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1.
Biochemistry (Mosc) ; 86(9): 1128-1138, 2021 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-34565316

RESUMEN

Potato virus Y (PVY) is one of the most common and harmful plant viruses. Translation of viral RNA starts with the interaction between the plant cap-binding translation initiation factors eIF4E and viral genome-linked protein (VPg) covalently attached to the viral RNA. Disruption of this interaction is one of the natural mechanisms of plant resistance to PVY. The multigene eIF4E family in the potato (Solanum tuberosum L.) genome contains genes for the translation initiation factors eIF4E1, eIF4E2, and eIF(iso)4E. However, which of these factors can be recruited by the PVY, as well as the mechanism of this interaction, remain obscure. Here, we showed that the most common VPg variant from the PVY strain NTN interacts with eIF4E1 and eIF4E2, but not with eIF(iso)4E. Based on the VPg, eIF4E1, and eIF4E2 models and data on the natural polymorphism of VPg amino acid sequence, we suggested that the key role in the recognition of potato cap-binding factors belongs to the R104 residue of VPg. To verify this hypothesis, we created VPg mutants with substitutions at position 104 and examined their ability to interact with potato eIF4E factors. The obtained data were used to build the theoretical model of the VPg-eIF4E2 complex that differs significantly from the earlier models of VPg complexes with eIF4E proteins, but is in a good agreement with the current biochemical data.


Asunto(s)
Factor 4E Eucariótico de Iniciación/metabolismo , Proteínas de Plantas/metabolismo , Potyvirus/metabolismo , Proteínas Virales/metabolismo , Sitios de Unión , Factor 4E Eucariótico de Iniciación/química , Enlace de Hidrógeno , Simulación de Dinámica Molecular , Mutagénesis Sitio-Dirigida , Proteínas de Plantas/química , Unión Proteica , Isoformas de Proteínas/química , Isoformas de Proteínas/metabolismo , Estructura Terciaria de Proteína , Solanum tuberosum/metabolismo , Técnicas del Sistema de Dos Híbridos , Proteínas Virales/química , Proteínas Virales/genética
2.
Int J Mol Sci ; 22(6)2021 Mar 13.
Artículo en Inglés | MEDLINE | ID: mdl-33805784

RESUMEN

Hepatocellular carcinoma (HCC) frequently shows early invasion into blood vessels as well as intrahepatic metastasis. Innovations of novel small-molecule agents to block HCC invasion and subsequent metastasis are urgently needed. Moscatilin is a bibenzyl derivative extracted from the stems of a traditional Chinese medicine, orchid Dendrobium loddigesii. Although moscatilin has been reported to suppress tumor angiogenesis and growth, the anti-metastatic property of moscatilin has not been elucidated. The present results revealed that moscatilin inhibited metastatic behavior of HCC cells without cytotoxic fashion in highly invasive human HCC cell lines. Furthermore, moscatilin significantly suppressed the activity of urokinase plasminogen activator (uPA), but not matrix metalloproteinase (MMP)-2 and MMP-9. Interestingly, moscatilin-suppressed uPA activity was through down-regulation the protein level of uPA, and did not impair the uPA receptor and uPA inhibitory molecule (PAI-1) expressions. Meanwhile, the mRNA expression of uPA was inhibited via moscatilin in a concentration-dependent manner. In addition, the expression of phosphorylated Akt, rather than ERK1/2, was inhibited by moscatilin treatment. The expression of phosphor-IκBα, and -p65, as well as κB-luciferase activity were also repressed after moscatilin treatment. Transfection of constitutively active Akt (Myr-Akt) obviously restored the moscatilin-inhibited the activation of NF-κB and uPA, and cancer invasion in HCC cells. Taken together, these results suggest that moscatilin impedes HCC invasion and uPA expression through the Akt/NF-κB signaling pathway. Moscatilin might serve as a potential anti-metastatic agent against the disease progression of human HCC.


Asunto(s)
Antineoplásicos Fitogénicos/farmacología , Compuestos de Bencilo/farmacología , Movimiento Celular/efectos de los fármacos , FN-kappa B/genética , Proteínas Proto-Oncogénicas c-akt/genética , Activador de Plasminógeno de Tipo Uroquinasa/genética , Animales , Línea Celular Tumoral , Proliferación Celular/efectos de los fármacos , Embrión de Pollo , Membrana Corioalantoides/irrigación sanguínea , Membrana Corioalantoides/efectos de los fármacos , Factor 4E Eucariótico de Iniciación/genética , Factor 4E Eucariótico de Iniciación/metabolismo , Regulación Neoplásica de la Expresión Génica , Hepatocitos/efectos de los fármacos , Hepatocitos/metabolismo , Hepatocitos/patología , Humanos , Metaloproteinasa 2 de la Matriz/genética , Metaloproteinasa 2 de la Matriz/metabolismo , Metaloproteinasa 9 de la Matriz/genética , Metaloproteinasa 9 de la Matriz/metabolismo , FN-kappa B/antagonistas & inhibidores , FN-kappa B/metabolismo , Neovascularización Patológica/genética , Neovascularización Patológica/metabolismo , Neovascularización Patológica/prevención & control , Proteínas Proto-Oncogénicas c-akt/antagonistas & inhibidores , Proteínas Proto-Oncogénicas c-akt/metabolismo , Proteínas Quinasas S6 Ribosómicas 70-kDa/genética , Proteínas Quinasas S6 Ribosómicas 70-kDa/metabolismo , Transducción de Señal , Serina-Treonina Quinasas TOR/genética , Serina-Treonina Quinasas TOR/metabolismo , Activador de Plasminógeno de Tipo Uroquinasa/antagonistas & inhibidores , Activador de Plasminógeno de Tipo Uroquinasa/metabolismo
3.
Oxid Med Cell Longev ; 2020: 5363546, 2020.
Artículo en Inglés | MEDLINE | ID: mdl-32064026

RESUMEN

The present study was performed to evaluate the antioxidant and intestinal protective effects of baicalin-copper on deoxynivalenol-challenged piglets. Forty weaned piglets were randomly divided into four groups and assigned to different diets: (1) basal diet (Con), (2) 4 mg/kg deoxynivalenol of basal diet (DON), (3) 5 g/kg baicalin-copper of basal diet (BCU); and (4) 4 mg/kg deoxynivalenol + 5 g/kg baicalin-copper of basal diet (DBCU). The results showed that the ADFI and ADG of piglets in the DON group were markedly lower than those in the Con group, but the ADFI and ADG of the DBCU group were not significantly different from those of the Con group. In piglets fed a DON-contaminated diet, dietary supplementation with BCU significantly decreased the mRNA levels of P70S6K, 4E-BP1, and HSP70 in the liver, the protein expression of HO-1 in the jejunum, and the expression of p-Nrf2 and p-NF-κB in the ileum but increased Mn-SOD activity in serum. Dietary supplementation with BCU increased jejunal maltase, ZIP4 and MT mRNA levels, and serum concentrations of Arg, Val, Ile, Leu, Lys, and Tyr in DON-contaminated piglets. In summary, BCU can alleviate the growth impairment induced by DON and enhance antioxidant capacity and nutrition absorption in piglets fed DON-contaminated diets.


Asunto(s)
Antioxidantes/metabolismo , Flavonoides/farmacología , Íleon/efectos de los fármacos , Yeyuno/efectos de los fármacos , Estrés Oxidativo/efectos de los fármacos , Tricotecenos/toxicidad , Aminoácidos/sangre , Alimentación Animal , Animales , Proteínas de Transporte de Catión/genética , Proteínas de Transporte de Catión/metabolismo , Cobre/química , Dieta , Suplementos Dietéticos , Factor 4E Eucariótico de Iniciación/genética , Factor 4E Eucariótico de Iniciación/metabolismo , Proteínas HSP70 de Choque Térmico/genética , Proteínas HSP70 de Choque Térmico/metabolismo , Hemo-Oxigenasa 1/genética , Hemo-Oxigenasa 1/metabolismo , Íleon/metabolismo , Yeyuno/citología , Yeyuno/enzimología , Yeyuno/metabolismo , Hígado/metabolismo , Factor 2 Relacionado con NF-E2/genética , Factor 2 Relacionado con NF-E2/metabolismo , FN-kappa B/genética , FN-kappa B/metabolismo , Estrés Oxidativo/genética , Proteínas Quinasas S6 Ribosómicas 70-kDa/genética , Proteínas Quinasas S6 Ribosómicas 70-kDa/metabolismo , Suero/enzimología , Suero/metabolismo , Superóxido Dismutasa-1/sangre , Porcinos , alfa-Glucosidasas/genética , alfa-Glucosidasas/metabolismo
4.
J Med Food ; 23(1): 29-36, 2020 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-31532323

RESUMEN

Muscle atrophy, which is characterized by a decrease in muscle mass, function, and protein content, can be caused by aging, disease, and physical inactivity. Red bean or Adzuki bean (Vigna angularis) has been consumed as an edible legume. Red bean possesses various functional properties, such as antidiabetes, antiaging, anti-inflammatory, anticancer, and hepatoprotective activities. However, little is known about its potential inhibitory effect on muscle atrophy. In this study, we investigated the inhibitory effect of red bean extract (RBE) on muscle atrophy in an immobilized hindlimb muscle of C57BL/6J mice. RBE dose-dependently increased grip strength, exercise endurance, muscle weight, and myofiber area. At the molecular level, RBE significantly reduced the mRNA expression of proteolysis-related genes, such as muscle ring finger and muscle atrophy F-box by preventing the translocation of Forkhead box 3. RBE also activated the phosphatidylinositol 3 kinase/Akt pathway, subsequently stimulating the mammalian target of rapamycin/70-kDa ribosomal protein S6 kinase/eukaryotic initiation factor 4E binding protein 1 pathway involved in protein synthesis. Overall, red bean could be used as a functional food ingredient or therapeutic agent to inhibit muscle atrophy.


Asunto(s)
Músculo Esquelético/efectos de los fármacos , Atrofia Muscular/tratamiento farmacológico , Extractos Vegetales/uso terapéutico , Vigna/química , Aminoácidos de Cadena Ramificada , Animales , Biomarcadores/análisis , Factor 4E Eucariótico de Iniciación/metabolismo , Ratones , Ratones Endogámicos C57BL , Distribución Aleatoria , Restricción Física , Proteínas Quinasas S6 Ribosómicas 70-kDa/metabolismo , Serina-Treonina Quinasas TOR/metabolismo
5.
Med Sci Sports Exerc ; 50(8): 1540-1548, 2018 08.
Artículo en Inglés | MEDLINE | ID: mdl-29554013

RESUMEN

PURPOSE: Neuromuscular electrical stimulation (NMES) is commonly used in rehabilitation settings to increase muscle mass and strength. However, the effects of NMES on muscle growth are not clear and no human studies have compared anabolic signaling between low-frequency (LF) and high-frequency (HF) NMES. The purpose of this study was to determine the skeletal muscle anabolic signaling response to an acute bout of LF- and HF-NMES. METHODS: Eleven young healthy volunteers (6 men, 5 women) received an acute bout of LF-NMES (20 Hz) and HF-NMES (60 Hz). Muscle biopsies were obtained from the vastus lateralis muscle before the first NMES treatment and 30 min after each NMES treatment. Phosphorylation of the following key anabolic signaling proteins was measured by Western blot, and proteins are expressed as a ratio of phosphorylated to total: mammalian target of rapamycin, p70-S6 kinase 1, and eukaryotic initiation factor 4E binding protein 1. RESULTS: Compared with pre-NMES, phosphorylation of mammalian target of rapamycin was upregulated 40.2% for LF-NMES (P = 0.018) and 68.4% for HF-NMES (P < 0.0001), and HF-NMES was 29.3% greater than LF-NMES (P = 0.026). Phosphorylation of p70-S6 kinase 1 after HF-NMES was 96.6% higher than pre-NMES (P = 0.001) and was not different between pre-NMES and LF-NMES (although it was 50.4% higher after LF-NMES) or LF- and HF-NMES (P > 0.05). There were no differences between treatment conditions for eukaryotic initiation factor 4E binding protein 1 phosphorylation (P > 0.05). CONCLUSIONS: An acute bout of LF- and HF-NMES upregulated anabolic signaling with HF-NMES producing a greater anabolic response compared with LF-NMES, suggesting that HF stimulation may provide a stronger stimulus for processes that initiate muscle hypertrophy. In addition, the stimulation frequency parameter should be considered by clinicians in the design of optimal NMES treatment protocols.


Asunto(s)
Estimulación Eléctrica/métodos , Diana Mecanicista del Complejo 1 de la Rapamicina/metabolismo , Unión Neuromuscular/metabolismo , Músculo Cuádriceps/crecimiento & desarrollo , Músculo Cuádriceps/metabolismo , Transducción de Señal , Adulto , Estudios Cruzados , Terapia por Estimulación Eléctrica/métodos , Factor 4E Eucariótico de Iniciación/metabolismo , Femenino , Humanos , Masculino , Fuerza Muscular/fisiología , Músculo Cuádriceps/inervación , Entrenamiento de Fuerza , Proteínas Quinasas S6 Ribosómicas 70-kDa/metabolismo , Regulación hacia Arriba , Adulto Joven
6.
Mol Plant Microbe Interact ; 30(9): 754-762, 2017 09.
Artículo en Inglés | MEDLINE | ID: mdl-28609214

RESUMEN

The viral protein genome-linked (VPg) of potyviruses is a protein covalently linked to the 5' end of viral RNA. It interacts with eIF4E, a component of the cellular translation initiation complex. It has been suggested that the 5' RNA-linked VPg could mimic the cellular mRNA cap, promoting synthesis of viral proteins. Here, we report evidence for recruitment of the plant eIF4E by Lettuce mosaic virus (LMV, potyvirus) particles via the 5' RNA-linked VPg. Analysis of the viral population was performed by enzyme-linked immunosorbent assay-based tests, either with crude extracts of LMV-infected tissues or purified viral particles. In both cases, LMV-VPg and LMV-eIF4E subpopulations could be detected. After reaching a maximum within the first 2 weeks postinoculation, these populations decreased and very few labeled particles were found later than 3 weeks postinoculation. The central domain of VPg (CD-VPg) was found to be exposed at the surface of the particles. Using a purified recombinant lettuce eIF4E and CD-VPg-specific antibodies, we demonstrate that the plant factor binds to the VPg via its central domain. Moreover, the plant eIF4E factor could be imaged at one end of the particles purified from LMV plant extracts, by immunoredox atomic force microscopy coupled to scanning electrochemical microscopy. We discuss the biological significance of these results.


Asunto(s)
Factor 4E Eucariótico de Iniciación/metabolismo , Genoma Viral , Lactuca/virología , Potyvirus/metabolismo , ARN Viral/metabolismo , Proteínas Virales/metabolismo , Virión/metabolismo , Anticuerpos , Proteínas de la Cápside/metabolismo , Microscopía de Fuerza Atómica , Oxidación-Reducción , Enfermedades de las Plantas/virología , Unión Proteica , Recombinación Genética/genética
7.
Am J Physiol Cell Physiol ; 310(11): C874-84, 2016 Jun 01.
Artículo en Inglés | MEDLINE | ID: mdl-27053525

RESUMEN

Protein synthesis is stimulated by resistance exercise and intake of amino acids, in particular leucine. Moreover, activation of mammalian target of rapamycin complex 1 (mTORC1) signaling by leucine is potentiated by the presence of other essential amino acids (EAA). However, the contribution of the branched-chain amino acids (BCAA) to this effect is yet unknown. Here we compare the stimulatory role of leucine, BCAA, and EAA ingestion on anabolic signaling following exercise. Accordingly, eight trained volunteers completed four sessions of resistance exercise during which they ingested either placebo, leucine, BCAA, or EAA (including the BCAA) in random order. Muscle biopsies were taken at rest, immediately after exercise, and following 90 and 180 min of recovery. Following 90 min of recovery the activity of S6 kinase 1 (S6K1) was greater than at rest in all four trials (Placebo

Asunto(s)
Aminoácidos de Cadena Ramificada/administración & dosificación , Aminoácidos Esenciales/administración & dosificación , Leucina/administración & dosificación , Complejos Multiproteicos/agonistas , Músculo Esquelético/efectos de los fármacos , Entrenamiento de Fuerza , Proteínas Adaptadoras Transductoras de Señales/metabolismo , Adulto , Biopsia , Glucemia/metabolismo , Proteínas de Ciclo Celular , Metabolismo Energético/efectos de los fármacos , Factor 4E Eucariótico de Iniciación/metabolismo , Voluntarios Sanos , Humanos , Insulina/sangre , Ácido Láctico/sangre , Masculino , Diana Mecanicista del Complejo 1 de la Rapamicina , Complejos Multiproteicos/metabolismo , Músculo Esquelético/enzimología , Fosfoproteínas/metabolismo , Fosforilación , Biosíntesis de Proteínas/efectos de los fármacos , Proteínas Quinasas S6 Ribosómicas 70-kDa/metabolismo , Transducción de Señal/efectos de los fármacos , Serina-Treonina Quinasas TOR/metabolismo , Factores de Tiempo , Resultado del Tratamiento
8.
Molecules ; 21(2)2016 Feb 06.
Artículo en Inglés | MEDLINE | ID: mdl-26861281

RESUMEN

Preparations of Deguelia duckeana, known in Brazil as timbó, are used by indigenous people to kill fish. Reinvestigation of its extracts resulted in the isolation and identification of 11 known flavonoids identified as 3,5,4'-trimethoxy-4-prenylstilbene (1), 4-methoxyderricidine (2), lonchocarpine (3), 4-hydroxylonchocarpine (4), 4-methoxylonchocarpine (5), 5-hydroxy-4',7-dimethoxy-6-prenylflavanone (6), 4'-hydroxyisolonchocarpine (7), 4'-methoxyisolonchocarpine (8), 3',4',7-trimethoxyflavone (9), 3',4'-methylenedioxy-7-methoxyflavone (10), and 2,2-dimethyl-chromone-5,4'-hydroxy-5'-methoxyflavone (11). Except for 1, 3, and 4 all of these flavonoids have been described for the first time in D. duckeana and the flavanone 6 for the first time in nature. Compounds 2, 3, 4, 7, 9, and 10 were studied for their potential to induce cell death in neuronal SK-N-SH cells. Only the chalcone 4 and the flavanone 7 significantly induced lactate dehydrogenase (LDH) release, which was accompanied by activation of caspase-3 and impairment of energy homeostasis in the MTT assay and may explain the killing effect on fish. Interestingly, the flavone 10 reduced cell metabolism in the MTT assay without inducing cytotoxicity in the LDH assay. Furthermore, the flavonoids 2, 3, 4, 7, and 10 induced phosphorylation of the AMP-activated protein kinase (AMPK) and the eukaryotic elongation factor 2 (eEF2). The initiation factor eIF4E was dephosphorylated in the presence of these compounds. The initiation factor eIF2alpha was not affected. Further studies are needed to elucidate the importance of the observed effects on protein synthesis and potential therapeutic perspectives.


Asunto(s)
Fabaceae/química , Flavonoides/toxicidad , Extractos Vegetales/toxicidad , Procesamiento Proteico-Postraduccional/efectos de los fármacos , Adenilato Quinasa/metabolismo , Línea Celular Tumoral , Supervivencia Celular/efectos de los fármacos , Factor 2 Eucariótico de Iniciación/metabolismo , Factor 4E Eucariótico de Iniciación/metabolismo , Flavonoides/aislamiento & purificación , Humanos , Factor 2 de Elongación Peptídica/metabolismo , Fosforilación , Extractos Vegetales/aislamiento & purificación
9.
Sci Rep ; 6: 18800, 2016 Jan 05.
Artículo en Inglés | MEDLINE | ID: mdl-26728896

RESUMEN

The eukaryotic translation initiation factor 4E (eIF4E) is considered as a key survival protein involved in cell cycle progression, transformation and apoptosis resistance. Herein, we demonstrate that medicinal plant derivative 3-AWA (from Withaferin A) suppressed the proliferation and metastasis of CaP cells through abrogation of eIF4E activation and expression via c-FLIP dependent mechanism. This translational attenuation prevents the de novo synthesis of major players of metastatic cascades viz. c-FLIP, c-Myc and cyclin D1. Moreover, the suppression of c-FLIP due to inhibition of translation initiation complex by 3-AWA enhanced FAS trafficking, BID and caspase 8 cleavage. Further ectopically restored c-Myc and GFP-HRas mediated activation of eIF4E was reduced by 3-AWA in transformed NIH3T3 cells. Detailed underlying mechanisms revealed that 3-AWA inhibited Ras-Mnk and PI3-AKT-mTOR, two major pathways through which eIF4E converges upon eIF4F hub. In addition to in vitro studies, we confirmed that 3-AWA efficiently suppressed tumor growth and metastasis in different mouse models. Given that 3-AWA inhibits c-FLIP through abrogation of translation initiation by co-targeting mTOR and Mnk-eIF4E, it (3-AWA) can be exploited as a lead pharmacophore for promising anti-cancer therapeutic development.


Asunto(s)
Adenosina Trifosfatasas/metabolismo , Proteínas de Transporte de Catión/metabolismo , Fosfatidilinositol 3-Quinasas/metabolismo , Proteínas Proto-Oncogénicas c-akt/metabolismo , Transducción de Señal , Serina-Treonina Quinasas TOR/metabolismo , Proteínas ras/metabolismo , Proteínas Adaptadoras Transductoras de Señales , Animales , Proteína Reguladora de Apoptosis Similar a CASP8 y FADD/genética , Proteína Reguladora de Apoptosis Similar a CASP8 y FADD/metabolismo , Carcinoma de Ehrlich/genética , Carcinoma de Ehrlich/metabolismo , Carcinoma de Ehrlich/patología , Proteínas Portadoras/metabolismo , Caspasa 8/metabolismo , Proteínas de Ciclo Celular , Línea Celular Tumoral , Movimiento Celular/genética , ATPasas Transportadoras de Cobre , Modelos Animales de Enfermedad , Factor 4E Eucariótico de Iniciación/metabolismo , Factores Eucarióticos de Iniciación , Humanos , Masculino , Ratones , Metástasis de la Neoplasia , Fosfoproteínas/metabolismo , Fosforilación , Biosíntesis de Proteínas/efectos de los fármacos , Transporte de Proteínas , Witanólidos/farmacología , Receptor fas/metabolismo
10.
Amino Acids ; 48(1): 257-267, 2016 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-26334346

RESUMEN

Suboptimal nutrient intake represents a limiting factor for growth and long-term survival of low-birth weight infants. The objective of this study was to determine if in neonates who can consume only 70 % of their protein and energy requirements for 8 days, enteral leucine supplementation will upregulate the mammalian target of rapamycin (mTOR) pathway in skeletal muscle, leading to an increase in protein synthesis and muscle anabolism. Nineteen 4-day-old piglets were fed by gastric tube 1 of 3 diets, containing (kg body weight(-1) · day(-1)) 16 g protein and 190 kcal (CON), 10.9 g protein and 132 kcal (R), or 10.8 g protein + 0.2 % leucine and 136 kcal (RL) at 4-h intervals for 8 days. On day 8, plasma AA and insulin levels were measured during 6 post-feeding intervals, and muscle protein synthesis rate and mTOR signaling proteins were determined at 120 min post-feeding. At 120 min, leucine was highest in RL (P < 0.001), whereas insulin, isoleucine and valine were lower in RL and R compared to CON (P < 0.001). Compared to RL and R, the CON diet increased (P < 0.01) body weight, protein synthesis, phosphorylation of S6 kinase (p-S6K1) and 4E-binding protein (p-4EBP1), and activation of eukaryotic initiation factor 4 complex (eIF4E · eIF4G). RL increased (P ≤ 0.01) p-S6K1, p-4EBP1 and eIF4E · eIF4G compared to R. In conclusion, when protein and energy intakes are restricted for 8 days, leucine supplementation increases muscle mTOR activation, but does not improve body weight gain or enhance skeletal muscle protein synthesis in neonatal pigs.


Asunto(s)
Alimentación Animal/análisis , Suplementos Dietéticos/análisis , Leucina/metabolismo , Proteínas Musculares/metabolismo , Biosíntesis de Proteínas , Porcinos/metabolismo , Serina-Treonina Quinasas TOR/metabolismo , Animales , Metabolismo Energético , Factor 4E Eucariótico de Iniciación/genética , Factor 4E Eucariótico de Iniciación/metabolismo , Femenino , Insulina/metabolismo , Masculino , Proteínas Musculares/genética , Músculo Esquelético/crecimiento & desarrollo , Músculo Esquelético/metabolismo , Fosforilación , Porcinos/genética , Porcinos/crecimiento & desarrollo
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