@article {2650,
	title = {Propofol protects against hydrogen peroxide-induced injury in cardiac H9c2 cells via Akt activation and Bcl-2 up-regulation},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {389},
	number = {1},
	year = {2009},
	note = {ISI Document Delivery No.: 555SMTimes Cited: 4Cited Reference Count: 26Wang, Baohua Shravah, Jayant Luo, Honglin Raedschelders, Koen Chen, David D. Y. Ansley, David M.},
	month = {Nov},
	pages = {105-111},
	type = {Article},
	abstract = {<p>Propofol is a widely used intravenous anesthetic agent with antioxidant properties secondary to its phenol based chemical structure. Treatment with propofol has been found to attenuate oxidative stress and prevent ischemia/reperfusion injury in rat heart. Here, we report that propofol protects cardiac H9c2 cells from hydrogen peroxide (H2O2)-induced injury by triggering the activation of Akt and a parallel up-regulation of Bcl-2. We show that pretreatment with propofol significantly protects against H2O2-induced injury. We further demonstrate that propofol activates the PI3K-Akt signaling pathway. The protective effect of propofol on H2O2-induced injury is reversed by PI3K inhibitor wortmannin, which effectively suppresses propofol-induced activation of Akt, up-regulation of Bcl-2, and protection from apoptosis. Collectively, our results reveal a new mechanism by which propofol inhibits H2O2-induced injury in cardiac H9c2 cells, supporting a potential application of propofol as a preemptive cardioprotectant in clinical settings such as coronary bypass surgery. (C) 2009 Elsevier Inc. All rights reserved.</p>},
	keywords = {15-F-2T-ISOPROSTANE FORMATION, Akt, antioxidant capacity, apoptosis, Bcl-2, CARDIOMYOCYTES, ENDOTHELIAL-CELLS, H9c2 cells, INJURY, KINASE-C, OXIDATIVE STRESS, Propofol, RAT-HEART, REDUCES APOPTOSIS, REPERFUSION, SENSITIVITY, SURVIVAL},
	isbn = {0006-291X},
	doi = {doi: 10.1016/j.bbrc.2009.08.097},
	url = {<Go to ISI>://000274534900020},
	author = {Wang, B. H. and Shravah, J. and Luo, H. L. and Raedschelders, K. and Chen, D. D. Y. and Ansley, D. M.}
}
@article {2422,
	title = {Thymic progenitor homing and lymphocyte homeostasis are linked via S1P-controlled expression of thymic P-selectin/CCL25},
	journal = {Journal of Experimental Medicine},
	volume = {206},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 444VXTimes Cited: 19Cited Reference Count: 55Gossens, Klaus Naus, Silvia Corbel, Stephane Y. Lin, Shujun Rossi, Fabio M. V. Kast, Joergen Ziltener, Hermann J.},
	month = {Apr},
	pages = {761-778},
	type = {Article},
	abstract = {Thymic T cell progenitor (TCP) importation is a periodic, gated event that is dependent on the expression of functional P-selectin ligands on TCPs. Occupancy of intrathymic TCP niches is believed to negatively regulate TCP importation, but the nature of this feedback mechanism is not yet resolved. We show that P-selectin and CCL25 are periodically expressed in the thymus and are essential parts of the thymic gate-keeping mechanism. Periodicity of thymic TCP receptivity and the size of the earliest intrathymic TCP pool were dependent on the presence of functional P-selectin ligand on TCPs. Furthermore, we show that the numbers of peripheral blood lymphocytes directly affected thymic P-selectin expression and TCP receptivity. We identified sphingosine-1-phosphate (S1P) as one feedback signal that could mediate influence of the peripheral lymphocyte pool on thymic TCP receptivity. Our findings suggest a model whereby thymic TCP importation is controlled by both early thymic niche occupancy and the peripheral lymphocyte pool via S1P.},
	keywords = {ADULT-MOUSE, ENDOTHELIAL-CELLS, EPITHELIAL-CELLS, KAPPA-B, LIGAND PSGL-1, MICE, NECROSIS-FACTOR-ALPHA, P-SELECTIN, PLASMA SPHINGOSINE 1-PHOSPHATE, T-CELLS},
	isbn = {0022-1007},
	url = {<Go to ISI>://000266009600006},
	author = {Gossens, K. and Naus, S. and Corbel, S. Y. and Lin, S. J. and Rossi, F. M. V. and Kast, J. and Ziltener, H. J.}
}
@article {1505,
	title = {Identification of sokotrasterol sulfate as a novel proangiogenic steroid},
	journal = {Circulation Research},
	volume = {99},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 070DTTimes Cited: 3Cited Reference Count: 39Murphy, Siun Larrivee, Bruno Pollet, Ingrid Craig, Kyle S. Williams, David E. Huang, Xin-Hui Abbott, Megan Wong, Fred Curtis, Cameron Conrads, Thomas P. Veenstra, Timothy Puri, Mira Hsiang, York Roberge, Michel Andersen, Raymond J. Karsan, Aly},
	month = {Aug},
	pages = {257-265},
	type = {Article},
	abstract = {The potential to promote neovascularization in ischemic tissues using exogenous agents has become an exciting area of therapeutics. In an attempt to identify novel small molecules with angiogenesis promoting activity, we screened a library of natural products and identified a sulfated steroid, sokotrasterol sulfate, that induces angiogenesis in vitro and in vivo. We show that sokotrasterol sulfate promotes endothelial sprouting in vitro, new blood vessel formation on the chick chorioallantoic membrane, and accelerates angiogenesis and reperfusion in a mouse hindlimb ischemia model. We demonstrate that sulfation of the steroid is critical for promoting angiogenesis, as the desulfated steroid exhibited no endothelial sprouting activity. We thus developed a chemically synthesized sokotrasterol sulfate analog, 2 beta,3 alpha,6 alpha-cholestanetrisulfate, that demonstrated equivalent activity in the hindlimb ischemia model and resulted in the generation of stable vessels that persisted following cessation of therapy. The function of sokotrasterol sulfate was dependent on cyclooxygenase-2 activity and vascular endothelial growth factor induction, as inhibition of either cyclooxygenase-2 or vascular endothelial growth factor blocked angiogenesis. Surface expression of alpha(v)beta(3) integrin was also necessary for function, as neutralization of alpha(v)beta(3) integrin, but not beta(1) integrin, binding abrogated endothelial sprouting and antiapoptotic activity in response to sokotrasterol sulfate. Our findings indicate that sokotrasterol sulfate and its analogs can promote angiogenesis in vitro and in vivo and could potentially be used for promoting neovascularization to relieve the sequelae of vasoocclusive diseases.},
	keywords = {ACTIVATION, ANGIOGENESIS, apoptosis, ARTERIOGENESIS, ENDOTHELIAL-CELLS, endothelium, IN-VITRO, INHIBITION, INTEGRIN ALPHA(V)BETA(3), ischemia, MARINE NATURAL-PRODUCTS, NF-KAPPA-B},
	isbn = {0009-7330},
	url = {<Go to ISI>://000239501200009},
	author = {Murphy, S. and Larrivee, B. and Pollet, I. and Craig, K. S. and Williams, D. E. and Huang, X. H. and Abbott, M. and Wong, F. and Curtis, C. and Conrads, T. P. and Veenstra, T. and Puri, M. and Hsiang, Y. and Roberge, M. and Andersen, R. J. and Karsan, A.}
}
@article {330,
	title = {Plasmid DNA damage caused by methylated arsenicals, ascorbic acid and human liver ferritin},
	journal = {Toxicology Letters},
	volume = {133},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 575QMTimes Cited: 46Cited Reference Count: 499th International Congress of ToxicologyJUL 08-12, 2001BRISBANE, AUSTRALIA},
	month = {Jul},
	pages = {47-57},
	type = {Proceedings Paper},
	abstract = {Both dimethylarsinic acid (DMA(V)) and dimethylarsinous acid (DMA(III)) release iron from human liver ferritin (HLF) with or without the presence of ascorbic acid. With ascorbic acid the rate of iron release from HLF by DMA(V) was intermediate (3.37 nM/min, P < 0.05) and by DMA(III) was much higher (16.3 nM/min, P < 0.001). No pBR322 plasmid DNA damage was observed from in vitro exposure to arsenate (iAs(V)), arsenite (iAs(III)), monomethylarsonic acid (MMA(V)), monomethylarsonous acid (MMA(III)) or DMA(V) alone. DNA damage was observed following DMA(III) exposure; coexposure to DMA(III) and HLF caused more DNA damage; considerably higher amounts of DNA damage was caused by coexposure of DMA(III), HLF and ascorbic acid. Diethylenetriaminepentaacetic acid (an iron chelator), significantly inhibited DNA damage. Addition of catalase (which can increase Fe2+ concentrations) further increased the plasmid DNA damage. Iron-dependent DNA damage could be a mechanism of action of human arsenic carcinogenesis. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.},
	keywords = {arsenic, BIOCHEMICAL PARAMETERS, CARCINOGENESIS, DIMETHYLARSINIC ACID, dimethylarsinous acid, DMA(111), DNA damage, ENDOTHELIAL-CELLS, human liver ferritin, INDUCTION, INORGANIC ARSENICS, iron, MICE, MONOMETHYLARSONOUS ACID, reactive oxygen, species, STRAND BREAKS},
	isbn = {0378-4274},
	url = {<Go to ISI>://000176959200005},
	author = {Ahmad, S. and Kitchin, K. T. and Cullen, W. R.}
}
@article {4600,
	title = {Methylarsenicals and arsinothiols are potent inhibitors of mouse liver thioredoxin reductase},
	journal = {Chemical Research in Toxicology},
	volume = {12},
	number = {10},
	year = {1999},
	note = {ISI Document Delivery No.: 248DFTimes Cited: 114Cited Reference Count: 64},
	month = {Oct},
	pages = {924-930},
	type = {Article},
	abstract = {Thioredoxin reductase (TR, EC 1.6.4.5) was purified 5800-fold from the livers of adult male B6C3F1 mice. The estimated molecular mass of the purified protein was about 57 kDa, The activity of the purified enzyme was monitored by the NADPH-dependent reduction of 5,5{\textquoteright}-dithiobis(2-nitrobenzoic acid) (DTNB); this activity was fully inhibited by 1 mu M aurothioglucose. Arsenicals and arsinothiols, complexes of As-III-containing compounds with L-cysteine or glutathione, were tested as inhibitors of the DTNB reductase activity of the purified enzyme. Pentavalent arsenicals were much less potent inhibitors than trivalent arsenicals. Among all the arsenicals, CH3AsIII was the most potent inhibitor of TR. CH3AsIII was found to be a competitive inhibitor of the reduction of DTNB (K-i similar to 100 nM) and a noncompetitive inhibitor of the oxidation of NADPH. The inhibition of TR by CH3AsIII was time-dependent and could not be reversed by the addition of a dithiol-containing molecule, 2,3-dimercaptosuccinic acid, to the reaction mixture. The inhibition of TR by CH3AsIII required the simultaneous presence of NADPH in the reaction mixture. However, unlike other pyridine nucleotide disulfide oxidoreductases, there was no evidence that mouse liver TR was inactivated by exposure to NADPH. Treatment with CH3AsIII did not increase the NADPH oxidase activity of the purified enzyme. Thus, CH3AsIII, a putative intermediate in the pathway for the biomethylation of As, is a potent and irreversible inhibitor of an enzyme involved in the response of the cell to oxidative stress.},
	keywords = {ARSENATE REDUCTASE, CANCER-CELLS, ENDOTHELIAL-CELLS, ESCHERICHIA-COLI, GLUTATHIONE-REDUCTASE, KAPPA-B ACTIVATION, LIPOAMIDE DEHYDROGENASE, MAMMALIAN THIOREDOXIN, MULTI-ENZYME COMPLEX, RABBIT ERYTHROCYTES},
	isbn = {0893-228X},
	url = {<Go to ISI>://000083259500008},
	author = {Lin, S. and Cullen, W. R. and Thomas, D. J.}
}
