500.14352/86792
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Ciencias Químicas
Department
Bioquímica y Biología Molecular
Area
Bioquímica y Biología Molecular
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2018 - 201912020 - 20231
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Author: Turnay Abad, Francisco Javier ×

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    Beyond allergic progression: From molecules to microbes as barrier modulators in the gut-lung axis functionality
    (Frontiers in Allergy, 2023) Parrón Ballesteros, Jorge; Rubén García Gordo; López Rodríguez, Juan Carlos; Olmo López, Nieves; Villalba Díaz, María Teresa; Batanero Cremades, Eva; Turnay Abad, Francisco Javier
    The “epithelial barrier hypothesis” states that a barrier dysfunction can result in allergy development due to tolerance breakdown. This barrier alteration may come from the direct contact of epithelial and immune cells with the allergens, and indirectly, through deleterious effects caused by environmental changes triggered by industrialization, pollution, and changes in the lifestyle. Apart from their protective role, epithelial cells can respond to external factors secreting IL-25 IL-33, and TSLP, provoking the activation of ILC2 cells and a Th2-biased response. Several environmental agents that influence epithelial barrier function, such as allergenic proteases, food additives or certain xenobiotics are reviewed in this paper. In addition, dietary factors that influence the allergenic response in a positive or negative way will be also described here. Finally, we discuss how the gut microbiota, its composition, and microbe-derived metabolites, such as short-chain fatty acids, alter not only the gut but also the integrity of distant epithelial barriers, focusing this review on the gut-lung axis.
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    Molecular dissection of the membrane aggregation mechanisms induced by monomeric annexin A2
    (Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2018) López Rodríguez, Juan Carlos; Martínez-Carmona, Francisco J.; Rodríguez Crespo, José Ignacio; Lizarbe Iracheta, María Antonia; Turnay Abad, Francisco Javier
    Annexins are a multigene family of proteins involved in aggregation and fusion processes of biological membranes. One of its best-known members is annexin A2 (or p36), capable of binding to acidic phospholipids in a calcium-dependent manner, as occurs with other members of the same family. In its heterotetrameric form, especially with protein S100A10 (p11), annexin A2 has been involved as a determinant factor in innumerable biological processes like tumor development or anticoagulation. However, the subcellular coexistence of different pools of the protein, in which the monomeric form of annexin A2 is growing in functional relevance, is to date poorly described. In this work we present an exhaustive structural and functional characterization of monomeric human annexin A2 by using different recombinant mutants. The important role of the amphipathic N-terminal α-helix in membrane binding and aggregation has been analyzed. We have also studied the potential implication of lateral "antiparallel" protein dimers in membrane aggregation. In contrast to what was previously suggested, formation of these dimers negatively regulate aggregation. We have also confirmed the essential role of three lysine residues located in the convex surface of the molecule in calcium-free and calcium-dependent membrane binding and aggregation. Finally, we propose models for annexin A2-mediated vesicle aggregation mechanisms.