RESUMEN
This study explored the expression of interleukin 17D (IL-17D) secreted by human ovariancarcinoma cells and the effect of exogenous IL-17D transfection on MICA, which is the ligand of NKG2D, on the surface of ovary carcinoma cells. Human ovarian papillary serous adenocarcinoma cell line SKOV3, empty vector control cell line SKOV3/vector, exogenous human IL-17D stable-transfected cell line SKOV3/IL-17D, as well as cisplatin (CDDP)-resistant cell SKOV/CDDP were cultured; ovarian adenocarcinoma cell line OVCAR-3, empty vector control cell line OVCAR3/vector and OVCAE3/IL- 17D were observed under a microscope. In the study, methyl-thiazolyl-tetrazolium (MTT) method was used to detect the inhibition rate, resistance index and proliferation of SKOV3 and SKOV3/CDDP. It was found that the expression of IL-17 D in SKOV3/CDDP was much higher than that of its parent cell line SKOV3; IL-17D might be correlated to the drug resistance of cells; the proliferation of SKOV3 transfected with IL-17D was significantly accelerated, indicating IL-17D may be effective in promoting the growth of oncocyte.
Asunto(s)
Adenocarcinoma/patología , Inmunidad Innata/efectos de los fármacos , Interleucina-17/fisiología , Neoplasias Ováricas/patología , Adenocarcinoma Papilar/patología , División Celular , Línea Celular Tumoral , Cisplatino/farmacología , Cistadenocarcinoma Seroso/patología , Resistencia a Antineoplásicos , Ensayos de Selección de Medicamentos Antitumorales , Femenino , Regulación Neoplásica de la Expresión Génica , Antígenos de Histocompatibilidad Clase I/biosíntesis , Antígenos de Histocompatibilidad Clase I/genética , Humanos , Interleucina-17/genética , Proteínas de Neoplasias/biosíntesis , Proteínas de Neoplasias/genética , Proteínas Recombinantes de Fusión/metabolismo , TransfecciónRESUMEN
The high molecular weight glutenin subunits 14 and 15 were purified from cultivars of bread wheat (Triticum aestivum) Xiaoyan 6 by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) appled a new method for visualizing protein in gels. N-terminal amino acid sequences were homologous comparing with other High-Molecular-Weight glutenin subunits. The result suggested that they were basic protein analyzed by two-dimensional electrophoresis of IEF(Isoelectric Focussing) x SDS-PAGE and NEPHGE(Non-Equilibrium PI-gradient Electrophoresis) x SDS-PAGE.
Asunto(s)
Glútenes/análogos & derivados , Glútenes/química , Secuencia de Aminoácidos , Electroforesis en Gel Bidimensional , Glútenes/aislamiento & purificación , Datos de Secuencia Molecular , Peso Molecular , Subunidades de ProteínaRESUMEN
Prawn (Penaeus penicillatus) acid phosphatase (EC 3.1.3.2) catalyzes the nonspecific hydrolysis of phosphate monoesters. The effects of some pollutants in sea water on the enzyme activity results in the loss of the biological function of the enzyme, which leads to disruption of phosphate metabolism in cells. This paper analyzes the effects of methanol on the activity and conformation of prawn acid phosphatase. The results show that low concentrations of methanol can lead to reversible inactivation. Inhibition of the enzyme by methanol is classified as non-competitive inhibition, and the inhibition constant (Ki) is 8.5%. Conformational changes of the enzyme molecule in methanol solutions of different concentrations were measured using fluorescence emission, differential UV-absorption, and circular dichroism spectra. Increased methanol concentrations caused the fluorescence emission intensity of the enzyme to increase. The ultraviolet difference spectra of the enzyme denatured with methanol had two negative peaks, at 222 and 270 nm, and a positive peak at 236 nm. The changes in the fluorescence and ultraviolet difference spectra reflected the changes of the microenvironments of tryptophan and tyrosine residues of the enzyme. The CD spectrum changes of the enzyme show that the secondary structure of the enzyme also changed some. These results suggest that methanol is a non-competitive inhibitor and the conformational integrity of the enzyme is essential for its activity.
