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Caspase-3-like Death Protease is Inhibited by Interleukin-7
Hong, Soon-Duck,Lee, Sang-Han,Tsuruo, Takashi,Lee, Dong-Sun Korean Society of Life Science 1999 Journal of Life Science Vol.9 No.1
Highly metastatic mouse T-lymphoma CS21 cells can grow in vitro when cocultured with CA12 lymph node stromal cells, but they undergo apoptotic cell death when separated from CA12 stromal cells. It has been found that cysteine and interleukin-7(IL-7) as antiapoptotic soluble factors that produced by CA12 stromal cells. In this study, we report that an ICE family protease is activated in CS21 cells when separated from CA12 stromal cells and cultured alone. Enzyme purification using an avidin affinity column revealed that the involved cysteine protease possessed caspase3-like death protease activity. In addition, when IL-7 was added to CS21 cell culture, the protease activity could not be detected during partial purification of the enzyme. Taken together, these results strongly suggest that the caspase3-like protease activation is suppressed by IL-7 as an antiapoptotic factor that leads to abrogation of apoptosis execution.
Sung, Jong-Hyuk,Yu, Kyung-Ha,Park, Jin-Sun,Tsuruo, Takashi,Kim, Dae-Duk,Shim, Chang-Koo,Chung, Suk-Jae American Society for Pharmacology and Experimental 2005 Drug metabolism and disposition: the biological fa Vol.33 No.3
<P>The kinetics and mechanism by which tacrine is distributed in the rat brain were examined. Tacrine levels in plasma and striatal extracellular fluid were used to evaluate the pharmacokinetics of this process. The K(D,brain) was decreased with the dose for tacrine, indicating that the distribution to the brain is saturable. The uptake of organic cations such as choline, 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), and carnitine was inhibited by the addition of tacrine to cultures of mouse immortalized brain capillary endothelial cells. In addition, the apical to basal transport and basal to apical transport of tacrine were inhibited by the addition of organic cations to cultures of LLC-PK1 cells, suggesting that tacrine transport across the blood-brain barrier (BBB) is mediated by organic cation transport system(s). Consistent with the in vitro results, a standard reverse transcription-polymerase chain reaction procedure was able to amplify the message of mOCT2 and mOCTN2, but not mOCT1, in MBEC4 (mouse brain microvessel endothelial cell line 4) cells. Similarly, mRNAs for rOCT2 and rOCTN2 were present in representative rat brain samples. To determine whether OCT2 and/or OCTN2 transport tacrine, these transporters were cloned and then transfected in SK-HEP1 and HEK 293 cells. The uptake of choline, MPP, and TEA was inhibited by the presence of tacrine in rOCT2-expressing SK-HEP1 cells, whereas the uptake of carnitine was inhibited by the presence of tacrine in rOCTN2-expressing HEK 293 cells. Collectively, these observations suggest that the transport of tacrine across the BBB is mediated, at least in part, by multiple organic cation transport systems in rats.</P>
Gold nanoparticles supported on mesoporous iron oxide for enhanced CO oxidation reaction
Tanaka, Shunsuke,Lin, Jianjian,Kaneti, Yusuf Valentino,Yusa, Shin-ichi,Jikihara, Yohei,Nakayama, Tsuruo,Zakaria, Mohamed Barakat,Alshehri, Abdulmohsen Ali,You, Jungmok,Hossain, Md. Shahriar A.,Yamauch The Royal Society of Chemistry 2018 Nanoscale Vol.10 No.10
<P>Herein, we report the synthesis of gold (Au)-loaded mesoporous iron oxide (Fe2O3) as a catalyst for both CO and NH3 oxidation. The mesoporous Fe2O3 is firstly prepared using polymeric micelles made of an asymmetric triblock copolymer poly(styrene-<I>b</I>-acrylic acid-<I>b</I>-ethylene glycol) (PS-<I>b</I>-PAA-<I>b</I>-PEG). Owing to its unique porous structure and large surface area (87.0 m<SUP>2</SUP> g<SUP>−1</SUP>), the as-prepared mesoporous Fe2O3 can be loaded with a considerably higher amount of Au nanoparticles (Au NPs) (7.9 wt%) compared to the commercial Fe2O3 powder (0.8 wt%). Following the Au loading, the mesoporous Fe2O3 structure is still well-retained and Au NPs with varying sizes of 3-10 nm are dispersed throughout the mesoporous support. When evaluated for CO oxidation, the Au-loaded mesoporous Fe2O3 catalyst shows up to 20% higher CO conversion efficiency compared to the commercial Au/Fe2O3 catalyst, especially at lower temperatures (25-150 °C), suggesting the promising potential of this catalyst for low-temperature CO oxidation. Furthermore, the Au-loaded mesoporous Fe2O3 catalyst also displays a higher catalytic activity for NH3 oxidation with a respectable conversion efficiency of 37.4% compared to the commercial Au/Fe2O3 catalyst (15.6%) at 200 °C. The significant enhancement in the catalytic performance of the Au-loaded mesoporous Fe2O3 catalyst for both CO and NH3 oxidation may be attributed to the improved dispersion of the Au NPs and enhanced diffusivity of the reactant molecules due to the presence of mesopores and a higher oxygen activation rate contributed by the increased number of active sites, respectively.</P>
Evidence of carrier‐mediated transport in the penetration of donepezil into the rat brain
Kim, Mi‐,Hwa,Maeng, Han‐,Joo,Yu, Kyung‐,Ha,Lee, Kyeong‐,Ryoon,Tsuruo, Takashi,Kim, Dae‐,Duk,Shim, Chang‐,Koo,Chung, Suk‐,Jae Wiley Subscription Services, Inc., A Wiley Company 2010 Journal of Pharmaceutical Sciences Vol.99 No.3
<P><B>Abstract</B></P><P>The objective of this study was to characterize the mechanism that controls the transport of donepezil into the brain. The apparent brain uptake clearance (CL<SUB>app,br</SUB>) was decreased as a function of the dose of donepezil, suggesting an involvement of a saturable transport process via transporter(s) in the penetration across the blood–brain barrier (BBB). Consistent with <I>in vivo</I> results, the uptake of substrates for organic cation transporters was significantly reduced by donepezil in both MBEC4 cells (i.e., a model for BBB) and HEK 293 cells expressing the transporters found in the brain, indicative of the involvement of organic cation transporters in the transport of the drug. Furthermore, donepezil transport was enhanced (<I>p</I> < 0.01) in HEK 293 cells expressing rOCNT1, rOCTN2, or rCHT1. The CL<SUB>app,br</SUB> was reduced up to 52.8% of the control in rats that had been pretreated with choline, while the CL<SUB>app,br</SUB> was unaffected with pretreatments with organic cations other than choline, suggesting that choline and donepezil share a common transport mechanism in the penetration across the BBB <I>in vivo</I>. Taken together, these observations suggest that the transport of donepezil across the BBB is mediated by organic cation transporters such as choline transport system(s). © 2009 Wiley‐Liss, Inc. and the American Pharmacists Association J Pharm Sci 99: 1548–1566, 2010</P>