Browsing by Author "Serrano Larrea, Valentina"

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    El ácido nicotínico aumenta el transporte celular de colesterol de las lipoproteínas de alta densidad en pacientes con hipoalfalipoproteinemia
    (2015) Figueroa, Catalina; Droppelmann Droppelmann, Katherine Ann; Quinones, Verónica; Amigo Boker, Ludwig Peter; Mendoza, Camila; Serrano Larrea, Valentina; Véjar, Margarita; Maiz Gurruchaga, Manuel Alberto; Rigotti Rivera, Attilio
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    Antihypertensive Agents in Older Adults : A Systematic Review and Meta-Analysis of Randomized Clinical Trials
    (2019) Murad, Mohammad Hassan; Larrea Mantilla, Laura; Haddad, Abdullah; Spencer Bonilla, Gabriela; Serrano Larrea, Valentina; Rodríguez Gutiérrez, René; Álvarez Villalobos, Neri; Benkhadra, Khaled; Gionfriddo, Michael R.; Prokop, Larry J.; Brito, Juan P.; Ponce, Oscar J.
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    APOA5 Q97X Mutation Identified through homozygosity mapping causes severe hypertriglyceridemia in a Chilean consanguineous family
    (2012) Dussaillant, Catalina; Serrano Larrea, Valentina; Maiz Gurruchaga, Manuel Alberto; Eyheramendy Duerr, Susana; Cataldo Bascuñan, Luis Rodrigo; Smalley Meylan, Susan Valerie; Rigotti Rivera, Attilio; Rubio, Lorena.; Lagos Arévalo, Carlos Fernando; Santos Martín, José Luis
    Abstract Background Severe hypertriglyceridemia (HTG) has been linked to defects in LPL, APOC2, APOA5, LMF1 and GBIHBP1 genes. However, a number of severe HTG cases are probably caused by as yet unidentified mutations. Very high triglyceride plasma levels (>112 mmol/L at diagnosis) were found in two sisters of a Chilean consanguineous family, which is strongly suggestive of a recessive highly penetrant mutation. The aim of this study was to determine the genetic locus responsible for the severe HTG in this family. Methods We carried out a genome-wide linkage study with nearly 300,000 biallelic markers (Illumina Human CytoSNP-12 panel). Using the homozygosity mapping strategy, we searched for chromosome regions with excess of homozygous genotypes in the affected cases compared to non-affected relatives. Results A large homozygous segment was found in the long arm of chromosome 11, with more than 2,500 consecutive homozygous SNP shared by the proband with her affected sister, and containing the APOA5/A4/C3/A1 cluster. Direct sequencing of the APOA5 gene revealed a known homozygous nonsense Q97X mutation (p.Gln97Ter) found in both affected sisters but not in non-affected relatives nor in a sample of unrelated controls. Conclusion The Q97X mutation of the APOA5 gene in homozygous status is responsible for the severe hypertriglyceridemia in this family. We have shown that homozygosity mapping correctly pinpointed the genomic region containing the gene responsible for severe hypertriglyceridemia in this consanguineous Chilean family.
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    Cetoacidosis diabética : Casuística 2008-2012, epidemiología y fisiopatología
    (2014) Olmos Coelho, Pablo Roberto; Donoso Henríquez, Aníbal Tomás; Arab Verdugo, Juan Pablo; Niklitschek, I.; Mertens, N.; Arce, E.; Lemus, R.; Serrano Larrea, Valentina; Grassi Corrales, Bruno; Strodthoff Simunovic, Kristel; Abbott Cáceres, Eduardo Francisco; Aizman, Andrés; González, M.
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    Does Health Coaching Grow Capacity in Cancer Survivors? A Systematic Review
    (2018) Barakat, Suzette; Boehmer, Kasey; Abdelrahim, Marwan; Ahn, Sangwoo; Al-Khateeb, Addulrahman; Älvarez Villalobos Neri; Prokop, Larry; Erwin, Patricia J.; Fleming, Kirsten; Serrano Larrea, Valentina; Spencer Bonilla, Gabriela; Murad, Mohammad Hassan
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    Effect of estrogen replacement therapy on bone and cardiovascular outcomes in women with turner syndrome : a systematic review and meta-analysis
    (2017) Serrano Larrea, Valentina; Cintron, D.; Rodríguez, R.; Latortue, P.; Erwin, P.; Murad, M.
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    Estrogen-based hormone therapy in women with primary ovarian insufficiency : a systematic review
    (2017) Burgos, N.; Cintron, D.; Latortue, P.; Serrano Larrea, Valentina; Gutiérrez, R.; Faubion, S.; Spencer, G.; Erwin, P.; Murad, M.
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    Evaluación de la carga de tratamiento en pacientes operados de cirugía bariátrica
    (2022) Pueyes Huencho, Valentina Estevania; Serrano Larrea, Valentina; Pontificia Universidad Católica de Chile. Escuela de Medicina
    Antecedentes: La cirugía bariátrica (CB) es la alternativas de tratamiento más efectivas para perder peso, junto a mejoría de comorbilidades y calidad de vida (CV) en personas que viven con obesidad. Durante el seguimiento postquirúrgico prolongado, los pacientes podrían percibir o no la “carga de tratamiento” (CDT) al adherir a los protocolos de autocuidado, sin embargo, no ha sido descrita en este grupo. Objetivo: Traducir, adaptar y validar al español el instrumento “PETS” para evaluación de CDT en personas con CB y describir la CDT y su asociación con parámetros relevantes de salud. Diseño: Estudio transversal de autoreporte, mediante instrumentos específicos para evaluar CDT y CV. Incluyó 51 adultos operados de CB los años 2019 y 2020 en Red de Salud UC Christus. Para validación de “PETS” realizamos análisis de consistencia interna en cada dimensión. Los datos se expresaron como medias (DS) y proporciones. Para diferencias en comparación de frecuencias se consideró la no superposición de IC 95% y para asociaciones entre CDT y CV, %EPP, nº de diagnósticos y nº de medicamentos prescritos se obtuvo coeficiente de correlación de Spearman. Resultados: La edad media de los participantes fue 41 años (± 10) y el promedio de IMC actual 26.9 kg/m2 (± 4.5). Las escalas del “PETS” mostraron una consistencia interna α entre 0.7 a 0.93. Los puntajes de PETS más altos surgieron en las dimensiones “gastos médicos y sanitarios” (45.1 ± 16.2), “citas médicas” (36.2 ± 25.1) e “información médica” (34.2 ± 11.7). Se observó asociación inversa entre CDT y CV, y entre algunas dimensiones de CDT y %EPP. No existió asociación entre CDT y nº de medicamentos prescritos, ni de diagnósticos. Conclusiones: “PETS” en español es válido para la evaluar la CDT en este grupo de personas. Los pacientes perciben una mayor CDT en las dimensiones que se asocian estrecha e inversamente con CV y %EPP.
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    GLUCOSE EFFECT IN THE EXPRESSION OF ENDOTHELIAL LIPASE IN HUMAN ENDOTHELIAL CELLS AND IN PATIENTS WITH DIABETES MELLITUS TYPE 2
    (2011) Pierart, Camila; Serrano Larrea, Valentina; Rubio Quiroz, Lorena Alejandra; Ebensperger González, Roberto Alejandro; Foncea Ávila, Rocío Eugenia
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    Identification and functional analysis of missense mutations in the lecithin cholesterol acyltransferase gene in a Chilean patient with hypoalphalipoproteinemia
    (2019) Tobar, Hugo E.; Cataldo Bascuñan, Luis Rodrigo; González, Trinidad.; Rodríguez, Ricardo.; Serrano Larrea, Valentina; Arteaga Ll., Antonio; Vicuña Zauschkevich, Lucas.; Miranda Marín, José Patricio; Álvarez-Mercado, Ana.; Lagos, Carlos.
    Abstract Background Lecithin-cholesterol acyltransferase (LCAT) is a plasma enzyme that esterifies cholesterol in high- and low-density lipoproteins (HDL and LDL). Mutations in LCAT gene causes familial LCAT deficiency, which is characterized by very low plasma HDL-cholesterol levels (Hypoalphalipoproteinemia), corneal opacity and anemia, among other lipid-related traits. Our aim is to evaluate clinical/biochemical features of a Chilean family with a proband showing clinical signs of familial LCAT deficiency, as well as to identify and assess the functional effects of LCAT mutations. Methods An adult female proband with hypoalphalipoproteinemia, corneal opacity and mild anemia, as well as her first-degree relatives, were recruited for clinical, biochemical, genetic, in-silico and in-vitro LCAT analysis. Sequencing of exons and intron-exon boundaries was performed to identify mutations. Site-directed mutagenesis was carried out to generate plasmids containing cDNA with wild type or mutant sequences. Such expression vectors were transfected to HEK-239 T cells to asses the effect of LCAT variants in expression, synthesis, secretion and enzyme activity. In-silico prediction analysis and molecular modeling was also used to evaluate the effect of LCAT variants. Results LCAT sequencing identified rare p.V333 M and p.M404 V missense mutations in compound heterozygous state in the proband, as well the common synonymous p.L363 L variant. LCAT protein was detected in proband’s plasma, but with undetectable enzyme activity compared to control relatives. HEK-293 T transfected cells with vector expression plasmids containing either p.M404 V or p.V333 M cDNA showed detectable LCAT protein expression both in supernatants and lysates from cultured cells, but with much lower enzyme activity compared to cells transfected with the wild-type sequence. Bioinformatic analyses also supported a causal role of such rare variations in LCAT lack of function. Additionally, the proband carried the minor allele of the synonymous p.L363 L variant. However, this variant is unlikely to affect the clinical phenotype of the proband given its relatively high frequency in the Chilean population (4%) and its small putative effect on plasma HDL-cholesterol levels. Conclusion Genetic, biochemical, in vitro and in silico analyses indicate that the rare mutations p.M404 V and p.V333 M in LCAT gene lead to suppression of LCAT enzyme activity and cause clinical features of familial LCAT deficiency.Abstract Background Lecithin-cholesterol acyltransferase (LCAT) is a plasma enzyme that esterifies cholesterol in high- and low-density lipoproteins (HDL and LDL). Mutations in LCAT gene causes familial LCAT deficiency, which is characterized by very low plasma HDL-cholesterol levels (Hypoalphalipoproteinemia), corneal opacity and anemia, among other lipid-related traits. Our aim is to evaluate clinical/biochemical features of a Chilean family with a proband showing clinical signs of familial LCAT deficiency, as well as to identify and assess the functional effects of LCAT mutations. Methods An adult female proband with hypoalphalipoproteinemia, corneal opacity and mild anemia, as well as her first-degree relatives, were recruited for clinical, biochemical, genetic, in-silico and in-vitro LCAT analysis. Sequencing of exons and intron-exon boundaries was performed to identify mutations. Site-directed mutagenesis was carried out to generate plasmids containing cDNA with wild type or mutant sequences. Such expression vectors were transfected to HEK-239 T cells to asses the effect of LCAT variants in expression, synthesis, secretion and enzyme activity. In-silico prediction analysis and molecular modeling was also used to evaluate the effect of LCAT variants. Results LCAT sequencing identified rare p.V333 M and p.M404 V missense mutations in compound heterozygous state in the proband, as well the common synonymous p.L363 L variant. LCAT protein was detected in proband’s plasma, but with undetectable enzyme activity compared to control relatives. HEK-293 T transfected cells with vector expression plasmids containing either p.M404 V or p.V333 M cDNA showed detectable LCAT protein expression both in supernatants and lysates from cultured cells, but with much lower enzyme activity compared to cells transfected with the wild-type sequence. Bioinformatic analyses also supported a causal role of such rare variations in LCAT lack of function. Additionally, the proband carried the minor allele of the synonymous p.L363 L variant. However, this variant is unlikely to affect the clinical phenotype of the proband given its relatively high frequency in the Chilean population (4%) and its small putative effect on plasma HDL-cholesterol levels. Conclusion Genetic, biochemical, in vitro and in silico analyses indicate that the rare mutations p.M404 V and p.V333 M in LCAT gene lead to suppression of LCAT enzyme activity and cause clinical features of familial LCAT deficiency.Abstract Background Lecithin-cholesterol acyltransferase (LCAT) is a plasma enzyme that esterifies cholesterol in high- and low-density lipoproteins (HDL and LDL). Mutations in LCAT gene causes familial LCAT deficiency, which is characterized by very low plasma HDL-cholesterol levels (Hypoalphalipoproteinemia), corneal opacity and anemia, among other lipid-related traits. Our aim is to evaluate clinical/biochemical features of a Chilean family with a proband showing clinical signs of familial LCAT deficiency, as well as to identify and assess the functional effects of LCAT mutations. Methods An adult female proband with hypoalphalipoproteinemia, corneal opacity and mild anemia, as well as her first-degree relatives, were recruited for clinical, biochemical, genetic, in-silico and in-vitro LCAT analysis. Sequencing of exons and intron-exon boundaries was performed to identify mutations. Site-directed mutagenesis was carried out to generate plasmids containing cDNA with wild type or mutant sequences. Such expression vectors were transfected to HEK-239 T cells to asses the effect of LCAT variants in expression, synthesis, secretion and enzyme activity. In-silico prediction analysis and molecular modeling was also used to evaluate the effect of LCAT variants. Results LCAT sequencing identified rare p.V333 M and p.M404 V missense mutations in compound heterozygous state in the proband, as well the common synonymous p.L363 L variant. LCAT protein was detected in proband’s plasma, but with undetectable enzyme activity compared to control relatives. HEK-293 T transfected cells with vector expression plasmids containing either p.M404 V or p.V333 M cDNA showed detectable LCAT protein expression both in supernatants and lysates from cultured cells, but with much lower enzyme activity compared to cells transfected with the wild-type sequence. Bioinformatic analyses also supported a causal role of such rare variations in LCAT lack of function. Additionally, the proband carried the minor allele of the synonymous p.L363 L variant. However, this variant is unlikely to affect the clinical phenotype of the proband given its relatively high frequency in the Chilean population (4%) and its small putative effect on plasma HDL-cholesterol levels. Conclusion Genetic, biochemical, in vitro and in silico analyses indicate that the rare mutations p.M404 V and p.V333 M in LCAT gene lead to suppression of LCAT enzyme activity and cause clinical features of familial LCAT deficiency.Abstract Background Lecithin-cholesterol acyltransferase (LCAT) is a plasma enzyme that esterifies cholesterol in high- and low-density lipoproteins (HDL and LDL). Mutations in LCAT gene causes familial LCAT deficiency, which is characterized by very low plasma HDL-cholesterol levels (Hypoalphalipoproteinemia), corneal opacity and anemia, among other lipid-related traits. Our aim is to evaluate clinical/biochemical features of a Chilean family with a proband showing clinical signs of familial LCAT deficiency, as well as to identify and assess the functional effects of LCAT mutations. Methods An adult female proband with hypoalphalipoproteinemia, corneal opacity and mild anemia, as well as her first-degree relatives, were recruited for clinical, biochemical, genetic, in-silico and in-vitro LCAT analysis. Sequencing of exons and intron-exon boundaries was performed to identify mutations. Site-directed mutagenesis was carried out to generate plasmids containing cDNA with wild type or mutant sequences. Such expression vectors were transfected to HEK-239 T cells to asses the effect of LCAT variants in expression, synthesis, secretion and enzyme activity. In-silico prediction analysis and molecular modeling was also used to evaluate the effect of LCAT variants. Results LCAT sequencing identified rare p.V333 M and p.M404 V missense mutations in compound heterozygous state in the proband, as well the common synonymous p.L363 L variant. LCAT protein was detected in proband’s plasma, but with undetectable enzyme activity compared to control relatives. HEK-293 T transfected cells with vector expression plasmids containing either p.M404 V or p.V333 M cDNA showed detectable LCAT protein expression both in supernatants and lysates from cultured cells, but with much lower enzyme activity compared to cells transfected with the wild-type sequence. Bioinformatic analyses also supported a causal role of such rare variations in LCAT lack of function. Additionally, the proband carried the minor allele of the synonymous p.L363 L variant. However, this variant is unlikely to affect the clinical phenotype of the proband given its relatively high frequency in the Chilean population (4%) and its small putative effect on plasma HDL-cholesterol levels. Conclusion Genetic, biochemical, in vitro and in silico analyses indicate that the rare mutations p.M404 V and p.V333 M in LCAT gene lead to suppression of LCAT enzyme activity and cause clinical features of familial LCAT deficiency.Abstract Background Lecithin-cholesterol acyltransferase (LCAT) is a plasma enzyme that esterifies cholesterol in high- and low-density lipoproteins (HDL and LDL). Mutations in LCAT gene causes familial LCAT deficiency, which is characterized by very low plasma HDL-cholesterol levels (Hypoalphalipoproteinemia), corneal opacity and anemia, among other lipid-related traits. Our aim is to evaluate clinical/biochemical features of a Chilean family with a proband showing clinical signs of familial LCAT deficiency, as well as to identify and assess the functional effects of LCAT mutations. Methods An adult female proband with hypoalphalipoproteinemia, corneal opacity and mild anemia, as well as her first-degree relatives, were recruited for clinical, biochemical, genetic, in-silico and in-vitro LCAT analysis. Sequencing of exons and intron-exon boundaries was performed to identify mutations. Site-directed mutagenesis was carried out to generate plasmids containing cDNA with wild type or mutant sequences. Such expression vectors were transfected to HEK-239 T cells to asses the effect of LCAT variants in expression, synthesis, secretion and enzyme activity. In-silico prediction analysis and molecular modeling was also used to evaluate the effect of LCAT variants. Results LCAT sequencing identified rare p.V333 M and p.M404 V missense mutations in compound heterozygous state in the proband, as well the common synonymous p.L363 L variant. LCAT protein was detected in proband’s plasma, but with undetectable enzyme activity compared to control relatives. HEK-293 T transfected cells with vector expression plasmids containing either p.M404 V or p.V333 M cDNA showed detectable LCAT protein expression both in supernatants and lysates from cultured cells, but with much lower enzyme activity compared to cells transfected with the wild-type sequence. Bioinformatic analyses also supported a causal role of such rare variations in LCAT lack of function. Additionally, the proband carried the minor allele of the synonymous p.L363 L variant. However, this variant is unlikely to affect the clinical phenotype of the proband given its relatively high frequency in the Chilean population (4%) and its small putative effect on plasma HDL-cholesterol levels. Conclusion Genetic, biochemical, in vitro and in silico analyses indicate that the rare mutations p.M404 V and p.V333 M in LCAT gene lead to suppression of LCAT enzyme activity and cause clinical features of familial LCAT deficiency.Abstract Background Lecithin-cholesterol acyltransferase (LCAT) is a plasma enzyme that esterifies cholesterol in high- and low-density lipoproteins (HDL and LDL). Mutations in LCAT gene causes familial LCAT deficiency, which is characterized by very low plasma HDL-cholesterol levels (Hypoalphalipoproteinemia), corneal opacity and anemia, among other lipid-related traits. Our aim is to evaluate clinical/biochemical features of a Chilean family with a proband showing clinical signs of familial LCAT deficiency, as well as to identify and assess the functional effects of LCAT mutations. Methods An adult female proband with hypoalphalipoproteinemia, corneal opacity and mild anemia, as well as her first-degree relatives, were recruited for clinical, biochemical, genetic, in-silico and in-vitro LCAT analysis. Sequencing of exons and intron-exon boundaries was performed to identify mutations. Site-directed mutagenesis was carried out to generate plasmids containing cDNA with wild type or mutant sequences. Such expression vectors were transfected to HEK-239 T cells to asses the effect of LCAT variants in expression, synthesis, secretion and enzyme activity. In-silico prediction analysis and molecular modeling was also used to evaluate the effect of LCAT variants. Results LCAT sequencing identified rare p.V333 M and p.M404 V missense mutations in compound heterozygous state in the proband, as well the common synonymous p.L363 L variant. LCAT protein was detected in proband’s plasma, but with undetectable enzyme activity compared to control relatives. HEK-293 T transfected cells with vector expression plasmids containing either p.M404 V or p.V333 M cDNA showed detectable LCAT protein expression both in supernatants and lysates from cultured cells, but with much lower enzyme activity compared to cells transfected with the wild-type sequence. Bioinformatic analyses also supported a causal role of such rare variations in LCAT lack of function. Additionally, the proband carried the minor allele of the synonymous p.L363 L variant. However, this variant is unlikely to affect the clinical phenotype of the proband given its relatively high frequency in the Chilean population (4%) and its small putative effect on plasma HDL-cholesterol levels. Conclusion Genetic, biochemical, in vitro and in silico analyses indicate that the rare mutations p.M404 V and p.V333 M in LCAT gene lead to suppression of LCAT enzyme activity and cause clinical features of familial LCAT deficiency.
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    Lipid-Lowering Agents in Older Individuals : A Systematic Review and Meta-Analysis of Randomized Clinical Trials
    (2019) Ponce, O.J.; Larrea-Mantilla, L.; Hemmingsen, B.; Serrano Larrea, Valentina; Rodriguez-Gutierrez, R.; Spencer-Bonilla, G.; Alvarez-Villalobos, N.; Benkhadra, K.; Haddad, A.; Gionfriddo, M.R.; Prokop, L.J.; Brito, J.P.; Murad, M.H.
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    Minimally Disruptive Medicine for Patients with Diabetes
    (2017) Serrano Larrea, Valentina; Spencer, G.; Boehmer, K.; Montori, V.
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    Oxytocin for preventing postpartum haemorrhage (PPH) in non-facility birth settings
    (2015) Pantoja Calderón, Tomás; Abalos, E.; Chapman, E.; Vera Pérez-Gacitúa, Claudio Mauricio; Serrano Larrea, Valentina
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    Shared decision-making in the care of individuals with diabetes
    (2016) Serrano Larrea, Valentina; Rodríguez Gutiérrez, R.; Hargraves, I.; Gionfriddo, M. R.; Tamhane, S.; Montori, V.
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    The Efficacy and Adverse Events of Testosterone Replacement Therapy in Hypogonadal Men : A Systematic Review and Meta-Analysis of Randomized, Placebo-Controlled Trials
    (2018) Ponce, Oscar J.; Spencer Bonilla, Gabriela; Alvarez Villalobos, Neri; Serrano Larrea, Valentina; Singh Ospina, Naykky; Rodríguez Gutiérrez, René; Salcido Montenegro, Alejandro; Benkhadra, Raed; Prokop, Larry J.; Bhasin, Shalender; Brito, Juan P.
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    Toma de decisiones compartidas en la atención de pacientes con diabetes mellitus: un desafío para Latinoamérica
    (2017) Serrano Larrea, Valentina; Larrea, Laura; Rodríguez Gutiérrez, René; Spencer Bonilla, Gabriela; Málaga, Germán; Hargraves, Ian; Montori, Víctor M.
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    Tu-P7:141 Induction of endotelial dysfunction by homocysteine is mediated by a redox-sensitive map kinase signaling
    (2006) Foncea Ávila, Rocío Eugenia; Reyes, F.; Rubio Quiroz, Lorena Alejandra; Lagunas, R.; Serrano Larrea, Valentina; Maiz, A.; Ebensperger González, Roberto Alejandro