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      • Zinc-enriched(ZEN) terminals in mouse olfactory bulb

        Jo, Seung Mook,Won, Moo Ho,Cole, Toby B.,Jensen, Morten Skovgaard,Palmiter, Richard D.,Danscher, Gorm 한림대학교 환경·생명과학연구소 2000 일송 의학ㆍ생명과학 심포지엄 Vol.- No.2

        The present study was designed to localize zinc-enriched (ZEN) terminals in mouse olfactory bulb by means of ZnT3 immunocytochemistry (ICC) and zinc autometallography (AMG). The immunocytochemical staining of ZnT3 was closely correlated with the AMG pattern. ZEN terminals were defined as terminals showing both ZnT3 immunoreactivities and AMG granules. At the light microscopic level, dense staining patterns for ZnT3 immunoreactivity were seen in the granule cell layer and the olfactory glomerular layer. At the ultrastructural level, ZEN terminals were restricted to presynaptic terminals with single or multiple postsynaptic thickenings. The postsynaptic profiles contacting ZEN terminals appeared to be dendrites or somata of granule cells in the granule cell layer and periglomerular cells and mitral/tufted (M/T) cells in the olfactory glomerular layer. This suggests with granule cels and periglomerular cells, and(2) olfactory receptor terminals contacting dendritic profiles of M/T cells or periglomerular cells. The close correlation between ZEN terminals and the glutamatergic system is discussed.

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        Glyceollin Transport, Metabolism, and Effects on P-Glycoprotein Function in Caco-2 Cells

        Chukwuemezie Chimezie,Adina C. Ewing,Syeda S. Quadri,Richard B. Cole,Stephen M. Boue,Christopher F. Omari,Melyssa Bratton,Elena Glotser,Elena Skripnikova,Ian Townley,Robert E. Stratford 한국식품영양과학회 2014 Journal of medicinal food Vol.17 No.4

        Glyceollins are phytoalexins produced in soybeans from their isoflavone precursor daidzein. Their impressive anticancer and glucose normalization effects in rodents have generated interest in their therapeutic potential. The aim of the present studies was to begin to understand glyceollin intestinal transport and metabolism, and their potential effects on P-glycoprotein (Pgp) in Caco-2 cells. At 10 and 25 lM, glyceollin permeability was 2.4 – 0.16 · 10- 4 cm/sec and 2.1 – 0.15 · 10- 4 cm/sec, respectively, in the absorptive direction. Basolateral to apical permeability at 25 lM was 1.6 – 0.10 · 10- 4 cm/sec. Results suggest high absorption potential of glyceollin by a passive-diffusion-dominated mechanism. A sulfate conjugate at the phenolic hydroxyl position was observed following exposure to Caco-2 cells. In contrast to verapamil inhibition of the net secretory permeability of rhodamine 123 (R123) and its enhancement of calcein AM uptake into Caco-2 cells, neither glyceollin nor genistein inhibited Pgp (MDR1; ABCB1) up to 300 lM. There was no significant change in MDR1 mRNA expression, Pgp protein expression, or R123 transport in cells exposed to glyceollin or genistein for 24 h up to 100 lM. Collectively, these results suggest that glyceollin has the potential to be well absorbed, but that, similar to the isoflavone genistein, its absorption may be reduced substantially by intestinal metabolism; further, they indicate that glyceollin does not appear to alter Pgp function in Caco-2 cells.

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