6 results on '"Medina-Gali, Regla Maria"'
Search Results
2. A combination of Polypodium leucotomos extract with vitamin A, vitamin C and selenium as an immune adjuvant against recurrent infections.
- Author
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Colino, Alejandra Visedo, Rocamora, Flavia Tamara Hernández, Zapata, José Pardo, Gosálbez, Julio, del Mar Ortega-Villaizán Romo, María, Medina-Gali, Regla Maria, Fernández, David González, and Pérez-Fernández, Alejandro
- Subjects
DISEASE relapse ,IMMUNOLOGICAL adjuvants ,VITAMIN C ,SELENIUM ,SELENOPROTEINS ,VITAMIN A ,INFLAMMATION ,SWEET potatoes - Abstract
Plant chemodiversity is a helpful tool for disease prevention and a basis for adjuvant treatments to conventional therapies. In this regard, the extract of Polypodium leucotomos rhizomes, PLE, has shown benefits fighting inflammation and recurrent infections but its molecular mechanism is poorly undersood. This work shows that Plesinox 3A, containing PLE, Vitamins A, C, and selenium, helps modulate the initial inflammatory response triggered by bacterial LPS through the upregulation of IL8 and IL10, together with downregulation of COX2, IL1B and TNF, in a more efficient manner than PLE alone. Additionally, this formulation enhances the antiviral response through the upregulation of MX1, IFNA1 and IFNG in different cell types. Finally, the addition of vitamins and selenium to PLE in Plesinox 3A greatly boosts the anti-bacterial properties of PLE alone. Overall, these findings support the combined use of PLE, vitamins, and selenium, in the form of Plesinox 3A as an immune booster to prevent recurrent infections, highlighting a gene set potentially involved in its beneficial effect, as well as showing its direct anti-bacterial properties, which are greater than those of PLE alone. [ABSTRACT FROM AUTHOR]
- Published
- 2023
- Full Text
- View/download PDF
3. G protein-coupled oestrogen receptor activation by Bisphenol-A disrupts protection from apoptosis conferred by oestrogen receptors ERα and ERβ in pancreatic beta cells
- Author
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Babiloni-Chust, Ignacio, primary, Dos Santos, Reinaldo Sousa, additional, Medina-Gali, Regla Maria, additional, Perez-Serna, Atenea Alexandra, additional, Encinar, Jose Antonio, additional, Martinez-Pinna, Juan, additional, Gustafsson, Jan-Ake, additional, Marroqui, Laura, additional, and Nadal, Angel, additional
- Published
- 2022
- Full Text
- View/download PDF
4. pH-Dependent Solution Structure and Activity of a Reduced Form of the Host-Defense Peptide Myticin C (Myt C) from the Mussel Mytilus galloprovincialis.
- Author
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Martinez-Lopez, Alicia, Encinar, Jose Antonio, Medina-Gali, Regla Maria, Balseiro, Pablo, Garcia-Valtanen, Pablo, Figueras, Antonio, Novoa, Beatriz, and Estepa, Amparo
- Abstract
Myticin C (Myt C) is a highly variable host-defense peptide (HDP) associated to the immune response in the mediterranean mussel (Mytilus galloprovincialis), which has shown to be active across species due to its strong antiviral activity against a fish rhabdovirus found in fish cells overexpressing this HDP. However, the potential antimicrobial properties of any synthetic analogue of Myt C has not yet been analysed. Thus, in this work we have synthesised the sequence of the mature peptide of Myt C variant c and analysed the structure activity relationships of its reduced (non-oxidized) form (red-MytCc). In contrast to results previously reported for oxidized isoforms of mussel myticins, red-MytCc was not active against bacteria at physiological pH and showed a moderate antiviral activity against the viral haemorrhagic septicaemia (VHS) rhabdovirus. However, its chemotactic properties remained active. Structure/function studies in neutral and acid environments by means of infrared spectroscopy indicated that the structure of red-MytCc is pH dependent, with acid media increasing its alpha-helical content. Furthermore, red-MytCc was able to efficiently aggregate artificial phospholipid membranes at low pH, as well as to inhibit the Escherichia coli growth, suggesting that this activity is attributable to its more structured form in an acidic environment. All together, these results highlight the dynamic and environmentally sensitive behavior of red-Myt C in solution, and provide important insights into Myt C structure/activity relationships and the requirements to exert its antimicrobial/immunomodulatory activities. On the other hand, the pH-dependent direct antimicrobial activity of Myt C suggests that this HDP may be a suitable template for the development of antimicrobial agents that would function selectively in specific pH environments, which are sorely needed in this "antibiotic-resistance era". [ABSTRACT FROM AUTHOR]
- Published
- 2013
- Full Text
- View/download PDF
5. PH-dependent solution structure and activity of a reduced form of the host-defense peptide myticin C (Myt C) from the mussel mytilus galloprovincialis
- Author
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Beatriz Novoa, Antonio Figueras, Pablo Garcia-Valtanen, A. Martinez-Lopez, Amparo Estepa, José Antonio Encinar, Pablo Balseiro, Regla María Medina-Gali, Ministerio de Economía y Competitividad (España), Generalitat Valenciana, Martinez-Lopez, Alicia, Encinar, Jose Antonio, Medina-Gali, Regla Maria, Balseiro, Pablo, Garcia-Valtanen, Pablo, Figueras, Antonio, Novoa, Beatriz, and Estepa, Amparo
- Subjects
PH ,Pharmaceutical Science ,Peptide ,myticin ,mussel ,HDPs ,AMPs ,VHSV ,chemotaxis ,pH ,structure ,infrared spectroscopic ,liposomes ,medicine.disease_cause ,Protein Structure, Secondary ,chemistry.chemical_compound ,Protein structure ,Anti-Infective Agents ,Drug Discovery ,Protein Isoforms ,Pharmacology, Toxicology and Pharmaceutics (miscellaneous) ,lcsh:QH301-705.5 ,Cells, Cultured ,Myticin ,chemistry.chemical_classification ,Chemotaxis ,Fishes ,Blood Proteins ,Hydrogen-Ion Concentration ,Antimicrobial ,Solutions ,Biochemistry ,Rhabdoviridae ,Infrared spectroscopic ,Phospholipid ,Biology ,Antiviral Agents ,Article ,Structure-Activity Relationship ,medicine ,Escherichia coli ,Structure–activity relationship ,Animals ,Mytilus ,Ph ,Structure ,Bivalvia ,chemistry ,lcsh:Biology (General) ,Liposomes ,Mussel ,Peptides ,Antimicrobial Cationic Peptides - Abstract
19 páginas, 6 figuras, Myticin C (Myt C) is a highly variable host-defense peptide (HDP) associated to the immune response in the mediterranean mussel (Mytilus galloprovincialis), which has shown to be active across species due to its strong antiviral activity against a fish rhabdovirus found in fish cells overexpressing this HDP. However, the potential antimicrobial properties of any synthetic analogue of Myt C has not yet been analysed. Thus, in this work we have synthesised the sequence of the mature peptide of Myt C variant c and analysed the structure activity relationships of its reduced (non-oxidized) form (red-MytCc). In contrast to results previously reported for oxidized isoforms of mussel myticins, red-MytCc was not active against bacteria at physiological pH and showed a moderate antiviral activity against the viral haemorrhagic septicaemia (VHS) rhabdovirus. However, its chemotactic properties remained active. Structure/function studies in neutral and acid environments by means of infrared spectroscopy indicated that the structure of red-MytCc is pH dependent, with acid media increasing its alpha-helical content. Furthermore, red-MytCc was able to efficiently aggregate artificial phospholipid membranes at low pH, as well as to inhibit the Escherichia coli growth, suggesting that this activity is attributable to its more structured form in an acidic environment. All together, these results highlight the dynamic and environmentally sensitive behavior of red-Myt C in solution, and provide important insights into Myt C structure/activity relationships and the requirements to exert its antimicrobial/immunomodulatory activities. On the other hand, the pH-dependent direct antimicrobial activity of Myt C suggests that this HDP may be a suitable template for the development of antimicrobial agents that would function selectively in specific pH environments, which are sorely needed in this “antibiotic-resistance era”., This work was supported by the Spanish grants AGL2011-28921-C03, BFU2008-00602 and CONSOLIDER INGENIO 2010 CSD2007-00002 and 2008-00005 from MINECO as well as by the grants SIC-2012-003 and ACOMP/2013/230 from Generalitat Valenciana (Spain).
- Published
- 2013
6. Increasing versatility of the DNA vaccines through modification of the subcellular location of plasmid-encoded antigen expression in the in vivo transfected cells
- Author
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Regla María Medina-Gali, Maria del Mar Ortega-Villaizan, Luis Perez, Pablo Garcia-Valtanen, Amparo Estepa, Julio Coll, A. Martinez-Lopez, Veronica Chico, Martinez-Lopez, Alicia, Garcia-Valtanen, Pablo, Del, Mar Ortega-Villaizan Maria, Chico, Verónica, Medina-Gali, Regla Maria, Perez, Luis, Coll, Julio, and Estepa, Amparo
- Subjects
Oncorhynchus ,Gene Expression ,lcsh:Medicine ,Antibodies, Viral ,DNA vaccination ,Virus ,Cell Line ,Fish Diseases ,Plasmid ,Immune system ,Antigen ,Hemorrhagic Septicemia, Viral ,Vaccines, DNA ,Animals ,antibodies ,lcsh:Science ,Antigens, Viral ,Viral Structural Proteins ,trout ,B cells ,Multidisciplinary ,biology ,Viral Vaccine ,lcsh:R ,Viral Vaccines ,vaccines ,Virology ,cell cultures ,Cell culture ,biology.protein ,Immunization ,lcsh:Q ,enzyme-linked immunity ,Antibody ,Research Article - Abstract
The route of administration of DNA vaccines can play a key role in the magnitude and quality of the immune response triggered after their administration. DNA vaccines containing the gene of the membrane-anchored glycoprotein (gpG) of the fish rhabdoviruses infectious haematopoietic necrosis virus (IHNV) or viral haematopoietic septicaemia virus (VHSV), perhaps the most effective DNA vaccines generated so far, confer maximum protection when injected intramuscularly in contrast to their low efficacy when injected intraperitoneally. In this work, taking as a model the DNA vaccine against VHSV, we focused on developing a more versatile DNA vaccine capable of inducing protective immunity regardless of the administration route used. For that, we designed two alternative constructs to gpG1-507 (the wild type membrane-anchored gpG of VHSV) encoding either a soluble (gpG1-462) or a secreted soluble (gpGLmPle20-462) form of the VHSV-gpG. In vivo immunisation/challenge assays showed that only gpGLmPle20-462 (the secreted soluble form) conferred protective immunity against VHSV lethal challenge via both intramuscular and intraperitoneal injection, being this the first description of a fish viral DNA vaccine that confers protection when administered intraperitoneally. Moreover, this new DNA vaccine construct also conferred protection when administered in the presence of an oil adjuvant suggesting that DNA vaccines against rhabdoviruses could be included in the formulation of current multicomponent-intaperitoneally injectable fish vaccines formulated with an oil adjuvant. On the other hand, a strong recruitment of membrane immunoglobulin expressing B cells, mainly membrane IgT, as well as t-bet expressing T cells, at early times post-immunisation, was specifically observed in the fish immunised with the secreted soluble form of the VHSV-gpG protein; this may indicate that the subcellular location of plasmid-encoded antigen expression in the in vivo transfected cells could be an important factor in determining the ways in which DNA vaccines prime the immune response. © 2013 Martinez-Lopez et al.
- Published
- 2013
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