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1.
Chinese Journal of Industrial Hygiene and Occupational Diseases ; (12): 2-7, 2023.
Artículo en Chino | WPRIM | ID: wpr-970702

RESUMEN

Objective: To investigate the effect of nuclear factor erythroid 2-related factor 2 (Nrf2) in the alteration of tight junction protein expression in choroid plexus epithelial cells created by lanthanum-activated matrix metalloproteinase 9 (MMP9) . Methods: In October 2020, immortalized rat choroid plexus epithelial cell line (Z310) cells were used as the blood-cerebrospinal fluid barrier in vitro, and were divided into control group and 0.125, 0.25, 0.5 mmol/L lanthanum chloride (LaCl(3)) treatment group. After treating Z310 cells with different concentrations of LaCl(3) for 24 hours, the morphological changes of Z310 cells were observed under inverted microscope, the protein expression levels of MMP9, occludin and zonula occludens-1 (ZO-1) were observed by cellular immunofluorescence method, and the protein expression levels of MMP9, tissue inhibitors of metalloproteinase1 (TIMP1) , occludin, ZO-1 and Nrf2 were detected by Western blotting. The level of reactive oxygen species (ROS) in cells was detected by flow cytometry. Results: Compared with the control group, Z310 cells in the LaCl(3) treatment group were smaller in size, with fewer intercellular junctions, and more dead cells and cell fragments. The expression level of MMP9 protein in cells treated with 0.25 and 0.5 mmol/L LaCl(3) was significantly higher than that in the control group (P<0.05) , and the expression level of TIMP1 and tight junction proteins occudin and ZO-1 was significantly lower than that in the control group (P<0.05) . Compared with the control group, the ROS production level in the 0.25, 0.5 mmol/L LaCl(3) treatment group was significantly increased (P<0.05) , and the Nrf2 protein expression level in the 0.125, 0.25, 0.5 mmol/L LaCl(3) treatment group was significantly decreased (P<0.05) . Conclusion: Lanthanum may increase the level of ROS in cells by down regulating the expression of Nrf2, thus activating MMP9 to reduce the expression level of intercellular tight junction proteins occludin and ZO-1.


Asunto(s)
Ratas , Animales , Metaloproteinasa 9 de la Matriz/metabolismo , Factor 2 Relacionado con NF-E2/metabolismo , Proteínas de Uniones Estrechas/metabolismo , Ocludina/farmacología , Plexo Coroideo/metabolismo , Especies Reactivas de Oxígeno/metabolismo , Lantano/farmacología , Células Epiteliales , Proteína de la Zonula Occludens-1/metabolismo , Fosfoproteínas/farmacología
2.
Indian J Exp Biol ; 2006 Oct; 44(10): 783-90
Artículo en Inglés | IMSEAR | ID: sea-63452

RESUMEN

Lactoferrin (Lf), an iron-binding multifunctional glycoprotein, abundantly present in colostrum and milk of different species such as humans, bovines, and mice has been shown that bovine colostral Lf is transported into the CSF via plasma in newborn calves. Specific Lf-receptors (Lf-R) are present in different cells of different species. In the present study, we report for the first time, the presence and distribution of Lf-R in the intestine and choroid plexus in newborn calves. Brush-border membrane vesicles (BBMV) were prepared from the mucosa of duodenum, jejunum, ileum, colon, epithelium overlying Peyer's patches (EOPP) in jejunum (EOPPJ) and ileum (EOPPI), and choroid plexus membranes. Receptor binding assays were carried out using 125I labeled bovine Lf. Specific and saturable Lf-R were found in BBMV of all the intestinal segments and choroid plexus examined. Nonlinear regression and Scatchard plot analyses clearly revealed that EOPP had the highest binding maximal (Bmax), and lowest in colon. The maximum dissociation constant (Kd) 0.7 microM was in colon while, Bmax and Kd in choroid plexus membrane were 16.87 nmol/mg protein and 0.34 microM, respectively. All these findings together strongly suggested that Lf was transported into CSF via plasma through receptor mediated transcytosis.


Asunto(s)
Animales , Animales Recién Nacidos , Bovinos , Plexo Coroideo/metabolismo , Sistema Digestivo/metabolismo , Microvellosidades/metabolismo , Unión Proteica , Receptores de Superficie Celular/metabolismo
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