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Rifampin enhances cytochrome P450 (CYP) 2B6-mediated efavirenz 8-hydroxylation in healthy volunteers
Cho, D.Y.,Shen, J.H.Q.,Lemler, S.M.,Skaar, T.C.,Li, L.,Blievernicht, J.,Zanger, U.M.,Kim, K.B.,Shin, J.G.,Flockhart, D.A.,Desta, Z. 日本藥物動態學會 2016 DRUG METABOLISM AND PHARMACOKINETICS Vol.31 No.2
The effect of rifampin on the in vivo metabolism of the antiretroviral drug efavirenz was evaluated in healthy volunteers. In a cross-over placebo control trial, healthy subjects (n = 20) were administered a single 600 mg oral dose of efavirenz after pretreatment with placebo or rifampin (600 mg/day for 10 days). Plasma and urine concentrations of efavirenz, 8-hydroxyefavirenz and 8,14-dihydroxyefavirenz were measured by LC-MS/MS. Compared to placebo treatment, rifampin increased the oral clearance (by ~2.5-fold) and decreased maximum plasma concentration (C<SUB>max</SUB>) and area under the plasma concentration-time curve (AUC<SUB>0-~</SUB>) of efavirenz (by ~1.6- and ~2.5-fold respectively) (p < 0.001). Rifampin treatment substantially increased the C<SUB>max</SUB> and AUC<SUB>0-12h</SUB> of 8-hydroxyefavirenz and 8,14-dihydroxyefavirenz, metabolic ratio (AUC<SUB>0-72h</SUB> of metabolites to AUC<SUB>0-72h</SUB> efavirenz) and the amount of metabolites excreted in urine (Ae<SUB>0-12hr</SUB>) (all, p < 0.01). Female subjects had longer elimination half-life (1.6-2.2-fold) and larger weight-adjusted distribution volume (1.6-1.9-fold) of efavirenz than male subjects (p < 0.05) in placebo and rifampin treated groups respectively. In conclusion, rifampin enhances CYP2B6-mediated efavirenz 8-hydroxylation in vivo. The metabolism of a single oral dose of efavirenz may be a suitable in vivo marker of CYP2B6 activity to evaluate induction drug interactions involving this enzyme.
Belliveau, H.F.,Yu, Y.Y.,Luo, Y.,Qin, F.X.,Wang, H.,Shen, H.X.,Sun, J.F.,Yu, S.C.,Srikanth, H.,Phan, M.H. Elsevier 2017 JOURNAL OF ALLOYS AND COMPOUNDS Vol.692 No.-
<P><B>Abstract</B></P> <P>We report on the structural, mechanical, and magnetocaloric properties of annealed melt-extracted Gd<SUB>53</SUB>Al<SUB>24</SUB>Co<SUB>20</SUB>Zr<SUB>3</SUB> amorphous microwires of ∼70 μm diameter. During heat treatment small islands of nanocrystallities are generated and isolated in the amorphous region for the wires. The size of the nanocrystallities ranges from 5 nm to 10 nm. The observed lattice distortion from the nanocrystallities causes changes in the magnetic properties of the wires. The annealing temperature of 100 °C has the largest strength (1845 MPa) as compared to wires annealed at other temperatures. This is likely to trigger nanophase transformation in the amorphous region and these nanocrystals have been preserved through the increase of annealing temperature. The formulation of the nanocrystalline islands is also verified by the selected-area electron diffraction (SAED). The microwires exhibit a large and reversible magnetocaloric effect (MCE), with the maximum isothermal magnetic entropy change (−Δ<I>S</I> <SUB>M</SUB>) and refrigerant capacity (<I>RC</I>) values of 9.5 J/kg K and 689 J/kg respectively for the microwire annealed at 100 °C. This <I>RC</I> is about 35%, 67%, and 91% larger than those of bulk Gd<SUB>53</SUB>Al<SUB>24</SUB>Co<SUB>20</SUB>Zr<SUB>3</SUB> (∼509 J/kg), Gd (∼410 J/kg), and Gd<SUB>5</SUB>Si<SUB>2</SUB>Ge<SUB>1.9</SUB>Fe<SUB>0.1</SUB> (∼360 J/kg) regardless of their ordering temperatures. These results demonstrate the ability to tune the mechanical and magnetic properties of the microwires by thermal annealing.</P> <P><B>Highlights</B></P> <P> <UL> <LI> The impact of nanocrystallization in Gd<SUB>53</SUB>Al<SUB>24</SUB>Co<SUB>20</SUB>Zr<SUB>3</SUB> microwires. </LI> <LI> Enhanced mechanical strength. </LI> <LI> Enhanced magnetocaloric response. </LI> </UL> </P>
Fabrication of p-Type Nitrogen-Doped MgZnO by Depressing N-Related Donors
B. Yao,Z. P. Wei,Y. F. Li,D. Z. Shen,Y. M. Lu,Z. Z. Zhang,B. H. Li,C. J. Zheng,X. H. Wang,J. Y. Zhang,D. X. Zhao,X. W. Fan,Z. K. Tang 한국물리학회 2008 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.53 No.5
Wurtzite nitrogen-doped MgZnO (MgZnO:N) films were grown on c-plane sapphire by using plasma-assisted molecular beam epitaxy with radical NO as the oxygen source and nitrogen dopant. P-type conduction of MgZnO:N was obtained by decreasing the donor defects ((N2)O, VO, etc.) through annealing, revealing a hole concentration of 6.1 × 1017 cm−3 and a mobility of 6.42 cm2/Vs. Furthermore, as-grown p-type films with a hole concentration of 1 × 1017 cm−3 and a mobility of 3 cm2/Vs were obtained by decreasing the (N2)O double donor defect through control of the plasma conditions. ZnMgO:N/ZnO p-n junctions were obtained by using these p-type films. ode-like, rectifying I-V characteristics with a threshold voltage of about 5 V and a different reverse leakage current were observed at room temperature.
Novel anti-apoptotic mechanism of A20 through targeting ASK1 to suppress TNF-induced JNK activation
Won, M,Park, K A,Byun, H S,Sohn, K-C,Kim, Y-R,Jeon, J,Hong, J H,Park, J,Seok, J H,Kim, J M,Yoon, W-H,Jang, I-S,Shen, H M,Liu, Z G,Hur, G M Macmillan Publishers Limited 2010 CELL DEATH AND DIFFERENTIATION Vol.17 No.12
The zinc-finger protein A20 has crucial physiological functions as a dual inhibitor of nuclear factor-κB (NF-κB) activation and apoptosis in tumor necrosis factor (TNF) receptor 1 signaling pathway. Although the molecular basis for the anti-NF-κB function of A20 has been well elucidated, the anti-apoptotic function of A20 is largely unknown. Here, we report a novel mechanism underlying the anti-apoptotic function of A20: A20 blocks TNF-induced apoptosis through suppression of c-jun N-terminal kinase (JNK) by targeting apoptosis signal-regulating kinase1 (ASK1). First, the ectopic expression of A20 drastically inhibits TNF-induced JNK activation and apoptosis in multiple cell types including those deficient of NF-κB activation. Unexpectedly, the blunting effect of A20 on TNF-induced JNK activation is not mediated by affecting the TNFR1 signaling complex formation. Instead, A20 interacts with ASK1, an important MAPKK kinase in the JNK signaling cascade. More importantly, overexpression of wild-type A20, but not of mutant A20 (ZnF4; C624A, C627A), promotes degradation of the ASK1 through the ubiquitin-proteasome system. Taken together, the results from this study reveal a novel anti-apoptotic mechanism of A20 in TNF signaling pathway: A20 binds to ASK1 and mediates ASK1 degradation, leading to suppression of JNK activation and eventually blockage of apoptosis.