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1.
BMC Pediatr ; 24(1): 222, 2024 Apr 01.
Artigo em Inglês | MEDLINE | ID: mdl-38561702

RESUMO

BACKGROUND AND OBJECTIVES: To investigate the relationship between body mass index (BMI) and blood biochemical indicators in early adolescence, and to provide ideas for early prevention of diseases and explore possible disease-related predictors. METHODS: 3125 participants aged 10 ∼ 14 years were selected from China from the survey of "China Nutrition and Health Surveillance ( 2016 ∼ 2017 ) ". Employing advanced statistical methods, including generalized linear models, heatmaps, hierarchical clustering, and generalized additive models, the study delved into the associations between BMI and various biochemical indicators. RESULTS: In early adolescence, indicators including systolic pressure, diastolic pressure, weight, height, BMI, hemoglobin, blood uric acid, serum creatinine, albumin, vitamin A presented increasing trends with the increase of age ( P < 0.05 ), whereas LDL-C, vitamin D, and ferritin showed decreasing trends with the increase of age ( P < 0.05 ). The increase in hemoglobin and blood uric acid levels with age was more pronounced in males compared to females ( P < 0.05 ). BMI was positively correlated with blood glucose, hemoglobin, triglyceride, LDL-C, blood uric acid, serum creatinine, ferritin, transferrin receptor, hs-CRP, total protein, vitamin A ( P < 0.05 ). There was a significant BMI × age interaction in the correlation analysis with LDL-C, transferrin receptor, serum creatinine, and hs-CRP ( P < 0.05 ). BMI was a risk factor for hypertension, hypertriglyceridemia, low high density lipoprotein cholesterolemia, and metabolic syndrome in all age groups ( OR > 1, P < 0.05 ). CONCLUSIONS: High BMI was a risk factor for hypertension, hypertriglyceridemia, low high density lipoprotein cholesterolemia, and MetS in early adolescents. With the focus on energy intake beginning in early adolescence, the maintenance of a healthy weight warrants greater attention.


Assuntos
Hipertensão , Hipertrigliceridemia , Masculino , Feminino , Humanos , Adolescente , Índice de Massa Corporal , Proteína C-Reativa/análise , LDL-Colesterol , Ácido Úrico , Creatinina , Vitamina A , Hipertensão/epidemiologia , Lipoproteínas HDL , Hemoglobinas/análise , Ferritinas , Receptores da Transferrina
2.
Nutrients ; 14(23)2022 Dec 05.
Artigo em Inglês | MEDLINE | ID: mdl-36501203

RESUMO

Background: This study aimed to explore the correlation between body mass index (BMI) and dyslipidemia and the optimal cut-off point for BMI to distinguish the risk of dyslipidemia in lactating women. Methods: A total of 2295 lactating women subjects were included in this study, all within 2 years postpartum. All samples were from "China Children and Lactating Mothers Nutritional Health Surveillance (2016−2017)". BMI, blood lipids, demographic information, lifestyle habits, and other serum indicators were obtained in this survey. Generalized linear model, logistic regression, restricted cubic spline (RCS) and ROC curve analysis were used to evaluate the relationship among BMI, blood lipids, and dyslipidemia. Results: BMI in lactating women was positively correlated with total cholesterol (TC), triglyceride (TG), low-density lipoprotein cholesterol (LDL-C), but negatively correlated with high-density lipoproteincholesterol (HDL-C) (p < 0.05). Higher BMI in lactating women was associated with higher ORs of dyslipidemia (hypercholesterolemia, hypertriglyceridemia, high-LDL-cholesterolemia, low HDL-cholesterolemia) (p < 0.05). These associations were stable across age groups, breastfeeding child age (months), parity, physical activity level, fasting plasma glucose (FPG), and hemoglobin. These factors did not interact with this relationship (p > 0.05). The optimal cut-off point for BMI was 24.85 kg/m2 determined by using ROC analysis, which can distinguish the risk of dyslipidemia. Conclusions: BMI was positively correlated with risk of dyslipidemia. Maintaining an ideal weight may prevent dyslipidemia in lactating women, and BMI is recommended to be controlled below 24.85 kg/m2.


Assuntos
Dislipidemias , Lactação , Gravidez , Criança , Feminino , Humanos , Índice de Massa Corporal , HDL-Colesterol , Dislipidemias/epidemiologia , Lipídeos , Triglicerídeos , Fatores de Risco
3.
Chinese Journal of School Health ; (12): 1257-1260, 2021.
Artigo em Chinês | WPRIM (Pacífico Ocidental) | ID: wpr-886678

RESUMO

Objective@#To investigate the prevalence and associated factors of eating out among children and adolescents aged 6-17 in Hebei Province, and to explore the association between eating out and overweight/obesity.@*Methods@#Data came from Children and Nurse Nutrition Health Monitoring of China during 2016-2017. Questionnaire surveys and anthropometric measures was conducted among 3 330 children aged 6-17 in 12 survey sites. Multivariate Logistics stepwise regression model was used to analyze the influencing factors of eating out and the relationship between eating out and overweight/obesity.@*Results@#The proportion of eating out was 16.19%, and the rate of overweight and obesity was 29.43%. Multivariate analysis showed that the older children (junior high school students:OR=1.36; high school students:OR=3.57, both P<0.05) and adolescents from highincome families (10 000~<20 000 CNY:OR=1.48; ≥20 000 CNY:OR=2.93, both P<0.05) were more likely to eat out. Children and adolescents living in rural areas (OR=0.20, P<0.01), nononlychild (OR=0.76, P=0.02), day school students (OR=0.21, P<0.01), and the primary caregivers of the elderly (OR=0.69, P=0.03) were less likely to eat out. In addition, eating out was statistically associated with an increased risk of overweight and obesity (OR=1.31, P<0.01).@*Conclusion@#Eating out is common among children and adolescents aged 6-17 in Hebei Province. Residency, age, household income, onechild family, boarding and and eating out behaviors of primary caregivers are associated with eating out among children and adolescents. Eating out may increase the risk of overweight/obesity in children.

4.
PLoS One ; 9(11): e111737, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-25369323

RESUMO

A monoclonal antibody (McAb) against non-structural protein (NSP) 3B of foot-mouth-disease virus (FMDV) (3B4B1) was generated and shown to recognize a conserved epitope spanning amino acids 24-32 of 3B (GPYAGPMER) by peptide screening ELISA. This epitope was further shown to be a unique and predominant B cell epitope in 3B2, as sera from animals infected with different serotypes of FMDV blocked the ability of McAb 3B4B1 to bind to NSP 2C3AB. Also, a polyclonal antibody against NSP 2C was produced in a rabbit vaccinated with 2C epitope regions expressed in E. coli. Using McAb 3B4B1 and the 2C polyclonal antibody, a solid-phase blocking ELISA (SPB-ELISA) was developed for the detection of antibodies against NSP 2C3AB to distinguish FMDV-infected from vaccinated animals (DIVA test). The parameters for this SPB-ELISA were established by screening panels of sera of different origins. Serum samples with a percent inhibition (PI) greater than or equal to 46% were considered to be from infected animals, and a PI lower than 46% was considered to indicate a non-infected animal. This test showed a similar performance as the commercially available PrioCHECK NS ELISA. This is the first description of the conserved and predominant GPYAGPMER epitope of 3B and also the first report of a DIVA test for FMDV NSP 3B based on a McAb against this epitope.


Assuntos
Ensaio de Imunoadsorção Enzimática/métodos , Vírus da Febre Aftosa/isolamento & purificação , Febre Aftosa/diagnóstico , Proteínas não Estruturais Virais/análise , Sequência de Aminoácidos , Animais , Anticorpos Monoclonais/química , Anticorpos Monoclonais/imunologia , Bovinos , Epitopos/química , Epitopos/imunologia , Febre Aftosa/sangue , Febre Aftosa/imunologia , Vírus da Febre Aftosa/imunologia , Camundongos , Dados de Sequência Molecular , Coelhos , Ovinos , Suínos , Proteínas não Estruturais Virais/química , Proteínas não Estruturais Virais/imunologia
5.
J Virol Methods ; 170(1-2): 128-33, 2010 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-20863858

RESUMO

In recent years, the potential value of the non-structural proteins (NSP) 2C and 3ABC has been well documented for differentiation of animals infected with foot-and-mouth disease virus (FMDV) from vaccinated animals (DIVA). In order to develop a more sensitive approach to detect animals infected naturally in herds of FMDV-vaccinated animals, a 47.6kD fusion protein named 2C3AB was expressed in bacteria which incorporated two major B-cell epitope regions of 2C and the whole 3AB within the NSP of FMDV. The product reacted specifically with sera from animals infected with FMDV, but did not react with sera from non-vaccinated and healthy animals. The performance of 2C3AB was compared further with the 3ABC fusion protein as the antigen in an indirect ELISA format for DIVA. The results showed that the 2C3AB-ELISA had an even stronger signal reaction in the indirect ELISA and showed higher sensitivity than the 3ABC-ELISA for DIVA purposes and for detection of early virus infection in animals. Therefore, it is expected that the recombinant protein 2C3AB could be a good candidate protein with which to develop more sensitive methods for DIVA and for surveillance of herds infected subclinically under conditions of vaccination. This study indicates that the 2C3AB-ELISA can be used to confirm the results of the 3ABC-ELISA to improve the performance of the 3ABC-ELISA DIVA test.


Assuntos
Anticorpos Antivirais/sangue , Proteínas de Transporte/imunologia , Ensaio de Imunoadsorção Enzimática/veterinária , Vírus da Febre Aftosa/imunologia , Febre Aftosa/diagnóstico , Febre Aftosa/imunologia , Proteínas não Estruturais Virais/imunologia , Animais , Especificidade de Anticorpos , Infecções Assintomáticas , Western Blotting , Proteínas de Transporte/genética , Epitopos/genética , Epitopos/imunologia , Vírus da Febre Aftosa/genética , Vírus da Febre Aftosa/isolamento & purificação , Expressão Gênica , Proteínas Recombinantes de Fusão/imunologia , Sensibilidade e Especificidade , Proteínas não Estruturais Virais/genética , Vacinas Virais/imunologia
6.
Vet Res Commun ; 34(5): 445-57, 2010 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-20512625

RESUMO

A monoclonal antibody, 3BIgG, against the prokaryotically expressed foot-and-mouth disease virus (FMDV) non-structural protein (NSP) 3B was obtained. The 3BIgG-sepharose conjugant (3BmAb-6BFF) was prepared by adding the purified 3BIgG into epoxy-activated sepharose 6BFF, incubating with the inactivated FMDV, and then removing the sepharose by centrifugation. The vaccine was made from the supernatant emulsified with oil-adjuvant ISA206. Ten guinea pigs, 26 pigs and six cattle were vaccinated, and a vaccination control group was included without treatment with 3BmAb-6BFF. After 28 days, 9/10 pigs challenged with FMDV were protected, this result was the same as the control group, indicating that the vaccine potency was not reduced after treatment with 3BmAb-6BFF. The other animals were vaccinated weekly for nine weeks, and serum samples were collected to detect 3ABC-antibody titers. The results showed that 3ABC-antibody production was delayed and the positive antibody rates were lower when vaccination was carried out using vaccines treated with 3BmAb-6BFF compared with untreated vaccines. The findings of this study suggest that it is possible to reduce NSPs using a mAb-sepharose conjugant in FMD vaccines without reducing their efficacy.


Assuntos
Vírus da Febre Aftosa/imunologia , Febre Aftosa/prevenção & controle , Vacinas Virais/uso terapêutico , Animais , Anticorpos Monoclonais/imunologia , Anticorpos Antivirais/imunologia , Bovinos/imunologia , Bovinos/virologia , Febre Aftosa/imunologia , Cobaias/imunologia , Cobaias/virologia , Suínos/imunologia , Suínos/virologia , Vacinas de Produtos Inativados/imunologia , Vacinas de Produtos Inativados/uso terapêutico , Proteínas não Estruturais Virais/imunologia , Vacinas Virais/imunologia
7.
Sheng Wu Gong Cheng Xue Bao ; 25(1): 10-5, 2009 Jan.
Artigo em Chinês | MEDLINE | ID: mdl-19441220

RESUMO

In recent years, the potential value of nonstructural protein (NSP) 2C was well documented for distinguishing foot-and-mouth disease virus (FMDV) in infected animals and vaccinated animals. In order to develop a more sensitive approach to detect natural infected FMDV while there is no interact with vaccinated FMDV, we incorporated a major epitope region of 2C with whole 3AB coding region within NSP and expressed in Escherichia coli. We got a 47.6 kD fusion protein named 2C'3AB. The product showed a specific reactivity with FMDV from serum of infected animal by using Western blotting analysis. This suggests that this protein could be applied to distinguish infected FMDV and vaccinated FMDV. We further compared 2C'3AB protein with 3ABC fusion protein, another available protein used for detecting infected FMDV, using indirect ELISA assay. The results showed that 2C'3AB-ELISA had higher sensitivity than that of 3ABC-ELISA for distinguishing infected FMDV and vaccinated FMDV of sera from epidemic region. Therefore, this recombinant protein 2C'3AB is a good candidate protein to develop more sensitive method to differentiate infected FMDV and vaccinated FMDV from vaccinated animals. This finding will increase our capability to check the infectious virus carrier and finally improve FMDV infection control.


Assuntos
Proteínas de Transporte/imunologia , Epitopos/imunologia , Vírus da Febre Aftosa/genética , Proteínas Recombinantes de Fusão/imunologia , Proteínas não Estruturais Virais/imunologia , Animais , Especificidade de Anticorpos , Proteínas de Transporte/genética , Proteínas de Transporte/metabolismo , Escherichia coli/genética , Escherichia coli/metabolismo , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Proteínas não Estruturais Virais/genética , Proteínas não Estruturais Virais/metabolismo
8.
Wei Sheng Wu Xue Bao ; 48(6): 790-5, 2008 Jun.
Artigo em Chinês | MEDLINE | ID: mdl-18724495

RESUMO

OBJECTIVE: To purify and to detect reactivity of non-structural proteins 3A, 3B and 2C expressed in the Escherichia coli. METHODS: FMDV NSP 3A, 3B and 2C containing the major B-cell antigenic sites were expressed in E. coli. We got renatured 2C protein by lysing of isolated inclusion body using high concentration of urea, and then diluted in a buffer system containing oxidized/reduced glutathione. Purified 3A, 3B and 2C were obtained by Ni-NTA His Bind Resin affinity chromatography. The reactivity of three NSPs with sera of different origin was measured using an indirect ELISA and Western-blot. The reactivity of three proteins was compared with 3ABC and 3D by detecting sera of clinically healthy sheep that were collected from epidemic region of Asia I FMD. RESULTS: Proteins 3A and 3B were solubly expressed in bacteria, and 2C was expressed to form inclusion body. All three products could react specifically with sera from FMDV infected animal by western-blot and ELISA. The high coincident rates were observed between 3A, 3B, 2C and 3ABC. CONCLUSION: The results would provide useful materials for establishment of immunoelectro-transfer blot (EITB) diagnostic method, which could be used for differentiation of the FMDV infected animals from the vaccinated animals.


Assuntos
Escherichia coli/genética , Vírus da Febre Aftosa , Proteínas não Estruturais Virais/biossíntese , Proteínas não Estruturais Virais/isolamento & purificação , Animais , Especificidade de Anticorpos , Western Blotting , Ensaio de Imunoadsorção Enzimática , Expressão Gênica , Soros Imunes/análise , Soros Imunes/imunologia , Proteínas Recombinantes de Fusão/biossíntese , Proteínas Recombinantes de Fusão/química , Proteínas Recombinantes de Fusão/imunologia , Proteínas Recombinantes de Fusão/isolamento & purificação , Solubilidade , Proteínas não Estruturais Virais/química , Proteínas não Estruturais Virais/imunologia
9.
Artigo em Inglês | MEDLINE | ID: mdl-18023607

RESUMO

A novel nanocomposite of CdTe-PAMAM-MWNT was synthesized by covalently linking CdTe quantum dots (QDs) onto highly water-soluble multi-wall carbon nanotubes (MWNTs) functionalized with dendritic poly(amidoamine) (PAMAM). The IR, UV-vis and TEM methods has been used for the characterization of the composites. A facile method for controlling the density of QDs in the composite by simply changing the ratio of CdTe QDs/PAMAM-MWNT, as was verified by the TEM images. The experiments revealed that PAMAM and PAMAM-MWNT, once covalently linked with CdTe QDs, had remarkable effect on their fluorescence property. The fluorescence intensity of the CdTe-PAMAM hybrid was substantially enhanced as a compared to that of QDs, and the fluorescence was quenched greatly when QDs reacted with PAMAM-MWNT. The experimentally observed phenomena indicate that electron and energy transfer took place efficiently between CdTe QDs, PAMAM and MWNTs in the novel composite. These nanocomposits might hold great potential in photoelectron device and biotechnology applications.


Assuntos
Compostos de Cádmio/química , Dendrímeros/química , Nanocompostos/química , Nanotubos de Carbono/química , Pontos Quânticos , Telúrio/química , Microscopia de Força Atômica , Microscopia Eletrônica de Transmissão , Estrutura Molecular , Nanocompostos/ultraestrutura , Nanotubos de Carbono/ultraestrutura , Espectrofotometria , Espectroscopia de Infravermelho com Transformada de Fourier
10.
Anal Chim Acta ; 604(2): 170-6, 2007 Dec 05.
Artigo em Inglês | MEDLINE | ID: mdl-17996539

RESUMO

We report the synthesis of a novel looped enzyme-polyamidoamine nanocomposite with high enzyme loading density and long-term retention of bioactivity. The horseradish peroxidase (HRP) is first immobilized on fourth-grade (G4) poly(amidoamine) (PAMAM) dendrimer to form relatively a small enzyme-PAMAM composite, which is allowed to grow up into a larger one. The looped horseradish peroxidase-polyamidoamine (HRP-PAMAM) nanohybrid was characterized by TEM. The material obtained shows promising features as applied to the fabrication of high sensitive and long lifetime biosensors. In the presence of the hydroquinone mediator in the solution, the immobilized HRP exhibited excellent electro-catalytical response to H2O2. Under the optimal conditions, the resulting biosensor showed a linear response to H2O2 over a concentration range from 3.1x10(-6) to 2.0x10(-3) mol L(-1) with a sensitivity of 0.36 A L mol(-1) cm(-2) and a detection limit of 8.0x10(-7) mol L(-1). The sensitivity of the sensor response maintained over 70% of the original over 10 weeks. The catalytic activity of the looped enzyme-PAMAM nanohybrid form of HRP enzyme was obviously stabilized. As an extension, bienzyme sensor modified with glucose oxidase and HRP enzymatic PAMAM nanocomposites was constructed. The sensor exhibited improved performance and can be applied to the detection of glucose in real samples.


Assuntos
Técnicas Biossensoriais , Dendrímeros/química , Enzimas Imobilizadas/química , Peroxidase do Rábano Silvestre/química , Nanoestruturas , Poliaminas/química , Eletroquímica , Microscopia Eletrônica de Transmissão
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