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• W1986246872 abstract "One of the early features of diabetic retinopathy is the breakdown of the blood-retinal barrier (BRB) due to disruption of the tight junctions. Whereas impairment of the proteins involved in the disruption of the tight junctions of the internal BRB has been extensively studied, there is no information on the direct effect of high glucose concentration on the barrier function of the outer blood-retinal barrier (formed by the retinal pigment epithelium [RPE]). The aim of this study was to explore the effect of high glucose concentration on the expression of tight junction proteins (occludin, zonula occludens-1 [ZO-1] and claudin-1) in a human RPE line under two distinct glucose concentrations. An RPE cell line (ARPE-19) were cultured for 3 weeks in a medium supplemented with 10% fetal calf serum containing 5.5 mmol D-glucose (mimicking physiological conditions) or 25 mmol Dglucose (mimicking the hyperglycemia that occurs in diabetic patients). Occludin, ZO-1 and claudin-1 were studied by real-time polymerase chain reaction and Western blot at 14 and 21 days. Occludin and ZO-1 mRNA levels and protein content were similar in cultures maintained at 5.5 mmol and 25 mmol of D-glucose. In contrast, high glucose concentration (25 mmol) induced a clear upregulation in claudin-1 mRNA expression and protein content at 21 days (mRNA level: 1.03 vs 2.29; protein content: 0.92 vs 1.14). High glucose concentration leads to differential expression of tight junction proteins in ARPE-19 cells. In addition, our results suggest that the upregulation of claudin-1by glucose is involved in the increase of tight junction sealing function. The functional consequences and clinical applicability of these findings require further investigation. Una de las primeras consecuencias de la retinopatía diabética es la rotura de la barrera hematorretiniana (BHR) causada por la interrupción de las tight junctions. Mientras que la alteración de las proteínas implicadas en la interrupción de las tight junctions de la BHR interna ha sido estudiada extensamente, la información sobre este proceso en la barrera hematorretiniana externa (constituida por el epitelio pigmentario de la retina) es escasa. El objetivo de este trabajo es estudiar el cambio de expresión (ARNm y proteína) de ocludina, zonula occludens-1 y claudina-1 en células de epitelio pigmentario de retina (EPR) humanas con dos concentraciones diferentes de glucosa. Se utilizó una línea de células de EPR humano (ARPE-19), cultivada durante 3 semanas en un medio suplementado con un 10% de suero bovino fetal y con una concentración de 5,5 mmol de D-glucosa (simulando condiciones fisiológicas) o 25 mmol de D-glucosa (simulando la hiperglucemia que ocurre en pacientes diabéticos). Las proteínas de las tight junctions ocludina, zonula occludens-1 y claudina-1 se estudiaron por Western blot y PCR real time. Todas las determinaciones se hicieron a los 14 y 21 días. La expresión de ARNm y proteína de ocludina y ZO-1 fue similar en cultivos mantenidos a 5,5 y 25 mmol de Dglucosa. Por el contrario, en condiciones de hiperglucemia (25 mmol) se produjo un claro aumento en la expresión de ARNm de la claudina-1 y en el contenido de esta proteína a los 21 días (concentraciones de ARNm, 1,03 frente a 2,29; proteína, 0,92 frente a 1,14). La elevada concentración de glucosa produce una expresión diferencial de las proteínas de las tight junctions en células del epitelio pigmentario de la retina humana. Además, nuestros resultados sugieren que la hiperexpresión de la claudina-1 mediada por glucosa participaría en la función de sellado de las tight junctions. Las consecuencias funcionales y la traducción clínica de estos hallazgos serán motivo de futures investigaciones." @default.
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• W1986246872 date "2009-02-01" @default.
• W1986246872 modified "2023-10-17" @default.
• W1986246872 title "High glucose concentration leads to differential expression of tight junction proteins in human retinal pigment epithelial cells" @default.
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• W1986246872 doi "https://doi.org/10.1016/s1575-0922(09)70552-2" @default.
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