Structural bioinformatics of signaling proteins
Lab Head: Jordi Villà-Freixa
Computational Biochemistry & Biophysics Lab (CBBL)
Faculty of Science and Technology & Faculty of Medicine
University of Vic – Central University of Catalunya
IMPACT FACTOR (Σ): 4.8
1.- Agulló L, Malhotra S, Fissolo N, Montalban X, Comabella M. Molecular dynamics and intracellular signaling of the TNF-R1 with the R92Q mutation. J Neuroimmunol 289: 12–20 (2015)
2.- Agulló L, Buch I, Gutiérrez-de-Terán H, Garcia-Dorado D, Villà-Freixa J. Computational exploration of the binding mode of heme-dependent stimulators into the active catalytic domain of soluble guanylate cyclase. Proteins 84:1534-48 (2016)
3.- Molinos-Albert LM, Bilbao E, Agulló L, Marfil S, García E, Concepción ML, Izquierdo-Useros N, Vilaplana C, Nieto-Garai JA, Contreras FX, Floor M, Cardona PJ, Martinez-Picado J, Clotet B, Villà-Freixa J, Lorizate M, Carrillo J, Blanco J. Proteoliposomal formulations of an HIV-1 gp41-based miniprotein elicit a lipid-dependent immunodominant response overlapping the 2F5 binding motif. Sci Rep 7:40800 (2017)
Cell signaling in Multiple Sclerosis
Group Head: Xavier Montalbán
Clinical Neuroimmunology Lab, Multiple Sclerosis Center of Catalonia (CEM-Cat)
Vall d’Hebron Research Institute
IMPACT FACTOR (Σ): –
Introduction: TNF receptor 1 appears to have a key role in the autoimmune response. Some MS patients have mutations in this receptor. Our goal is to understand how they affect some of the most common mutations in the course of the disease.
a) the substitution R92Q reduces the age of onset of multiple sclerosis, but slows its progression
1.- Comabella M, Caminero AB, Malhotra S, Agulló L, et al. TNFRSF1A polymorphisms rs1800693 and rs4149584 in patients with multiple sclerosis. Neurology 80: 2010-6 (2013)
Role of the NO/cGMP system in myocardial infarction
2nd POSTDOC – RESEARCHER
Lab Head: David Garcia-Dorado
Experimental Cardiology Lab
Vall d’Hebron Research Institute
IMPACT FACTOR (Σ): 67.19
Introduction: The data on the effect of NO (or donors thereof) in myocardial infarction and the mechanisms by which it acted were contradictory at baseline. On the other hand, there was virtually no information on the operation of transduction system NO / cGMP on the heart during myocardial ischemia and reperfusion. Nor it is well known how the synthesis of cyclic GMP in the myocardial tissue is regulated under physiological conditions.
a) Synthesis of cyclic GMP decreases during myocardial ischemia and reperfusion.
b) Administration of substances that stimulate the synthesis of cyclic GMP by the end coronary occlusion normalized levels of endogenous cyclic GMP and reduces infarct size. Moreover, the beneficial effects of NO in these same models appear to be mediated by cyclic GMP.
c) For the first time in cardiomyocytes it has been found that a significant fraction of ‘soluble’ guanylyl cyclase enzyme is membrane associated. Furthermore, correlation studies carried out indicate that cyclic GMP synthesis in these cells could depend largely enzyme of this fraction membrane located.
1.- Agulló L, García-Dorado D, Inserte J et al. L-Arginine limits myocardial cell death secondary to hypoxia-reoxygenation by a cGMP dependent mechanism. Am J Physiol Heart Circ Physiol 276: H1574-H1580 (1999)
2.- Agulló L, García-Dorado D, Escalona N et al. Effect of ischemia on soluble and particulate guanylyl cyclase-mediated cGMP synthesis on cardiomyocytes. Am J Physiol Heart Circ Physiol 284: H2170-H2176 (2003)
3.- Agulló L, Garcia-Dorado D, Escalona N et al. Membrane-association of nitric oxide-sensitive guanylyl cyclase in cardiomyocytes. Cardiovasc Res 68: 65-74 (2005)
The nitric oxide (NO)/cyclic GMP transduction system in glial cells
PhD – 1st POSTDOC
Lab Heads: Agustina García, Fernando Picatoste
Laboratori de Neuroquímica, Institut de Biologia Biomédica (IBB), Biochemistry and Molecular Biology Department
University Autonoma de Barcelona (UAB)
IMPACT FACTOR (Σ): 47.71
CITATIONS: 856 (523 de una revisión)
Introduction: At the beginning of the study of nitric oxide (NO) in the (beginning of the 90’s) nervous system it was assumed that only NO synthase containing neurons.
a) The glial cells, contrary to what was assumed at the time of study, also contain constitutive NO synthase (apparently similar to neuronal, NOS1).
b) Although the enzyme is in vitro neuronal indistinguishable, the NO synthase is modulated differently in neurons and glial cells.
c) The activity transduction system NO / cGMP glial varies in different areas of the central nervous system and is particularly relevant in the cerebellum.
1.- Agulló L, García A. Different receptors mediate stimulation of nitric oxide-dependent cyclic GMP formation in neurons and astrocytes in culture. Biochem Biophys Res Commun 182: 1362-1368 (1992)
2.- Agulló L, García A. Characterization of noradrenaline-stimulated cyclic GMP formation in brain astrocytes in culture. Biochem J 288: 619-624 (1992)
3.- Murphy S, Simmons ML, Agulló L et al. Synthesis of nitric oxide in CNS glial cells. Trend Neurosci 16: 323-328 (1993)
Training in Clinical Laboratory managment
MEDICAL RESIDENCY (Q.I.R.)
Dept. Heads: Simon Schwartz, Lluis Arcalís
Depts. Clinical Biochemiditry, Hematology and Microbiology
Vall d’Hebron University Hospital
Amino acid neurotransmitter transporters
MASTER OF SCIENCE
Lab Heads: Carmen Aragón & Cecilio Giménez
Biochemistry and Molecular Biology Department – Center of Molecular Biology ‘Severo Ochoa’
University Autonoma de Madrid (UAM)
IMPACT FACTOR (Σ): 5.67
Introduction: Certain data indicated the existence of amino acid neurotransmitter release independent of Ca2+ in the synaptic terminals. The possibility of the involvement of transport systems into the cell in this process are discussed.
a) conveying systems amino acid neurotransmitters might be involved in their release during synaptic transmission (running in reverse as efflux systems).
1.- Agulló L, Jiménez B, Aragón C et al. ß-Alanine transport in synaptic plasma membrane vesicles from rat brain: efflux, exchange and stoichiometry. Eur J Biochem 159: 611-617 (1986)