In patients with septic shock, excessive fluid administration can lead to increased morbidity and mortality. The aim of this study was to evaluate the association between fluid balance, acute kidney injury and mortality in patients with septic shock.
Methods
A study of cases and controls was conducted in a pediatric intensive care unit. The fluid balance in the first 72 h and the presence of acute kidney injury was compared in patients diagnosed with septic shock who died against patients who survived the same condition. Univariate and multivariate analyses were performed.
Results
Forty-five cases and forty-five controls were included in the analysis. Mortality was associated with Pediatric Risk of Mortality (PRISM III) ≥ 26 points (OR 7.5, 95% CI 2.8-18.7; p = 0.000), Pediatric Logistic Organ Dysfunction (PELOD) ≥ 24 points (OR 11.0, 95% CI 4.1-29.4; p = 0.000), creatinine ≥ 0.65 mg/dl (OR 5.6, 95% CI 2.2-13.9; p = 0.000), lactate ≥ 2.5 mmol/l (OR 2.5, 95% CI 1.1-5.9; p = 0.033), SvO2 < 60% (OR 4.6, 95% CI 4.5-4.5; p = 0.001), positive balance > 9% in 72 h (OR 4.3, 95% CI 1.6-11.7; p = 0.003), acute kidney injury (OR 5.7, 95% CI: 2.2-15.1; p = 0.000). In the multivariate model, the values of PRISM ≥26 and PELOD ≥24 points were significant.
Conclusions
In patients who died due to septic shock, the multivariate model showed an association with PRISM ≥26 and PELOD ≥24 and a trend toward association with SvO2 <60% and positive balance of liquids > 9%.
背景:对于脓毒性休克患者,过量的输液可导致发病率和死亡率的增加。本研究的目的是评估脓毒性休克患者的体液平衡、急性肾损伤和死亡率之间的关系。方法在某儿科重症监护病房进行病例和对照研究。将诊断为脓毒性休克的死亡患者与相同情况下存活的患者在最初72小时内的体液平衡和是否存在急性肾损伤进行比较。进行单因素和多因素分析。结果纳入病例45例,对照组45例。死亡率与儿童死亡风险相关(PRISM III)≥26分(OR 7.5, 95% CI 2.8-18.7;p = 0.000),小儿Logistic脏器功能障碍(PELOD)≥24分(OR 11.0, 95% CI 4.1-29.4;p = 0.000),肌酐≥0.65 mg/dl (OR 5.6, 95% CI 2.2-13.9;p = 0.000),乳酸≥2.5 mmol/l (OR 2.5, 95% CI 1.1-5.9;p = 0.033), SvO2 <60%(或4.6,95% ci 4.5-4.5;P = 0.001),正平衡>72小时9% (OR 4.3, 95% CI 1.6-11.7;p = 0.003),急性肾损伤(OR 5.7, 95% CI: 2.2-15.1;p = 0.000)。在多变量模型中,PRISM≥26点和PELOD≥24点的值具有显著性。结论在脓毒性休克死亡的患者中,多因素模型显示PRISM≥26、PELOD≥24相关,SvO2≥60%、液体平衡≥60%相关;9%。
{"title":"Fluid balance and acute kidney injury in septic shock","authors":"Jesús Javier Martínez-García , Nidia Maribel León-Sicairos , Adrián Canizalez-Román , Bianca Azucena García-Arellano","doi":"10.1016/j.bmhime.2017.02.001","DOIUrl":"10.1016/j.bmhime.2017.02.001","url":null,"abstract":"<div><h3>Background</h3><p>In patients with septic shock, excessive fluid administration can lead to increased morbidity and mortality. The aim of this study was to evaluate the association between fluid balance, acute kidney injury and mortality in patients with septic shock.</p></div><div><h3>Methods</h3><p>A study of cases and controls was conducted in a pediatric intensive care unit. The fluid balance in the first 72<!--> <!-->h and the presence of acute kidney injury was compared in patients diagnosed with septic shock who died against patients who survived the same condition. Univariate and multivariate analyses were performed.</p></div><div><h3>Results</h3><p>Forty-five cases and forty-five controls were included in the analysis. Mortality was associated with Pediatric Risk of Mortality (PRISM III) ≥ 26 points (OR 7.5, 95% CI 2.8-18.7; <em>p<!--> <!-->=</em> <!-->0.000), Pediatric Logistic Organ Dysfunction (PELOD) ≥ 24 points (OR 11.0, 95% CI 4.1-29.4; <em>p</em> <!-->=<!--> <!-->0.000), creatinine ≥ 0.65<!--> <!-->mg/dl (OR 5.6, 95% CI 2.2-13.9; <em>p</em> <!-->=<!--> <!-->0.000), lactate ≥ 2.5 mmol/l (OR 2.5, 95% CI 1.1-5.9; <em>p</em> <!-->=<!--> <!-->0.033), SvO2 < 60% (OR 4.6, 95% CI 4.5-4.5; <em>p</em> <!-->=<!--> <!-->0.001), positive balance > 9% in 72<!--> <!-->h (OR 4.3, 95% CI 1.6-11.7; <em>p</em> <!-->=<!--> <!-->0.003), acute kidney injury (OR 5.7, 95% CI: 2.2-15.1; <em>p</em> <!-->=<!--> <!-->0.000). In the multivariate model, the values of PRISM ≥26 and PELOD ≥24 points were significant.</p></div><div><h3>Conclusions</h3><p>In patients who died due to septic shock, the multivariate model showed an association with PRISM ≥26 and PELOD ≥24 and a trend toward association with SvO2 <60% and positive balance of liquids > 9%.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 4","pages":"Pages 282-288"},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.02.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54311206","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-07-01DOI: 10.1016/j.bmhime.2018.01.003
César Iván Ayala-Guzmán, Norma Ramos-Ibáñez, Luis Ortiz-Hernández
Background
An accurate assessment of physical activity in schoolchildren is necessary to implement strategies that promote active lifestyles. The objective of this study was to validate a self-administered questionnaire to assess physical activity and sedentary behaviors and to analyze differences in the validity according to nutritional status in Mexican schoolchildren.
Methods
Schoolchildren of 8-12 years of age answered a self-report physical activity and sedentary behaviors questionnaire to evaluate sedentary and light physical activity (SLPA) and moderate to vigorous physical activity (MVPA). The data of children who wore a triaxial accelerometer days were analyzed. Concordance between both methods to determine the time schoolchildren spend watching television was assessed using intraclass correlation coefficients and Bland-Altman method.
Results
The estimation of MVPA by questionnaires was higher than that of accelerometers by 117.6 minutes per week, and the estimation of SLPA was lower by 1,924.7 minutes per week. No correlation between the time assessed by accelerometers and the time reported in the questionnaires for SLPA and MVPA was detected. In normal-weighted children, a low correlation was observed between the time dedicated to playing video games with sedentary activities (ric=0.29, p=0.031) assessed by accelerometers.
Conclusions
Schoolchildren over-estimate MVPA and under-estimate SLPA. Body weight can be a factor influencing such bias.
背景准确评估学童的身体活动对于实施促进积极生活方式的策略是必要的。本研究的目的是验证一份评估身体活动和久坐行为的自我管理问卷,并根据墨西哥学童的营养状况分析其效度的差异。方法对8 ~ 12岁小学生进行自报体力活动和久坐行为问卷调查,评价其久坐和轻度体力活动(SLPA)和中度至剧烈体力活动(MVPA)。对佩戴三轴加速度计的儿童进行数据分析。采用班级内相关系数和Bland-Altman方法评估两种方法测定小学生看电视时间的一致性。结果问卷对MVPA的估计比加速度计高117.6 min /周,SLPA的估计比加速度计低1924.7 min /周。加速度计评估的时间与SLPA和MVPA问卷报告的时间没有相关性。在体重正常的儿童中,通过加速度计评估,用于玩电子游戏的时间与久坐活动的时间之间的相关性较低(ric=0.29, p=0.031)。结论小学生对MVPA高估,对SLPA低估。体重可能是影响这种偏见的一个因素。
{"title":"Accelerometry does not match with self-reported physical activity and sedentary behaviors in Mexican children","authors":"César Iván Ayala-Guzmán, Norma Ramos-Ibáñez, Luis Ortiz-Hernández","doi":"10.1016/j.bmhime.2018.01.003","DOIUrl":"https://doi.org/10.1016/j.bmhime.2018.01.003","url":null,"abstract":"<div><h3>Background</h3><p>An accurate assessment of physical activity in schoolchildren is necessary to implement strategies that promote active lifestyles. The objective of this study was to validate a self-administered questionnaire to assess physical activity and sedentary behaviors and to analyze differences in the validity according to nutritional status in Mexican schoolchildren.</p></div><div><h3>Methods</h3><p>Schoolchildren of 8-12 years of age answered a self-report physical activity and sedentary behaviors questionnaire to evaluate sedentary and light physical activity (SLPA) and moderate to vigorous physical activity (MVPA). The data of children who wore a triaxial accelerometer days were analyzed. Concordance between both methods to determine the time schoolchildren spend watching television was assessed using intraclass correlation coefficients and Bland-Altman method.</p></div><div><h3>Results</h3><p>The estimation of MVPA by questionnaires was higher than that of accelerometers by 117.6<!--> <!-->minutes per week, and the estimation of SLPA was lower by 1,924.7<!--> <!-->minutes per week. No correlation between the time assessed by accelerometers and the time reported in the questionnaires for SLPA and MVPA was detected. In normal-weighted children, a low correlation was observed between the time dedicated to playing video games with sedentary activities (r<sub>ic</sub>=0.29, <em>p</em>=0.031) assessed by accelerometers.</p></div><div><h3>Conclusions</h3><p>Schoolchildren over-estimate MVPA and under-estimate SLPA. Body weight can be a factor influencing such bias.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 4","pages":"Pages 272-281"},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2018.01.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137280860","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-05-01DOI: 10.1016/j.bmhime.2017.11.028
Yesenia Herrera , Sandra Contreras , Magdalena Hernández , Laura Álvarez , Yolanda Mora , Sergio Encarnación-Guevara
Background
A key process in cell regulation is protein phosphorylation, which is catalyzed by protein kinases and phosphatases. However, phosphoproteomics studies are difficult because of the complexity of protein phosphorylation and the number of phosphorylation sites.
Methods
We describe an efficient approach analyzing phosphopeptides in single, separated protein by two-dimensional gel electrophoresis. In this method, a titanium oxide (TiO2)-packed NuTip is used as a phosphopeptide trap, together with displacers as lactic acid in the loading buffer to increase the efficiency of the interaction between TiO2 and phosphorylated peptides.
Results
The results were obtained from the comparison of mass spectra of proteolytic peptides of proteins with a matrix-assisted laser desorption-ionization-time of flight (MALDI-TOF) instrument.
Conclusions
This method has been applied to identifying phosphoproteins involved in the symbiosis Rhizobium etli-Phaseolus vulgaris.
{"title":"Displacers improve the selectivity of phosphopeptide enrichment by metal oxide affinity chromatography","authors":"Yesenia Herrera , Sandra Contreras , Magdalena Hernández , Laura Álvarez , Yolanda Mora , Sergio Encarnación-Guevara","doi":"10.1016/j.bmhime.2017.11.028","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.11.028","url":null,"abstract":"<div><h3>Background</h3><p>A key process in cell regulation is protein phosphorylation, which is catalyzed by protein kinases and phosphatases. However, phosphoproteomics studies are difficult because of the complexity of protein phosphorylation and the number of phosphorylation sites.</p></div><div><h3>Methods</h3><p>We describe an efficient approach analyzing phosphopeptides in single, separated protein by two-dimensional gel electrophoresis. In this method, a titanium oxide (TiO<sub>2</sub>)-packed NuTip is used as a phosphopeptide trap, together with displacers as lactic acid in the loading buffer to increase the efficiency of the interaction between TiO<sub>2</sub> and phosphorylated peptides.</p></div><div><h3>Results</h3><p>The results were obtained from the comparison of mass spectra of proteolytic peptides of proteins with a matrix-assisted laser desorption-ionization-time of flight (MALDI-TOF) instrument.</p></div><div><h3>Conclusions</h3><p>This method has been applied to identifying phosphoproteins involved in the symbiosis <em>Rhizobium etli-Phaseolus vulgaris</em>.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 200-207"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.11.028","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138322674","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Chemical pesticides, widely used in agriculture and vector-borne disease control, have shown toxic effects on the environment and the people in contact with them. Bacillus thuringiensis is a widely used bacterium for alternative and safer control of insect pests. Its toxins are specific for insects but innocuous for mammals and may be used as powerful adjuvants when applied with vaccines. The objective of this work was to characterize some autochthonous B. thuringiensis strains, which could be used for the control of a local pest (Diatraea considerata Heinrich) that affects sugar cane crops in Sinaloa, Mexico. Also, to evaluate these strains as a source of Cry toxins, which may be used in the future as adjuvants for some vaccines.
Methods
Eight strains from field-collected dead insects were isolated. These were microbiologically identified as B. thuringiensis and confirmed by amplification and sequencing of 16S rDNA. Bioassays were performed to evaluate their pathogenicity against D. considerata, and Cry toxins were identified by proteomic analyses.
Results
An increased mortality among larvae infected with strain Bt-D was observed, and its toxin was identified as Cry1Ac.
Conclusions
The observed data showed that the selected strain was pathogenic to D. considerata and seemed to produce Cry1Ac protein, which has been reported as an adjuvant in different types of immunization.
{"title":"Characterization of Cry toxins from autochthonous Bacillus thuringiensis isolates from Mexico","authors":"Raquel Camacho-Millán , Elsa Maribel Aguilar-Medina , Héctor Quezada , Óscar Medina-Contreras , Genaro Patiño-López , Héctor Manuel Cárdenas-Cota , Rosalío Ramos-Payán","doi":"10.1016/j.bmhime.2017.11.027","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.11.027","url":null,"abstract":"<div><h3>Background</h3><p>Chemical pesticides, widely used in agriculture and vector-borne disease control, have shown toxic effects on the environment and the people in contact with them. <em>Bacillus thuringiensis</em> is a widely used bacterium for alternative and safer control of insect pests. Its toxins are specific for insects but innocuous for mammals and may be used as powerful adjuvants when applied with vaccines. The objective of this work was to characterize some autochthonous <em>B. thuringiensis</em> strains, which could be used for the control of a local pest (<em>Diatraea considerata</em> Heinrich) that affects sugar cane crops in Sinaloa, Mexico. Also, to evaluate these strains as a source of Cry toxins, which may be used in the future as adjuvants for some vaccines.</p></div><div><h3>Methods</h3><p>Eight strains from field-collected dead insects were isolated. These were microbiologically identified as <em>B. thuringiensis</em> and confirmed by amplification and sequencing of 16S rDNA. Bioassays were performed to evaluate their pathogenicity against <em>D. considerata</em>, and Cry toxins were identified by proteomic analyses.</p></div><div><h3>Results</h3><p>An increased mortality among larvae infected with strain Bt-D was observed, and its toxin was identified as Cry1Ac.</p></div><div><h3>Conclusions</h3><p>The observed data showed that the selected strain was pathogenic to <em>D. considerata</em> and seemed to produce Cry1Ac protein, which has been reported as an adjuvant in different types of immunization.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 193-199"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.11.027","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138424791","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-05-01DOI: 10.1016/j.bmhime.2017.11.026
Ana Laura Guzmán-Ortiz , Gerardo Aparicio-Ozores , Ricardo Valle-Rios , Oscar Medina-Contreras , Genaro Patiño-López , Héctor Quezada
Introduction
Relapse occurs in approximately 20% of Mexican patients with childhood acute lymphoblastic leukemia (ALL). In this group, chemoresistance may be one of the biggest challenges. An overview of complex cellular processes like drug tolerance can be achieved with proteomic studies.
Methods
The B-lineage pediatric ALL cell line CCRF-SB was gradually exposed to the chemotherapeutic vincristine until proliferation was observed at 6 nM, control cells were cultured in the absence of vincristine. The proteome from each group was analyzed by nanoHPLC coupled to an ESI-ion trap mass spectrometer. The identified proteins were grouped into overrepresented functional categories with the PANTHER classification system.
Results
We found 135 proteins exclusively expressed in the presence of vincristine. The most represented functional categories were: Toll receptor signaling pathway, Ras Pathway, B and T cell activation, CCKR signaling map, cytokine-mediated signaling pathway, and oxidative phosphorylation.
Conclusions
Our study indicates that signal transduction and mitochondrial ATP production are essential during adaptation of leukemic cells to vincristine, these processes represent potential therapeutic targets.
{"title":"Proteomic changes in a childhood acute lymphoblastic leukemia cell line during the adaptation to vincristine","authors":"Ana Laura Guzmán-Ortiz , Gerardo Aparicio-Ozores , Ricardo Valle-Rios , Oscar Medina-Contreras , Genaro Patiño-López , Héctor Quezada","doi":"10.1016/j.bmhime.2017.11.026","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.11.026","url":null,"abstract":"<div><h3>Introduction</h3><p>Relapse occurs in approximately 20% of Mexican patients with childhood acute lymphoblastic leukemia (ALL). In this group, chemoresistance may be one of the biggest challenges. An overview of complex cellular processes like drug tolerance can be achieved with proteomic studies.</p></div><div><h3>Methods</h3><p>The B-lineage pediatric ALL cell line CCRF-SB was gradually exposed to the chemotherapeutic vincristine until proliferation was observed at 6<!--> <!-->nM, control cells were cultured in the absence of vincristine. The proteome from each group was analyzed by nanoHPLC coupled to an ESI-ion trap mass spectrometer. The identified proteins were grouped into overrepresented functional categories with the PANTHER classification system.</p></div><div><h3>Results</h3><p>We found 135 proteins exclusively expressed in the presence of vincristine. The most represented functional categories were: Toll receptor signaling pathway, Ras Pathway, B and T cell activation, CCKR signaling map, cytokine-mediated signaling pathway, and oxidative phosphorylation.</p></div><div><h3>Conclusions</h3><p>Our study indicates that signal transduction and mitochondrial ATP production are essential during adaptation of leukemic cells to vincristine, these processes represent potential therapeutic targets.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 181-192"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.11.026","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138322673","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-05-01DOI: 10.1016/j.bmhime.2017.11.032
Angélica Torres-Arroyo , Arturo Ruiz-Lara , Adriana Castillo-Villanueva , Sara Teresa Méndez-Cruz , Sara Elvia Espinosa-Padilla , Francisco Javier Espinosa-Rosales , Flora Zarate-Mondragón , Roberto Cervantes-Bustamante , Vanessa Bosch-Canto , Iris Vizzuett-López , Juan Carlos Ordaz-Fávila , Jesús Oria-Hernández , Horacio Reyes-Vivas
Proteomics is the study of the expression of changes and post-translational modifications (PTM) of proteins along a metabolic condition either normal or pathological. In the field of health, proteomics allows obtaining valuable data for treatment, diagnosis or pathophysiological mechanisms of different illnesses. To illustrate the aforementioned, we describe two projects currently being performed at the Instituto Nacional de Pediatría: The immuno-proteomic study of cow milk allergy and the Proteomic study of childhood cataract.
Cow's milk proteins (CMP) are the first antigens to which infants are exposed and generate allergy in some of them. In Mexico, the incidence of CMP allergy has been estimated at 5-7%. Clinical manifestations include both gastrointestinal and extra-gastrointestinal symptoms, making its diagnosis extremely difficult. An inappropriate diagnosis affects the development and growth of children. The goals of the study are to identify the main immune-reactive CMP in Mexican pediatric population and to design more accurate diagnostic tools for this disease.
Childhood cataract is a major ocular disease representing one of the main causes of blindness in infants; in developing countries, this disease promotes up to 27% of cases related to visual loss. From this group, it has been estimated that close to 60% of children do not survive beyond two years after vision lost. PTM have been pointed out as the main cause of protein precipitation at the crystalline and, consequently, clouding of this tissue. The study of childhood cataract represents an outstanding opportunity to identify the PTM associated to the cataract-genesis process.
{"title":"Proteomics: a tool to develop novel diagnostic methods and unravel molecular mechanisms of pediatric diseases","authors":"Angélica Torres-Arroyo , Arturo Ruiz-Lara , Adriana Castillo-Villanueva , Sara Teresa Méndez-Cruz , Sara Elvia Espinosa-Padilla , Francisco Javier Espinosa-Rosales , Flora Zarate-Mondragón , Roberto Cervantes-Bustamante , Vanessa Bosch-Canto , Iris Vizzuett-López , Juan Carlos Ordaz-Fávila , Jesús Oria-Hernández , Horacio Reyes-Vivas","doi":"10.1016/j.bmhime.2017.11.032","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.11.032","url":null,"abstract":"<div><p>Proteomics is the study of the expression of changes and post-translational modifications (PTM) of proteins along a metabolic condition either normal or pathological. In the field of health, proteomics allows obtaining valuable data for treatment, diagnosis or pathophysiological mechanisms of different illnesses. To illustrate the aforementioned, we describe two projects currently being performed at the Instituto Nacional de Pediatría: The immuno-proteomic study of cow milk allergy and the Proteomic study of childhood cataract.</p><p>Cow's milk proteins (CMP) are the first antigens to which infants are exposed and generate allergy in some of them. In Mexico, the incidence of CMP allergy has been estimated at 5-7%. Clinical manifestations include both gastrointestinal and extra-gastrointestinal symptoms, making its diagnosis extremely difficult. An inappropriate diagnosis affects the development and growth of children. The goals of the study are to identify the main immune-reactive CMP in Mexican pediatric population and to design more accurate diagnostic tools for this disease.</p><p>Childhood cataract is a major ocular disease representing one of the main causes of blindness in infants; in developing countries, this disease promotes up to 27% of cases related to visual loss. From this group, it has been estimated that close to 60% of children do not survive beyond two years after vision lost. PTM have been pointed out as the main cause of protein precipitation at the crystalline and, consequently, clouding of this tissue. The study of childhood cataract represents an outstanding opportunity to identify the PTM associated to the cataract-genesis process.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 233-240"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.11.032","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138322720","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-05-01DOI: 10.1016/j.bmhime.2017.11.025
Karina Salvador-Severo , Leopoldo Gómez-Caudillo , Héctor Quezada , José de Jesús García-Trejo , Alan Cárdenas-Conejo , Martha Elisa Vázquez-Memije , Fernando Minauro-Sanmiguel
Background
Mitochondriopathies are multisystem diseases affecting the oxidative phosphorylation (OXPHOS) system. Skin fibroblasts are a good model for the study of these diseases. Fibroblasts with a complex IV mitochondriopathy were used to determine the molecular mechanism and the main affected functions in this disease.
Methods
Skin fibroblast were grown to assure disease phenotype. Mitochondria were isolated from these cells and their proteome extracted for protein identification. Identified proteins were validated with the MitoMiner database.
Results
Disease phenotype was corroborated on skin fibroblasts, which presented a complex IV defect. The mitochondrial proteome of these cells showed that the most affected proteins belonged to the OXPHOS system, mainly to the complexes that form supercomplexes or respirosomes (I, III, IV, and V). Defects in complex IV seemed to be due to assembly issues, which might prevent supercomplexes formation and efficient substrate channeling. It was also found that this mitochondriopathy affects other processes that are related to DNA genetic information flow (replication, transcription, and translation) as well as beta oxidation and tricarboxylic acid cycle.
Conclusions
These data, as a whole, could be used for the better stratification of these diseases, as well as to optimize management and treatment options.
{"title":"Mitochondrial proteomic profile of complex IV deficiency fibroblasts: rearrangement of oxidative phosphorylation complex/supercomplex and other metabolic pathways","authors":"Karina Salvador-Severo , Leopoldo Gómez-Caudillo , Héctor Quezada , José de Jesús García-Trejo , Alan Cárdenas-Conejo , Martha Elisa Vázquez-Memije , Fernando Minauro-Sanmiguel","doi":"10.1016/j.bmhime.2017.11.025","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.11.025","url":null,"abstract":"<div><h3>Background</h3><p>Mitochondriopathies are multisystem diseases affecting the oxidative phosphorylation (OXPHOS) system. Skin fibroblasts are a good model for the study of these diseases. Fibroblasts with a complex IV mitochondriopathy were used to determine the molecular mechanism and the main affected functions in this disease.</p></div><div><h3>Methods</h3><p>Skin fibroblast were grown to assure disease phenotype. Mitochondria were isolated from these cells and their proteome extracted for protein identification. Identified proteins were validated with the MitoMiner database.</p></div><div><h3>Results</h3><p>Disease phenotype was corroborated on skin fibroblasts, which presented a complex IV defect. The mitochondrial proteome of these cells showed that the most affected proteins belonged to the OXPHOS system, mainly to the complexes that form supercomplexes or respirosomes (I, III, IV, and V). Defects in complex IV seemed to be due to assembly issues, which might prevent supercomplexes formation and efficient substrate channeling. It was also found that this mitochondriopathy affects other processes that are related to DNA genetic information flow (replication, transcription, and translation) as well as beta oxidation and tricarboxylic acid cycle.</p></div><div><h3>Conclusions</h3><p>These data, as a whole, could be used for the better stratification of these diseases, as well as to optimize management and treatment options.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 175-180"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.11.025","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138322723","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-05-01DOI: 10.1016/j.bmhime.2017.03.002
Sergio Encarnación-Guevara
This review does not aim to be an up-to-date of proteomics in Mexico; it simply tries to trace its development, exposing the story of the researchers, laboratories and some institutions that have contributed to the establishment and development of this science in Mexico.
{"title":"The dawn and the first twenty-five years of proteomics in Mexico: a personal chronicle","authors":"Sergio Encarnación-Guevara","doi":"10.1016/j.bmhime.2017.03.002","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.03.002","url":null,"abstract":"<div><p>This review does not aim to be an up-to-date of proteomics in Mexico; it simply tries to trace its development, exposing the story of the researchers, laboratories and some institutions that have contributed to the establishment and development of this science in Mexico.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 208-211"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.03.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138399948","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-05-01DOI: 10.1016/j.bmhime.2017.03.001
Genaro Patiño-Lopez , Sergio Encarnación-Guevara
{"title":"Clinical Proteomics in Mexico: where do we stand?","authors":"Genaro Patiño-Lopez , Sergio Encarnación-Guevara","doi":"10.1016/j.bmhime.2017.03.001","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.03.001","url":null,"abstract":"","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 173-174"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.03.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138322676","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-05-01DOI: 10.1016/j.bmhime.2017.11.029
Laura Denise Manzanares-Meza , Claudia Ivonne Gutiérrez-Román , Oscar Medina-Contreras
Mass spectrometry has been the focus of technology development and application for imaging for several decades. Imaging mass spectrometry using matrix-assisted laser desorption ionization is a new and effective tool for molecular studies of complex biological samples such as tissue sections. As histological features remain intact throughout the analysis of a section, distribution maps of multiple analytes can be correlated with histological and clinical features. Spatial molecular arrangements can be assessed without the need for target-specific reagents, allowing the discovery of diagnostic and prognostic markers of different cancer types and enabling the determination of effective therapies.
{"title":"MALDI imaging: beyond classic diagnosis","authors":"Laura Denise Manzanares-Meza , Claudia Ivonne Gutiérrez-Román , Oscar Medina-Contreras","doi":"10.1016/j.bmhime.2017.11.029","DOIUrl":"https://doi.org/10.1016/j.bmhime.2017.11.029","url":null,"abstract":"<div><p>Mass spectrometry has been the focus of technology development and application for imaging for several decades. Imaging mass spectrometry using matrix-assisted laser desorption ionization is a new and effective tool for molecular studies of complex biological samples such as tissue sections. As histological features remain intact throughout the analysis of a section, distribution maps of multiple analytes can be correlated with histological and clinical features. Spatial molecular arrangements can be assessed without the need for target-specific reagents, allowing the discovery of diagnostic and prognostic markers of different cancer types and enabling the determination of effective therapies.</p></div>","PeriodicalId":100195,"journal":{"name":"Boletín Médico Del Hospital Infantil de México (English Edition)","volume":"74 3","pages":"Pages 212-218"},"PeriodicalIF":0.0,"publicationDate":"2017-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bmhime.2017.11.029","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138322675","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}