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1.
Nutrients ; 12(8)2020 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-32751521

RESUMO

Despite the emerging evidence of adverse consequences and interaction with doping substances, dietary supplements (DS) are commonly used by many Canadians. The purpose of this study was to evaluate the patterns and determinants of current DS use among non-athlete students at a Canadian university using a cross-sectional approach. Of the 475 participants who completed the online survey, 43.4% declared using DS in the past six months. Participants who were male, aged ≥20 years old, and had a parent/guardian with a bachelor's degree were significantly more likely to use DS. The types of DS used and the sources of information regarding DS were significantly influenced by age and gender. The most commonly used DS were vitamin and mineral and protein supplements. Most participants referred to healthcare professionals for information on DS, but many continued to depend on unreliable sources including family and friends. Of DS users, 10.1% reported experiencing adverse events from using DS. Findings from this study indicate that supplementation is very common among Canadian non-athlete students and highlight the urgent need for the development of educational programs surrounding DS use.


Assuntos
Suplementos Nutricionais/estatística & dados numéricos , Estudantes/estatística & dados numéricos , Adulto , Fatores Etários , Canadá , Estudos Transversais , Feminino , Humanos , Masculino , Fatores Sexuais , Universidades , Adulto Jovem
2.
J Vis Exp ; (33)2009 Nov 04.
Artigo em Inglês | MEDLINE | ID: mdl-19890248

RESUMO

Traditional spectrophotometry requires placing samples into cuvettes or capillaries. This is often impractical due to the limited sample volumes often used for protein analysis. The Thermo Scientific NanoDrop 2000c Spectrophotometer solves this issue with an innovative sample retention system that holds microvolume samples between two measurement surfaces using the surface tension properties of liquids, enabling the quantification of samples in volumes as low as 0.5-2 microL. The elimination of cuvettes or capillaries allows real time changes in path length, which reduces the measurement time while greatly increasing the dynamic range of protein concentrations that can be measured. The need for dilutions is also eliminated, and preparations for sample quantification are relatively easy as the measurement surfaces can be simply wiped with laboratory wipe. This video article presents modifications to traditional protein concentration determination methods for quantification of microvolume amounts of protein using A280 absorbance readings or the BCA colorimetric assay.


Assuntos
Nanotecnologia/instrumentação , Proteínas/análise , Espectrofotometria/instrumentação , Colorimetria/instrumentação , Colorimetria/métodos , Nanotecnologia/métodos , Sensibilidade e Especificidade , Espectrofotometria/métodos
3.
Curr Protoc Protein Sci ; Chapter 3: Unit 3.10, 2009 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-19235138

RESUMO

Methods for determining protein concentration that use progressively smaller amounts of material are continually being developed. A new way of minimizing the amount of sample used for spectroscopic analysis is providing more opportunities for greater quality control. Traditional spectrophotometric and fluorometric methods for determination of protein concentrations have long required placing samples into containment devices such as cuvettes or capillaries. A microsample retention system is changing that paradigm by using natural surface tension properties to capture and hold microvolume samples in place during measurement without traditional containment devices. The advantage of such a system is to dramatically reduce the amount of sample required (1 to 2 microl) while greatly increasing the dynamic range of protein concentrations that can be measured. Modifications to classic protein concentration determination protocols are presented to provide a microvolume alternative to traditional cuvette-based methods.


Assuntos
Fluorometria/métodos , Proteínas/química , Espectrofotometria/métodos , Fluorometria/instrumentação , Tamanho da Amostra , Espectrofotometria/instrumentação
4.
Oncogene ; 22(43): 6704-16, 2003 Oct 02.
Artigo em Inglês | MEDLINE | ID: mdl-14555984

RESUMO

The neuroendocrine (NE) cells represent the third cell population in the normal prostate. Results of several clinical studies strongly indicate that the NE cell population is greatly increased in prostate carcinomas during androgen ablation therapy that correlates with hormone-refractory growth and poor prognosis. However, the mechanism of NE cell enrichment in prostate carcinoma remains an enigma. We investigated the molecular mechanism by which androgen-sensitive C-33 LNCaP human prostate cancer cells become NE-like cells in an androgen-reduced environment, mimicking clinical phenomenon. In the androgen-depleted condition, androgen-sensitive C-33 LNCaP cells gradually acquired the NE-like morphology and expressed an increased level of neuron-specific enolase (NSE), a classical marker of neuronal cells. Several NE-like subclone cells were established. Biochemical characterizations of these subclone cells showed that receptor-type protein-tyrosine phosphatase alpha (RPTPalpha) is elevated and ERK is constitutively activated, several folds higher than that in parental cells. In androgen-depleted condition, PD98059, an MEK inhibitor, could efficiently block not only the activation of ERK, but also the acquisition of the NE-like morphology and the elevation of NSE in C-33 LNCaP cells. In RPTPalpha cDNA-transfected C-33 LNCaP cells, ERK was activated and NSE was elevated. In those cells in the presence of PD98059, the ERK activation and NSE elevation were abolished, following a dose-response fashion. Additionally, in constitutively active MEK mutant cDNA-transfected C-33 LNCaP cells, ERK was activated and NSE level was elevated, and cells obtained the NE-like phenotype. Our data collectively indicated that RPTPalpha signaling via ERK is involved in the NE transdifferentiation of androgen-sensitive C-33 LNCaP human prostate cancer cells in the androgen-depleted condition.


Assuntos
Androgênios/metabolismo , Neoplasias da Próstata/metabolismo , Proteínas Tirosina Fosfatases/metabolismo , Receptores de Superfície Celular , Transdução de Sinais , Western Blotting , Diferenciação Celular , Divisão Celular , DNA Complementar/metabolismo , Eletroforese em Gel de Poliacrilamida , Ativação Enzimática , Inibidores Enzimáticos/farmacologia , Flavonoides/farmacologia , Proteínas de Fluorescência Verde , Humanos , Proteínas Luminescentes/metabolismo , Masculino , Microscopia de Fluorescência , Proteínas Quinases Ativadas por Mitógeno/metabolismo , Modelos Biológicos , Fosfopiruvato Hidratase/biossíntese , Proteínas Tirosina Fosfatases Classe 4 Semelhantes a Receptores , Fatores de Tempo , Transfecção , Células Tumorais Cultivadas
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