Person:
Vivanco Martínez, Fernando

First Name

Fernando

Last Name

Vivanco Martínez

URI

https://hdl.handle.net/20.500.14352/84150

Affiliation

Universidad Complutense de Madrid

Faculty / Institute

Ciencias Químicas

Area

Bioquímica y Biología Molecular

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Now showing 1 - 10 of 11

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
Allergy to kiwi: a double-blind, placebo-controlled food challenge study in patients from a birch-free area.
(Journal of Allergy and Clinical Immunology, 2004) Alemán, Ana; Sastre, Joaquín; Quirce, Santiago; Heras González, Manuel De Las; Carnés, Jerónimo; Fernández-Caldas, Enrique; Pastor Vargas, Carlos; Blázquez, Ana Belén; Vivanco Martínez, Fernando; Cuesta-Herranz, Javier
ackground: Allergy to kiwi fruit is being increasingly reported, but it has never been evaluated by means of a double-blind, placebo-controlled food challenge (DBPCFC) study. Objective: We sought to assess kiwi allergy on the basis of a DBPCFC and identify the patterns of allergen recognition in sensitized patients from a birch-free area. Methods: Forty-three patients with allergy symptoms who were sensitized to kiwi were evaluated by means of clinical history, skin tests, IgE determinations, and DBPCFCs. The pattern of allergen recognition was assessed by means of IgE immunoblotting. Sequence analysis of IgE-binding bands was performed by using Edman degradation. Results: DBPCFCs were performed in 33 patients; 4 patients had experienced severe anaphylaxis, and 6 patients declined informed consent. DBPCFC results were positive in 23 patients and negative in 10 patients. The most frequent clinical manifestation was oral allergy syndrome. Twenty-one percent of the patients were not allergic to pollen. Forty-six percent of patients experienced systemic symptoms, and this happened with higher frequency in patients not allergic to pollen (100%). Twenty-eight percent of the patients were sensitized to latex. The IgE-binding bands in kiwi extract more frequently recognized by patient sera were those of 30, 24, 66, and 12 kd, and they could not be associated with any pattern of kiwi-induced allergic reactions. Conclusion: The results provide evidence that kiwi allergy is not a homogeneous disorder because several clinical subgroups can be established. No definite allergen-recognition pattern was associated with the type of allergic reactions to kiwi. One of 5 patients with kiwi allergy was not allergic to pollen, and these patients had the highest risk of systemic reactions to kiwi.
Serine 132 Is the C3 Covalent Attachment Point on the CH1 Domain of Human IgG1
(Journal of Biological Chemistry, 2001) Vidarte, Luis; Pastor Vargas, Carlos; Mas, Sebastian; Blázquez, Ana Belen; Rios, Vivian de los; Guerrero, Rosa; Vivanco Martínez, Fernando
The covalent binding of C3 (complement component C3) to antigen-antibody complexes (Ag.Ab; immune complexes (ICs)) is a key event in the uptake, transport, presentation, and elimination of Ag in the form of Ag.Ab.C3b (IC.C3b). Upon interaction of C3 with IgG.IC, C3b.C3b.IgG covalent complexes are formed that are detected on SDS-polyacrylamide gel electrophoresis by two bands corresponding to C3b.C3b (band A) and C3b.IgG (band B) covalent complexes. This allows one to evaluate the covalent binding of C3b to IgG antibodies. It has been described that C3b can attach to both the Fab (on the CH1 domain) and the Fc regions of IgG. Here the covalent interaction of C3b to the CH1 domain, a region previously described spanning residues 125-147, has been studied. This region of the CH1 domain is exposed to solvent and contains a cluster of six potential acceptor sites for ester bond formation with C3b (four Ser and two Thr). A set of 10 mutant Abs were generated with the putative acceptor residues substituted by Ala, and we studied their covalent interaction with C3b. Single (Ser-131, Ser-132, Ser-134, Thr-135, Ser-136, and Thr-139), double (positions 131-132), and multiple (positions 134-135-136, 131-132-134-135-136, and 131-132-134-135-136-139) mutants were produced. None of the mutants (single, double, or multiple) abolished completely the ability of IgG to bind C3b, indicating the presence of C3b binding regions other than in the CH1 domain. However, all mutant Abs, in which serine at position 132 was replaced by Ala, showed a significant decrease in the ability to form C3b.IgG covalent complexes, whereas the remaining mutants had normal activity. In addition we examined ICs using the F(ab')2 fragment of the mutant Abs, and only those containing Ala at position 132 (instead of Ser) failed to bind C3b. Thus Ser-132 is the binding site for C3b on the CH1 domain of the heavy chain, in the Fab region of human IgG.
Tissue proteomics in atherosclerosis: elucidating the molecular mechanisms of cardiovascular diseases
(Expert Review of Proteomics, 2009) Cuesta, Fernando de la; Álvarez Llamas, Gloria; Gil Dones, Félix; Martin-Rojas, Tatiana; Zubiri, Irene; Pastor Vargas, Carlos; Barderas, Maria ; Vivanco Martínez, Fernando
Atherosclerosis is a disease with higher levels of mortality in developed countries. Comprehension of the molecular mechanisms can yield very useful information in clinics for prevention, diagnosis and recovery monitoring. Proteomics represents an ideal methodology for this purpose, as proteins constitute the effectors of the different biological processes running during pathogenesis. To date, studies in atherosclerosis have been mainly focused on the search for plasma biomarkers. However, tissue proteomics allows going deeper into tissue secretomes, arterial layers or particular cells of interest, which, in turn, constitutes a more direct approximation to in vivo operating mechanisms. The aim of this review is to report latest advances in tissue proteomics in atherosclerosis and related diseases (e.g., aortic stenosis and ischemic injury).
Identification of Major Allergens in Watermelon
(International Archives on Allergy & Immunology, 2009) Pastor Vargas, Carlos; Cuesta-Herranz, Javier; Cases, Barbara; Pérez-Gordo, Marina; Figueredo, Elena; Heras González, Manuel De Las; Vivanco Martínez, Fernando
Background: Watermelon is a worldwide consumed Cucurbitaceae fruit that can elicit allergic reactions. However, the major allergens of watermelon are not known. The aim of this study is to identify and characterize major allergens in watermelon. Methods: Twenty-three patients allergic to watermelon took part in the study. The diagnosis was based on a history of symptoms and positive skin prick-prick tests to watermelon, confirmed by positive open oral challenge testing to watermelon pulp. Allergenic components were detected by SDS-PAGE and immunoblotting. Molecular characterization of IgE-binding bands was performed by N-terminal amino acid sequencing and mass spectrometry. Allergens were purified combining several chromatographic steps. Results: Several IgE binding bands (8-120 kDa) were detected in watermelon extract. Three major allergens were identified as malate dehydrogenase (36 kDa), triose phosphate isomerase (28 kDa) and profilin (13 kDa). Purified allergens individually inhibited IgE binding to the whole watermelon extract. Conclusions: All in all these results indicate that malate dehydrogenase, triose phosphate isomerase and profilin are major allergens involved in watermelon allergy.
Allergy to pumpkin and cross-reactivity to other Cucurbitaceae fruits
(The Journal of Allergy and Clinical Immunology, 2000) Figueredo, Elena ; Cuesta-Herranz, Javier ; Minguez, Ascensión ; Vidarte, Luis ; Pastor Vargas, Carlos; Heras González, Manuel De Las; Vivanco Martínez, Fernando; Lahoz, Carlos
Most human nephritis is due to glomerular deposition and/or formation of immune complexes (IC). In cultured mesangial cells, Fc receptor stimulation induces proliferation, matrix synthesis, and release of several mediators implicated in the initiation and progression of glomerular injury. Since Ig Fc fragments in vitro modified these phenomena, we studied the effects of systemic administration of IgG Fc fragments on the evolution of experimental IC nephritis. Fc fragment injection (1 mg/day i.p.) to rats with ongoing nephritis (proteinuria 20–50 mg/24 h vs 9 6 0.2 mg/24 h in controls) markedly ameliorates proteinuria, renal function, and morphological renal lesions. This was accompanied by a reduction in the renal synthesis of chemokines (monocyte chemoattractant protein-1, IFN-inducible protein-10, and cytokine-induced neutrophil chemoattractant-1), matrix proteins, and growth factors (platelet-derived growth factor, and TGF-b), and in the activity of transcription factors. The treatment did not affect the glomerular deposition of IgG IC and complement C1q. In contrast, a decrease in the renal expression and production of C3 was observed without changes in serum complement levels. In vitro, very low complement consumption and no C3b covalent interaction were observed with Fc fragments, confirming that they did not modify systemic complement activity. These results indicate that the administration of Fc fragments prevents the development of glomerular damage in an aggressive model of proliferative glomerulonephritis through mechanisms involving a reduced local generation of complement, chemokines and growth factors. Modulation of IC-mesangial cell interaction by Fc fragment administration could represent a new approach to the treatment of severe immune nephritis
An Optimal Protocol to Analyze the Rat Spinal Cord Proteome
(Biomarker Insights, 2009) Gil Dones, Félix; Alonso-Orgaz, Sergio; Avila, Gerardo; Martin-Rojas, Tatiana; Moral-Darde, Veronica; Barroso, Gemma; Vivanco Martínez, Fernando; Scott-Taylor, Julian; Barderas, Maria
Since the function of the spinal cord depends on the proteins found there, better defing the normal Spinal Cord Proteome is an important and challenging task. Although brain and cerebrospinal fluid samples from patients with different central nervous system (CNS) disorders have been studied, a thorough examination of specific spinal cord proteins and the changes induced by injury or associated to conditions such as neurodegeneration, spasticity and neuropathies has yet to be performed. In the present study, we aimed to describe total protein content in the spinal cord of healthy rats, employing different proteomics tools. Accordingly, we have developed a fast, easy, and reproducible sequential protocol for protein extraction from rat spinal cords. We employed conventional two dimensional electrophoresis (2DE) in different pH ranges (eg. 4–7, 3–11 NL) combined with identification by mass spectrometry (MALDI-TOF/TOF), as well as first dimension protein separation combined with Liquid Chromatography Mass Spectrometry/Mass Spectrometry (LC-MS/MS) to maximise the benefits of this technology. The value of these techniques is demonstrated here by the identification of several proteins known to be associated with neuroglial structures, neurotransmission, cell survival and nerve growth in the central nervous system. Furthermore this study identified many spinal proteins that have not previously been described in the literature and which may play an important role as either sensitive biomarkers of dysfunction or of recovery after Spinal Cord Injury.
IDENTIFICATION OF A NOVEL 17-kDa PROTEIN AS A FERRET ALLERGEN
(ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2009) González de Olano, David; Pastor Vargas, Carlos; Cases Ortega, Bárbara; Perez-Gordo, Marina; Moral Darde, Verónica; Vivanco Martínez, Fernando; Bartolomé, Borja
Domestic ferret (Mustela putorius furo) is a mammal from the Mustelidae family. It is the third most common uncaged pet in North America after dogs and cats. In Europe, its popularity is progressively increasing, and it is also becoming a common pet. The role of cats and dogs as a cause of allergy is well known. However, ferrets are not so widely studied as a source of relevant allergens.
Administration of IgG Fc Fragments Prevents Glomerular Injury in Experimental Immune Complex Nephritis
(The Journal of Immunology, 2000) Gómez-Guerrero, Carmen; Duque, Natalia; Casado, María Teresa ; Pastor Vargas, Carlos; Blanco, Julia; Mampaso, Francisco; Vivanco Martínez, Fernando; Egido, Jesús
Most human nephritis is due to glomerular deposition and/or formation of immune complexes (IC). In cultured mesangial cells, Fc receptor stimulation induces proliferation, matrix synthesis, and release of several mediators implicated in the initiation and progression of glomerular injury. Since Ig Fc fragments in vitro modified these phenomena, we studied the effects of systemic administration of IgG Fc fragments on the evolution of experimental IC nephritis. Fc fragment injection (1 mg/day i.p.) to rats with ongoing nephritis (proteinuria 20–50 mg/24 h vs 9 ± 0.2 mg/24 h in controls) markedly ameliorates proteinuria, renal function, and morphological renal lesions. This was accompanied by a reduction in the renal synthesis of chemokines (monocyte chemoattractant protein-1, IFN-inducible protein-10, and cytokine-induced neutrophil chemoattractant-1), matrix proteins, and growth factors (platelet-derived growth factor, and TGF-β), and in the activity of transcription factors. The treatment did not affect the glomerular deposition of IgG IC and complement C1q. In contrast, a decrease in the renal expression and production of C3 was observed without changes in serum complement levels. In vitro, very low complement consumption and no C3b covalent interaction were observed with Fc fragments, confirming that they did not modify systemic complement activity. These results indicate that the administration of Fc fragments prevents the development of glomerular damage in an aggressive model of proliferative glomerulonephritis through mechanisms involving a reduced local generation of complement, chemokines and growth factors. Modulation of IC-mesangial cell interaction by Fc fragment administration could represent a new approach to the treatment of severe immune nephritis.
Allergy to human seminal fluid: Cross-reactivity with dog dander
(The Journal of Allergy and Clinical Immunology, 2008) Basagaña, María; Bartolomé, Borja; Pastor Vargas, Carlos; Torres, Ferrán; Alonso, Rosario; Vivanco Martínez, Fernando; Cisteró-Bahíma, Anna
Background: Human seminal plasma (HSP) allergy is uncommon, with symptoms ranging from vulvovaginal pruritus to life-threatening anaphylaxis. Although several seminal plasma allergens have been reported and their molecular masses have been estimated to range between 12 and 75 kd, the prostate-specific antigen (PSA) has recently been identified as a causative allergen. Given that in a large number of cases symptoms appeared during or after the first intercourse, a cross-reactivity phenomenon might be implicated. Objective: We sought to assess the presence of IgE cross-reactivity among proteins from dog epithelium and HSP and to attempt to identify the allergens involved. Methods: Forty-one patients with dog epithelium allergy were selected. One of them experienced anaphylaxis in contact with her husband's seminal plasma. Skin prick tests, serum specific IgE measurements, SDS-PAGE immunoblotting, and inhibition tests were performed to study the pattern of IgE-binding proteins and the potential cross-reactivity between HSP and dog epithelium. Mass spectrometry was carried out to identify the protein involved in allergy reactions. Results: Twenty-four percent of the sera from patients with dog epithelium allergy recognized an IgE-binding band of 28 kd in HSP immunoblotting. Mass spectrometry identified this band as the PSA. SDS-PAGE immunoblotting-inhibition showed a complete IgE-binding inhibition when sera from these patients were preincubated with dog dander extract. Conclusions: IgE cross-reactivity among proteins from dog dander and human PSA is demonstrated.