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1.
Int J Radiat Biol ; 96(1): 35-46, 2020 01.
Artigo em Inglês | MEDLINE | ID: mdl-30394814

RESUMO

Purpose: There is a need to rapidly triage individuals for absorbed radiation dose following a significant nuclear event. Since most exposed individuals will not have physical dosimeters, we are developing a method to assess exposure dose based on the analysis of a specific panel of blood proteins that can be easily obtained from a fingerstick blood sample.Materials and methods: In three large non-human primate (NHP) studies, animals were exposed to single acute total body doses of x-ray or gamma radiation. A total of 895 blood samples were obtained at baseline and for 7 days after exposure, to evaluate the temporal progression of markers in each of 10 animals (5M/5F) in six dose groups receiving 0-10 Gy. We used tandem mass spectrometry and immunoassay techniques to identify radiation-responsive proteins in blood plasma samples.Results: A blood protein biomarker panel was developed based on analysis of blood plasma samples obtained from several irradiation studies in NHPs that aimed to simulate acute radiation injury in humans from a nuclear exposure event. Panels of several subsets of proteins were shown to accurately classify plasma samples into two exposure groups either above or below a critical dose threshold with sensitivities and specificities exceeding 90%.Conclusion: This study lays the groundwork for developing a radiation biodosimetry triage tool. Our results in NHPs must be compared with those in human patients undergoing radiotherapy to determine if the biomarker panel proteins exhibit a similar radiation response and allow adequate classification power in humans.


Assuntos
Proteínas Sanguíneas/análise , Sistemas Automatizados de Assistência Junto ao Leito , Radiometria/métodos , Animais , Biomarcadores/análise , Testes Hematológicos , Imunoensaio , Macaca mulatta , Fatores de Tempo
2.
Int J Radiat Biol ; 96(1): 22-34, 2020 01.
Artigo em Inglês | MEDLINE | ID: mdl-30605362

RESUMO

Purpose: In a significant nuclear event, hundreds of thousands of individuals will require rapid triage for absorbed radiation to ensure effective medical treatment and efficient use of medical resources. We are developing a rapid screening method to assess whether an individual received an absorbed dose of ≥2 Gy based on the analysis of a specific panel of blood proteins in a fingerstick blood sample.Materials and methods: We studied a data set of 1051 human blood samples obtained from radiotherapy patients, normal healthy individuals, and several special population groups. We compared the findings in humans with those from irradiation studies in non-human primates (NHPs).Results: We identified a panel of three protein biomarkers, salivary alpha amylase (AMY1), Flt3 ligand (FLT3L), and monocyte chemotactic protein 1 (MCP1), which are upregulated in human patients receiving fractionated doses of total body irradiation (TBI) therapy as a treatment for cancer. These proteins exhibited a similar radiation response in NHPs after single acute or fractionated doses of ionizing radiation.Conclusion: Our work provides confidence in this biomarker panel for biodosimetry triage using fingerstick blood samples and in the use of NHPs as a model for irradiated humans.


Assuntos
Proteínas Sanguíneas/análise , Radiometria/métodos , Triagem/métodos , Adolescente , Adulto , Idoso , Animais , Biomarcadores/sangue , Criança , Feminino , Humanos , Imunoensaio , Macaca mulatta , Masculino , Pessoa de Meia-Idade , Adulto Jovem
3.
Zoo Biol ; 38(6): 508-515, 2019 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-31541494

RESUMO

The study of wildlife health greatly contributes to understanding population dynamics and detecting conservation threats. The determination of the different fractions of plasma proteins (proteinogram) is an important laboratory tool to study wildlife health. The aim of this study was to characterize protein electrophoresis in wild Andean condors (Vultur gryphus) from north-western Patagonia and to evaluate differences according to age and sex classes. Once reference values of wild, apparently healthy individuals, were established, we compared these values to those of individuals received at the Buenos Aires Zoo in Argentina for rehabilitation due to various health problems. Reference proteinograms from wild Andean condors differed only in the α 1 and ß 2-fractions between sex categories. Males showed higher concentrations of these protein fractions than females. We found clear differences between wild birds and rehabilitating individuals. Total proteins, globulins, α 1-globulins, total α-globulins, ß 2-globulins, total ß-globulins, and γ-globulins were significantly higher in rehabilitating than in wild individuals, whereas albumin, α 2, and ß1-globulins were similar between these groups. The albumin/globulin ratio, as a general indicator of health, was significantly lower in rehabilitating than in wild individuals. The results indicate the effects on different protein fractions of pathologic processes occurring in individuals undergoing rehabilitation. Our results provide useful insights, contributing to improving diagnoses and prognoses in this species. This information may also be useful to assess the health status of Andean condors in studies of wild populations and for comparisons with other bird species.


Assuntos
Bem-Estar do Animal , Doenças das Aves/sangue , Proteínas Sanguíneas/análise , Eletroforese/veterinária , Falconiformes/sangue , Animais , Animais Selvagens , Falconiformes/fisiologia , Feminino , Masculino , Valores de Referência
4.
Chem Commun (Camb) ; 55(76): 11458-11461, 2019 Sep 19.
Artigo em Inglês | MEDLINE | ID: mdl-31535684

RESUMO

We report a polymer-based sensor that rapidly detects cancer based on changes in serum protein levels. Using three ratiometric fluorescence outputs, this simple system identifies early stage and metastatic lung cancer with a high level of accuracy exceeding many biomarker-based assays, making it an attractive strategy for point-of-care testing.


Assuntos
Biomarcadores Tumorais/sangue , Proteínas Sanguíneas/análise , Corantes Fluorescentes/química , Neoplasias Pulmonares/diagnóstico por imagem , Polímeros/química , Animais , Fluorescência , Humanos , Neoplasias Pulmonares/sangue , Neoplasias Pulmonares/secundário , Camundongos , Camundongos Transgênicos , Estrutura Molecular , Neoplasias Experimentais/sangue , Neoplasias Experimentais/diagnóstico por imagem , Neoplasias Experimentais/secundário , Testes Imediatos
5.
Vet J ; 251: 105348, 2019 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-31492388

RESUMO

This study examined the long-term effects of failure of passive transfer of immunity (FPT; diagnosed at 1-8 days of age) on subsequent milk production, growth, reproduction, and lactation performance in dairy heifers from 12 to 36 months of age. A total of 34 farms from the Waikato and Canterbury regions of New Zealand were enrolled in 2015. Each farm was visited on three occasions during the seasonal calving period (early, middle, and late). Blood samples were collected at each visit from 20 replacement heifer calves aged between 1 and 7 days to test for FPT. These heifers (n=1879) were monitored from birth until the end of their first lactation. From 12 months of age onwards, animals were weighed at 15 and 22 months, pregnancy tested 100 days following their first mating, and milk was sampled between 3-4 times during their first lactation to determine milk volume and milk component yields. Farmers recorded any mortality events. FPT had no effect on the odds of mortality from 12 to 22 months (P=0.57) and 12 to 34 months of age (P=0.44). There was no difference in bodyweight at 15 months (P=0.17) and 22 months of age (P=0.95), no significant difference in the odds of being diagnosed pregnant (OR 1.44; 95% CI 0.82-2.69), and no effect on milk solids (fat plus protein) yields (P=0.67). No associations were observed between serum total protein (STP) concentration and milk solids yields (P=0.22) and any other milk parameters. The data from this study indicate that FPT did not adversely affect productivity, performance, or mortality beyond 12 months of age in heifers reared in pasture-based systems.


Assuntos
Peso Corporal , Bovinos/crescimento & desenvolvimento , Imunidade Materno-Adquirida , Lactação , Animais , Animais Recém-Nascidos/imunologia , Proteínas Sanguíneas/análise , Bovinos/imunologia , Indústria de Laticínios , Feminino , Leite , Mortalidade , Nova Zelândia , Gravidez
6.
Adv Clin Chem ; 92: 141-199, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31472753

RESUMO

In the clinical setting, a blood sample is typically the starting point for biomarker search and discovery. Mass spectrometry (MS) is a highly sensitive and informative method for characterizing a very wide range of metabolites and proteins and is therefore a potentially powerful tool for biomarker discovery. However, the physicochemical characteristics of blood coupled with very large ranges of protein and metabolite concentrations present a significant technical obstacle for resolving and quantifying putative biomarkers by MS. Blood fractionation procedures are being developed to reduce the proteome/metabolome complexity and concentration ranges, allowing a greater diversity of analytes, including those at very low concentrations, to be quantified. In this chapter, several strategies for enriching and/or isolating specific blood components are summarized, including methods for the analysis of low and high molecular weight compounds, usually neglected in this type of assays, extracellular vesicles, and peripheral blood mononuclear cells (PBMCs). For each method, relevant practical information is presented for effective implementation.


Assuntos
Biomarcadores/sangue , Proteínas Sanguíneas/análise , Biomarcadores/análise , Humanos
7.
Anal Bioanal Chem ; 411(25): 6697-6709, 2019 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-31401670

RESUMO

The adulteration of meat products by the undeclared addition of commercially available blood plasma powder is quite conceivable due to low costs, high protein contents (about 70%), and advantageous functional properties. This applies particularly to pork, which has the highest meat production rate in the European Union. Evidence of this type of food fraud has been rather difficult to identify due to the lack of appropriate analytical methods, especially when adding plasma to meat of the same animal species. Consequently, a rapid UHPLC-MS/MS method for the detection of porcine blood plasma in emulsion-type pork sausages was developed. After protein extraction and tryptic digestion in a quick and simple one-pot process, species-specific marker peptides for porcine blood cell proteins (four markers) and plasma proteins (12 markers) were measured by UHPLC-MS/MS. Emulsion-type pork sausages were produced from a variety of raw materials that differed in the age or sex of the slaughtered pigs. Sausages were spiked with 0.5, 1, 1.5, 2, 3, or 5% meat substitution by one of two plasma powders, or produced as corresponding blank samples, and subjected to different thermal treatments as full or semi-preserves. Four plasma peptides were identified for the overall sample that allowed detection down to 0.7% meat substitution from the sum of their peak areas, with 5% error probability for both false positives and negatives.


Assuntos
Proteínas Sanguíneas/análise , Contaminação de Alimentos/análise , Produtos da Carne/análise , Carne Vermelha/análise , Animais , Cromatografia Líquida de Alta Pressão/economia , Cromatografia Líquida de Alta Pressão/métodos , Emulsões/química , Feminino , Análise de Alimentos/economia , Análise de Alimentos/métodos , Masculino , Peptídeos/análise , Plasma/química , Suínos , Espectrometria de Massas em Tandem/economia , Espectrometria de Massas em Tandem/métodos , Fatores de Tempo
8.
Nat Commun ; 10(1): 3605, 2019 08 09.
Artigo em Inglês | MEDLINE | ID: mdl-31399600

RESUMO

Microalbuminuria is an important clinical marker of several cardiovascular, metabolic, and other diseases such as diabetes, hypertension, atherosclerosis, and cancer. The accurate detection of microalbuminuria relies on albumin quantification in the urine, usually via an immunoturbidity assay; however, like many antibody-based assessments, this method may not be robust enough to function in global health applications, point-of-care assays, or wearable devices. Here, we develop an antibody-free approach using synthetic molecular recognition by constructing a polymer to mimic fatty acid binding to the albumin, informed by the albumin crystal structure. A single-walled carbon nanotube, encapsulated by the polymer, as the transduction element produces a hypsochromic (blue) shift in photoluminescence upon the binding of albumin in clinical urine samples. This complex, incorporated into an acrylic material, results in a nanosensor paint that enables the detection of microalbuminuria in patient samples and comprises a rapid point-of-care sensor robust enough to be deployed in resource-limited settings.


Assuntos
Albuminas/química , Albuminúria/diagnóstico , Técnicas Biossensoriais/métodos , Albuminas/isolamento & purificação , Albuminúria/urina , Biomarcadores/sangue , Biomarcadores/urina , Proteínas Sanguíneas/análise , Ácidos Graxos , Humanos , Imobilização , Nanoestruturas/química , Pintura , Espectrometria de Fluorescência , Urina/química
9.
Vet Parasitol ; 272: 40-43, 2019 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-31395203

RESUMO

In this study we evaluated the efficacy of trichlorfon against Haemonchus contortus, monitoring its influence on blood parameters and plasma enzymes of lambs with haemonchosis. A lamb group was orally treated with trichlorfon at 100 mg kg-1 while the other group was untreated. Split-plot design analysis was performed with the lamb groups defined as plots while the subplots were the four periods (weeks) of collection. The trichlorfon treatment promoted a significant and effective reduction of fecal egg counts after one week, with efficacies > 99%. After 21 days of treatment, detected blood parameters and serum levels of plasma enzymes were normal. Additionally, serum albumin and urea concentrations increased to normal values, which were not observed in untreated lambs. The treatment with this organophosphate, using a correct oral administration, may represent an effective therapeutic alternative for sheep infected with multi resistant strain of H. contortus.


Assuntos
Hemoncose/veterinária , Doenças dos Ovinos/tratamento farmacológico , Triclorfon/uso terapêutico , Animais , Anti-Helmínticos/uso terapêutico , Proteínas Sanguíneas/análise , Enzimas/sangue , Hemoncose/sangue , Haemonchus , Contagem de Ovos de Parasitas/veterinária , Ovinos , Doenças dos Ovinos/sangue
10.
Blood ; 134(12): 911-923, 2019 09 19.
Artigo em Inglês | MEDLINE | ID: mdl-31366617

RESUMO

There is increasing recognition that platelets have a functional role in the pathophysiology of sepsis, though this role has not been precisely defined. Whether sepsis alters the human platelet transcriptome and translational landscape has never been established. We used parallel techniques of RNA sequencing and ribosome footprint profiling to interrogate the platelet transcriptome and translatome in septic patients and healthy donors. We identified 1806 significantly differentially expressed (false discovery rate <0.05) transcripts in platelets from septic patients. Platelet translational events during sepsis were also upregulated. To explore the relevance of a murine model of sepsis, cecal ligation and puncture (CLP), we compared sepsis-induced changes in platelet gene expression between septic patients and mice subjected to CLP. Platelet transcriptional (ρ = 0.42, P = 3.2 × 10-285) and translational (ρ = 0.65, P = 1.09 × 10-56) changes were significantly correlated between septic patients and mice. We focused on ITGA2B, tracking and validating the expression, regulation, and functional impact of changes in ITGA2B during sepsis. Increased ITGA2B was identified in bone marrow megakaryocytes within 24 hours of sepsis onset. Subsequent increases in ITGA2B were seen in circulating platelets, suggesting dynamic trafficking of the messenger RNA. Transcriptional changes in ITGA2B were accompanied by de novo protein synthesis of αIIb and integrin αIIbß3 activation. Increased αIIb was associated with mortality in humans and mice. These findings provide previously unrecognized evidence that human and murine sepsis similarly alters the platelet transcriptional and translational landscape. Moreover, ITGA2B is upregulated and functional in sepsis due to trafficking from megakaryocytes and de novo synthesis in platelets and is associated with increased mortality.


Assuntos
Plaquetas/metabolismo , Sepse/genética , Sepse/metabolismo , Animais , Plaquetas/patologia , Proteínas Sanguíneas/análise , Proteínas Sanguíneas/genética , Proteínas Sanguíneas/metabolismo , Estudos de Casos e Controles , Feminino , Perfilação da Expressão Gênica , Humanos , Masculino , Camundongos , Biossíntese de Proteínas , Proteoma/análise , Proteômica , Sepse/sangue , Sepse/patologia , Índice de Gravidade de Doença , Transcrição Genética , Transcriptoma
11.
Anal Chim Acta ; 1079: 230-236, 2019 Nov 04.
Artigo em Inglês | MEDLINE | ID: mdl-31387716

RESUMO

The use of immobilized pH gradient (IPG) capillary isoelectric focusing (CIEF) was confirmed to be possible with packed capillaries. The success of this experiment was due to two key factors: first, the use of surface-confined atom transfer radical polymerization method led to an increase in active reaction sites on the surface of silica particles; second, the subsequent free radical reaction caused carrier ampholytes (CAs) to bond faster and firmer. Based on this scheme, both CIEF with free pH gradient and CIEF with IPG were performed in capillaries packed with 3 µm modified silica particles. In our online CIEF-UV platform, both reversible and irreversible adsorption of proteins was shown to be negligible. Four proteins were focused: cytochrome c (pI 10.2), myoglobin (pI 7.3), carbonic anhydrase (pI 5.9) and trypsin inhibitor (pI 4.5). The comparison of the two CIEF columns showed that the time required for focusing in the packed capillary with IPG is only increased by a factor of 1.5 compared to the packed capillary, giving complete focusing in less than 12 min at 400 V/cm. With the increment of the electric field (the maximum at 600 V/cm), the run time was continually decreasing in these packed capillaries while the peak shape was improving. The four proteins (pH 4.5-10.2) could be successfully separated in our online CIEF platform. Moreover, for the newly online CIEF platform, pressure-driven mobilization without an applied electric field was achieved in the packed capillary with immobilized pH gradient.


Assuntos
Eletroforese Capilar/instrumentação , Focalização Isoelétrica/instrumentação , Dióxido de Silício/química , Proteínas Sanguíneas/análise , Eletroforese Capilar/métodos , Humanos , Concentração de Íons de Hidrogênio , Focalização Isoelétrica/métodos
12.
J Dairy Sci ; 102(10): 8670-8690, 2019 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-31351726

RESUMO

Our goal was to determine the effect of systematically controlled variation in milk fat, true protein, casein, and serum protein concentrations on the sensory color, flavor and texture properties, instrumental color and viscosity, and milk fat globule size distribution of milk-based beverages. Beverage formulations were based on a complete balanced 3-factor (fat, true protein, and casein as a percentage of true protein) design with 3 fat levels (0.2, 1.0, and 2.0%), 4 true protein (TP) levels (3.00, 3.67, 4.34, and 5.00%) within each fat level, and 5 casein as a percentage of true protein (CN%TP) levels (5, 25, 50, 75, and 80%) within each protein level (for a total of 60 formulations within each of 2 replicates). Instrumental measures of Hunter L and a values and Commission Internationale de l'Éclairage (CIE) b* values, instrumental viscosity, particle size, flavor, sensory texture and sensory appearance evaluations were done on each pasteurized/homogenized beverage formulation. Within each of the 3 fat levels, higher serum protein concentration drove higher aroma intensity, sweet aromatic, cooked/sulfur, cardboard/doughy flavors, and sensory yellowness scores, whereas higher casein concentration drove higher instrumental viscosity in milk protein beverages. Increasing serum protein concentration increased yellowness, sweet aromatic, aroma intensity, cooked/sulfur, and cardboard/doughy flavors across all fat levels and also had the largest effect on L, a, and b* values, sensory whiteness, and opacity within each fat level. Increases in true protein increased throat cling and astringency intensities. Increases in fat concentration were correlated with higher L, a, and b* values, larger particle size, and increased sensory whiteness, mouth coating, cooked/milky, and milkfat flavors. Multiple linear regression of L, a, and b* values produced better predictions of sensory whiteness and yellowness of pasteurized milk protein beverages than simple linear regression of L or b* values, respectively. Formulating milk protein beverages to a higher true protein level increased astringency regardless of fat level. When formulating milk protein beverages, a product developer has a wide range of milk-based protein ingredient choices that differ in price and change price relationship across time. Understanding the expected relative effect of different milk protein ingredients on the textural and flavor characteristics of milk-based beverages could be used to help guide product reformulation decisions and ingredient choices to achieve a specific sensory profile while controlling total beverage ingredient cost.


Assuntos
Bebidas , Proteínas Sanguíneas/análise , Proteínas do Leite/análise , Leite , Paladar , Adulto , Animais , Bebidas/análise , Caseínas , Bovinos , Cor , Feminino , Glicolipídeos/análise , Glicoproteínas/análise , Humanos , Masculino , Pessoa de Meia-Idade , Leite/química , Tamanho da Partícula , Pasteurização , Viscosidade
13.
Analyst ; 144(16): 4865-4870, 2019 Aug 05.
Artigo em Inglês | MEDLINE | ID: mdl-31297492

RESUMO

Proteins play a key role in disease diagnosis, and protein discrimination is an important but difficult issue. Here, we report a novel strategy for improving protein discrimination through a facile colorimetric sensor array, which is based on DNA-gold nanoparticle (AuNP) conjugates manipulated by exonuclease I (Exo I). Different proteins exhibit diverse affinities toward the three DNAs, and the DNA-protein binding is resistant to the digestion of Exo I and protects the AuNPs from aggregation in high concentrations of NaCl media, forming distinct response patterns of the array. These response patterns as "fingerprints" can be acquired on the sensor array and then identified by linear discriminant analysis (LDA). The sensor array achieved the correct discrimination of 15 proteins at a 10 nM level in buffer solution and real serum samples. Also, the sensor array had the capability to discriminate individual proteins and the mixtures of them. Remarkably, the practicability of the sensor array was further confirmed by the identification of 35 unknown protein samples with 100% accuracy.


Assuntos
Proteínas Sanguíneas/análise , DNA/química , Exodesoxirribonucleases/química , Nanopartículas Metálicas/química , Animais , Proteínas Sanguíneas/química , Bovinos , Colorimetria/métodos , Análise Discriminante , Ouro/química , Humanos , Ácidos Nucleicos Imobilizados/química , Limite de Detecção , Oligodesoxirribonucleotídeos/química
14.
Biomed Chromatogr ; 33(11): e4647, 2019 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-31299101

RESUMO

The cytopoxic effect of RL2 lactaptin (the recombinant analog of proteolytic fragment of human kappa-casein) toward tumor cells in vitro and in vivo presents it as a novel promising antitumor drug. The binding of any drug with serum proteins can affect their activity, distribution, rate of excretion and toxicity in the human body. Here, we studied the ability of RL2 to bind to various blood serum proteins. Using magnetic microparticles bearing by RL2 as an affinity matrix, in combination with mass spectrometry and western blot analysis, we found a number of blood serum proteins possessing affinity for RL2. Among them IgA, IgM and IgG subclasses of immunoglobulins, apolipoprotein A1 and various cortactin isoforms were identified. This data suggests that in the bloodstream RL2 lactaptin takes part in complicate protein-protein interactions, which can affect its activity.


Assuntos
Antineoplásicos/metabolismo , Proteínas Sanguíneas/isolamento & purificação , Proteínas Sanguíneas/metabolismo , Caseínas/metabolismo , Imãs/química , Proteínas Sanguíneas/análise , Cromatografia de Afinidade/métodos , Humanos , Microesferas , Ácidos Polimetacrílicos/química , Proteínas Recombinantes/metabolismo , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
15.
Molecules ; 24(14)2019 Jul 19.
Artigo em Inglês | MEDLINE | ID: mdl-31330945

RESUMO

We have developed a methodology to capture acidic proteins, alkaline proteins, and glycoproteins separately in mouse serum using a combination of three functionalized temperature-responsive chromatographic stationary phases. The temperature-responsive polymer poly(N-isopropylacrylamide) was attached to the stationary phase, silica. The three temperature-responsive chromatographic stationary phase materials were prepared by reversible addition-fragmentation chain transfer polymerization. Alkaline, acidic, and boric acid functional groups were introduced to capture acidic proteins, alkaline proteins, and glycoproteins, respectively. The protein enrichment and release properties of the materials were examined using the acidic protein, bovine serum albumin; the alkaline protein, protamine; and the glycoprotein, horseradish peroxidase. Finally, the three materials were used to analyze mouse serum. Without switching the mobile phase, the capture and separation of mouse serum was achieved by the combination of three temperature-responsive chromatographic stationary phase materials. On the whole, 313 proteins were identified successfully. The number of different proteins identified using the new method was 1.46 times greater than the number of proteins that has been identified without applying this method. To our knowledge, this method is the first combinatorial use of three functionalized temperature-responsive chromatographic stationary phase silica materials to separate proteins in mouse serum.


Assuntos
Proteínas Sanguíneas/análise , Cromatografia , Temperatura Ambiente , Animais , Cromatografia/métodos , Cromatografia Líquida de Alta Pressão , Camundongos , Proteoma , Proteômica/métodos , Espectroscopia de Infravermelho com Transformada de Fourier , Termogravimetria
16.
Lipids Health Dis ; 18(1): 155, 2019 Jul 17.
Artigo em Inglês | MEDLINE | ID: mdl-31315681

RESUMO

OBJECTIVE: This study was to analyse the prevalence of type 2 diabetes mellitus (T2DM) in premenopausal and postmenopausal women. METHODS: A total of 3227 women met the requirements from June to December in 2014, including 207 cases of premenopausal women and 3020 cases of postmenopausal women. The prevalence of T2DM and the associated risk factors in the two groups were analysed. RESULTS: The prevalence of premenopausal women with T2DM was 12.1%, while the prevalence in postmenopausal women was 19.4% (P < 0.05). Total serum protein (TP) (OR = 1.164 95% CI = 1.023-1.324) (P = 0.021) is a major risk factor for premenopausal women with T2DM. The prevalence of T2DM increased with the increase in TP. In postmenopausal groups, the prevalence of T2DM was associated with age (OR = 1.037 95% CI = 1.024-1.051) (P < 0.001), BMI (OR = 1.076 95% CI = 1.044-1.109) (P < 0.001), blood pressure (OR = 1.521 95% CI = 1.234-1.875) (P < 0.001), triglycerides (TG) (OR = 1.106 95% CI = 1.027-1.190) (P = 0.008), blood urea nitrogen (BUN) (OR = 1.065 95% CI = 1.004-1.129) (P = 0.036), alanine aminotransferase (ALT) (OR = 1.009 95% CI = 1.003-1.016) (P = 0.004) and TP (OR = 1.031 95% CI = 1.005-1.057) (P = 0.018). CONCLUSIONS: Postmenopausal women have a higher rate of type 2 diabetes than premenopausal women. TP is a major risk factor for premenopausal women with T2DM. TP, ALT, and BUN are postmenopausal risk factors in addition to traditional risk factors such as obesity, lipidaemia and blood pressure. We should monitor risk factors and take early prevention and intervention measures to reduce the prevalence of diabetes and improve the quality of life of postmenopausal women. TRIAL REGISTRATION: ChiCTR, ChiCTR-TRC-14005029. Registered 29 July 2014, http://www.chictr.org.cn/showproj.aspx?proj=4545.


Assuntos
Proteínas Sanguíneas/análise , Diabetes Mellitus Tipo 2/sangue , Diabetes Mellitus Tipo 2/epidemiologia , Adulto , Idoso , Alanina Transaminase/sangue , Nitrogênio da Ureia Sanguínea , China/epidemiologia , Feminino , Humanos , Hipertensão/epidemiologia , Modelos Logísticos , Pessoa de Meia-Idade , Pós-Menopausa , Pré-Menopausa , Prevalência , Fatores de Risco , Triglicerídeos/sangue
17.
Nat Commun ; 10(1): 3160, 2019 07 18.
Artigo em Inglês | MEDLINE | ID: mdl-31320639

RESUMO

Although plasma proteins may serve as markers of neurological disease risk, the molecular mechanisms responsible for inter-individual variation in plasma protein levels are poorly understood. Therefore, we conduct genome- and epigenome-wide association studies on the levels of 92 neurological proteins to identify genetic and epigenetic loci associated with their plasma concentrations (n = 750 healthy older adults). We identify 41 independent genome-wide significant (P < 5.4 × 10-10) loci for 33 proteins and 26 epigenome-wide significant (P < 3.9 × 10-10) sites associated with the levels of 9 proteins. Using this information, we identify biological pathways in which putative neurological biomarkers are implicated (neurological, immunological and extracellular matrix metabolic pathways). We also observe causal relationships (by Mendelian randomisation analysis) between changes in gene expression (DRAXIN, MDGA1 and KYNU), or DNA methylation profiles (MATN3, MDGA1 and NEP), and altered plasma protein levels. Together, this may help inform causal relationships between biomarkers and neurological diseases.


Assuntos
Biomarcadores/sangue , Proteínas Sanguíneas/análise , Proteínas Sanguíneas/genética , Doenças do Sistema Nervoso/sangue , Doenças do Sistema Nervoso/genética , Idoso , Ilhas de CpG/genética , Metilação de DNA/genética , Epigênese Genética/genética , Feminino , Genoma Humano/genética , Estudo de Associação Genômica Ampla , Humanos , Masculino , Locos de Características Quantitativas/genética , Escócia
18.
J Dairy Res ; 86(3): 291-295, 2019 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-31292012

RESUMO

Serum protein distribution and concentration can be affected by different physiological and pathological conditions. The aim of this study was to evaluate the changes in the concentration of serum protein fractions and haptoglobin in clinically healthy dairy buffaloes during late pregnancy and early lactation. Blood and milk samples were collected from 30 buffaloes at around 7 d before expected calving (blood only) and 7, 30 and 50 d after calving. In serum samples, the total protein, haptoglobin, albumin, α1-, α2-, ß1-, ß2-, γ-globulins, and albumin/globulin ratio (A/G) values were evaluated. In milk, fat%, protein%, lactose%, somatic cell score (SCS) were assessed, along with milk yield (MY) and daily milk production (DMP). The peripartum period significantly influenced (P < 0.005) total protein, albumin, haptoglobin, α2-, ß2- and γ-globulins (P < 0.005). Milk yield, DMP and fat% changed significantly throughout the monitoring period (P < 0.005). Milk yield and DMP were positively correlated with total protein, albumin, ß2-globulins and A/G ratio, and negatively correlated with haptoglobin and α2-globulins. These results provide new knowledge about the serum protein electrophoretic pattern in Italian Mediterranean Buffaloes during the last phase of pregnancy and early stages of lactation.


Assuntos
Proteínas Sanguíneas/análise , Búfalos/sangue , Haptoglobinas/análise , Lactação/sangue , Parto/sangue , Animais , Búfalos/fisiologia , Feminino , Itália , Leite/química , Período Periparto/sangue , Gravidez , Albumina Sérica/análise , Soroglobulinas/análise
19.
Talanta ; 204: 613-625, 2019 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-31357343

RESUMO

A modified CUPRAC (cupric reducing antioxidant capacity) method was developed for the simultaneous estimation of protein oxidation and counteracting antioxidant defense, and the results were compared with those of a modified 2,4-dinitrophenylhydrazine (DNPH) carbonyl assay. The alkaline carbonyl method was cleared off interferences by solvent extraction using a cationic surfactant. Both solution and Nafion membrane sensor CUPRAC methods were used to measure the oxidative hazard in protein solutions. Bovine serum albumin, fetal bovine serum and egg white were used as protein probes, exposed to oxidation by Fe(II)-induced Fenton reaction in the absence and presence of selected antioxidants (ascorbic acid, cysteine, gallic acid, glutathione, and N-acetyl cysteine). Protein probes were initially unreactive toward the CUPRAC and DNPH reagents, but produced colored products upon Fenton oxidation which were bleached by antioxidants, enabling an indirect measurement of antioxidant activity (AOA) by difference. Spearman's rank test for antioxidants demonstrated that there was a strong correlation (+0.7 to +0.9) between the modified CUPRAC and carbonyl assays. There was also a strong correlation between the results of the solution phase and optical sensing CUPRAC methods (R2 > 0.95). As opposed to conventional antioxidant assays not using biologically relevant probes, this work utilizes protein probes for AOA assessment.


Assuntos
Proteínas Sanguíneas/análise , Proteínas do Ovo/análise , Carbonilação Proteica , Soroalbumina Bovina/análise , Animais , Antioxidantes/química , Proteínas Sanguíneas/química , Bovinos , Citrus sinensis , Colorimetria/métodos , Cobre/química , Proteínas do Ovo/química , Sucos de Frutas e Vegetais , Hidrazinas/química , Fenantrolinas/química , Aves Domésticas , Soroalbumina Bovina/química
20.
BMC Cancer ; 19(1): 741, 2019 Jul 29.
Artigo em Inglês | MEDLINE | ID: mdl-31357969

RESUMO

BACKGROUND: The overall prognosis of non-small cell lung cancer (NSCLC) is poor, and currently only patients with localized disease are potentially curable. Therefore, preferably non-invasively determined biomarkers that detect NSCLC patients at early stages of the disease are of high clinical relevance. The aim of this study was to identify and validate novel protein markers in plasma using the highly sensitive DNA-assisted multiplex proximity extension assay (PEA) to discriminate NSCLC from other lung diseases. METHODS: Plasma samples were collected from a total of 343 patients who underwent surgical resection for different lung diseases, including 144 patients with lung adenocarcinoma (LAC), 68 patients with non-malignant lung disease, 83 patients with lung metastasis of colorectal cancers and 48 patients with typical carcinoid. One microliter of plasma was analyzed using PEA, allowing detection and quantification of 92 established cancer related proteins. The concentrations of the plasma proteins were compared between disease groups. RESULTS: The comparison between LAC and benign samples revealed significantly different plasma levels for four proteins; CXCL17, CEACAM5, VEGFR2 and ERBB3 (adjusted p-value < 0.05). A multi-parameter classifier was developed to discriminate between samples from LAC patients and from patients with non-malignant lung conditions. With a bootstrap aggregated decision tree algorithm (TreeBagger), a sensitivity of 93% and specificity of 64% was achieved to detect LAC in this risk population. CONCLUSIONS: By applying the highly sensitive PEA, reliable protein profiles could be determined in microliter amounts of plasma. We further identified proteins that demonstrated different plasma concentration in defined disease groups and developed a signature that holds potential to be included in a screening assay for early lung cancer detection.


Assuntos
Adenocarcinoma de Pulmão/sangue , Proteínas Sanguíneas/análise , Carcinoma Pulmonar de Células não Pequenas/sangue , Detecção Precoce de Câncer/métodos , Neoplasias Pulmonares/sangue , Programas de Rastreamento/métodos , Idoso , Antígeno Carcinoembrionário/sangue , Quimiocinas CXC/sangue , Estudos de Coortes , Confiabilidade dos Dados , Feminino , Proteínas Ligadas por GPI/sangue , Humanos , Imunoensaio/métodos , Masculino , Modelos Biológicos , Curva ROC , Receptor ErbB-3/sangue , Sensibilidade e Especificidade , Estatísticas não Paramétricas , Receptor 2 de Fatores de Crescimento do Endotélio Vascular/sangue
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