Publications by authors named "Francisco Garrido"

Banana ( spp.) is the most economically important crop in Ecuador, with exports representing 35% of the agricultural GDP of the country. It covers 230,000 hectares, mostly concentrated in three coastal provinces, Guayas, Los Ríos, and El Oro.

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In 1895, Nicolás Sáenz proposed to the Chilean government to purchase a collection of "Inca" objects brought from Lima. This acquisition was approved in 1897. Despite the difficulties caused by the War of the Pacific, the Museo Nacional de Historia Natural (Chile) continued to acquire Peruvian antiquities, following a tradition of comparative studies of material culture.

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The accelerated scientific, technological, and social advances in recent years have posed new challenges for professional training institutions, where universities play a leading role. Medical schools have not been oblivious to this process. This is how Pontificia Universidad Católica de Chile implemented in 2015 a curricular reform derived from the joint work of academics, students and graduates.

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"Age-Friendly Cities and Communities" is an initiative launched by the WHO in 2007 that has spread to more than 1000 cities and communities around the world. This initiative is based on an integrated physical and social environment for older people, and a model of participatory, collaborative governance. An enabling social environment setting is just as important as material conditions in determining well-being in later life.

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Resettlement, as a major imperial policy in the Inca empire, appears to have been a widespread mechanism for labor mobilization and the dismantling of rebellions. While multiple ethnohistorical references exist regarding resettlement in the central Andes, the extent of this policy in the imperial provinces is still unknown, especially in cases of economic intensification that might have required more labor force. The δ18O isotope is a good proxy for human mobility when comparing the childhood isotopic signature in the teeth enamel and the local water signature at the place of death.

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Objective: To investigate safety and explore efficacy of efgartigimod (ARGX-113), an anti-neonatal Fc receptor immunoglobulin G1 Fc fragment, in patients with generalized myasthenia gravis (gMG) with a history of anti-acetylcholine receptor (AChR) autoantibodies, who were on stable standard-of-care myasthenia gravis (MG) treatment.

Methods: A phase 2, exploratory, randomized, double-blind, placebo-controlled, 15-center study is described. Eligible patients were randomly assigned (1:1) to receive 4 doses over a 3-week period of either 10 mg/kg IV efgartigimod or matched placebo combined with their standard-of-care therapy.

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Protein-protein interactions are an important mechanism for the regulation of enzyme function allowing metabolite channeling, crosstalk between pathways or the introduction of post-translational modifications. Therefore, a number of high-throughput studies have been carried out to shed light on the protein networks established under different pathophysiological settings. Surprisingly, this type of information is quite limited for enzymes of intermediary metabolism such as betaine homocysteine S-methyltransferase, despite its high hepatic abundancy and its role in homocysteine metabolism.

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Hydatid disease (HD) is a parasitic infection caused by the larvae of a tapeworm that is endemic to many regions around the world-South America, Africa, and Asia, in particular. Humans are infected as intermediate hosts in the parasite's life cycle; thus, HD can be seen in persons living in areas where animal husbandry is practiced. However, owing to the varied patterns of migration and immigration during the past several decades, HD can be diagnosed in individuals living anywhere.

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The paradigm of a cytoplasmic methionine cycle synthesizing/eliminating metabolites that are transported into/out of the nucleus as required has been challenged by detection of significant nuclear levels of several enzymes of this pathway. Here, we show betaine homocysteine S-methyltransferase (BHMT), an enzyme that exerts a dual function in maintenance of methionine levels and osmoregulation, as a new component of the nuclear branch of the cycle. In most tissues, low expression of Bhmt coincides with a preferential nuclear localization of the protein.

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Methionine adenosyltransferases MAT I and MAT III (encoded by Mat1a) catalyze S-adenosylmethionine synthesis in normal liver. Major hepatic diseases concur with reduced levels of this essential methyl donor, which are primarily due to an expression switch from Mat1a towards Mat2a. Additional changes in the association state and even in subcellular localization of these isoenzymes are also detected.

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Nutritional imbalance is emerging as a causative factor of hearing loss. Epidemiologic studies have linked hearing loss to elevated plasma total homocysteine (tHcy) and folate deficiency, and have shown that folate supplementation lowers tHcy levels potentially ameliorating age-related hearing loss. The purpose of this study was to address the impact of folate deficiency on hearing loss and to examine the underlying mechanisms.

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Fibromyalgia (FM) is recognized as a common condition, characterized by widespread pain and associated with sleep disturbances and poor-quality sleep. The Pittsburgh Sleep Questionnaire Index (PSQI) is one of the most recommended instruments to measure sleep quality and sleep disorders. The purpose of our study was to translate the questionnaire into Spanish and to assess the psychometric properties of the Spanish version of the PSQI.

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Aims: The discovery of methionine metabolism enzymes in the cell nucleus, together with their association with key nuclear processes, suggested a putative relationship between alterations in their subcellular distribution and disease.

Results: Using the rat model of d-galactosamine intoxication, severe changes in hepatic steady-state mRNA levels were found; the largest decreases corresponded to enzymes exhibiting the highest expression in normal tissue. Cytoplasmic protein levels, activities, and metabolite concentrations suffered more moderate changes following a similar trend.

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Mammalian methionine adenosyltransferase II (MAT II) is the only hetero-oligomer in this family of enzymes that synthesize S-adenosylmethionine using methionine and ATP as substrates. Binding of regulatory β subunits and catalytic α2 dimers is known to increase the affinity for methionine, although scarce additional information about this interaction is available. This work reports the use of recombinant α2 and β subunits to produce oligomers showing kinetic parameters comparable to MAT II purified from several tissues.

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Objective: The objective was to compare bedside ultrasound (US) to clinical examination for the detection of abscess.

Methods: This is a 24-month prospective, observational emergency department (ED) study. Adults with suspected nondraining abscess with planned incision and drainage (I&D) are included in the study.

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Methionine adenosyltransferase from Euglena gracilis (MATX) is a recently discovered member of the MAT family of proteins that synthesize S-adenosylmethionine. Heterologous overexpression of MATX in Escherichia coli rendered the protein mostly in inclusion bodies under all conditions tested. Therefore, a refolding and purification procedure from these aggregates was developed to characterize the enzyme.

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The methionine adenosyltransferase from the thermophile Methanococcus jannaschii is fully and irreversibly unfolded in the presence of guanidinium chloride. Unfolding of this dimeric protein is a three-state process in which a dimeric intermediate could be identified. The less stable secondary structural elements of the protein are the C-terminal ends of β-strands E2 and E6, as deduced from the behavior of tyrosine to tryptophan mutants at residues 72 and 170, which are located in the subunit interface.

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Archaea contain a class of methionine adenosyltransferases (MATs) that exhibit substantially higher stability than their mesophilic counterparts. Their sequences are highly divergent, but preserve the essential active site motifs of the family. We have investigated the origin of this increased stability using chemical denaturation experiments on Methanococcus jannaschii MAT (Mj-MAT) and mutants containing single tryptophans in place of tyrosine residues.

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This work presents a chemometric classification for a set of phosphodiesterase 5 inhibitors, based on a pattern recognition method widely used in quantitative structure-activity (QSAR) studies, hierarchical cluster analysis (HCA) and principal component analysis (PCA), aiming to access the most relevant structural and physicochemical variables related to phosphodiesterase 5 inhibition and to quantify the similarity of the structures within the set of inhibitors. Our model is capable of classifying a test set of 26 known phosphodiesterase 5 inhibitors in terms of similarity, the results being consistent with published experimental data.

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Equilibrium folding of rat liver BHMT (betaine-homocysteine methyltransferase), a TIM (triosephosphate isomerase)-barrel tetrameric protein, has been studied using urea as denaturant. A combination of activity measurements, tryptophan fluorescence, CD and sedimentation-velocity studies suggested a multiphasic process including two intermediates, a tetramer (I4) and a monomer (J). Analysis of denaturation curves for single- and six-tryptophan mutants indicated that the main changes leading to the tetrameric intermediate are related to alterations in the helix alpha4 of the barrel, as well as in the dimerization arm.

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A site-directed-mutagenesis study of putative active-site residues in rat liver betaine-homocysteine S-methyltransferase has been carried out. Identification of these amino acids was based on data derived from a structural model of the enzyme. No alterations in the CD spectra or the gel-filtration chromatography elution pattern were observed with the mutants, thus suggesting no modification in the secondary structure content or in the association state of the proteins.

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Betaine-homocysteine S-methyltransferase is one of the three enzymes involved in homocysteine catabolism. It uses betaine as the methyl donor to convert homocysteine into methionine, also producing dimethylglycine. Recombinant BHMT from rat liver was crystallized by the vapour-diffusion method in both native and seleniomethionyl-labelled forms.

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