Zobrazeno 1 - 10
of 92
pro vyhledávání: '"Richard D. Levere"'
Autor:
Yan Lavrovsky, M. E. Gerritsen, Richard D. Levere, Shigeki Shibahara, M L Schwartzman, Nader G. Abraham, Attallah Kappas, R A Stoltz
Publikováno v:
Proceedings of the National Academy of Sciences. 92:6798-6802
Heme oxygenase (HO) is a stress protein and has been suggested to participate in defense mechanisms against agents that may induce oxidative injury such as metals, endotoxin, heme/hemoglobin, and various cytokines. Overexpression of HO in cells might
Publikováno v:
Journal of Cellular Biochemistry. 57:409-414
Heme oxygenase is the rate-limiting enzyme in heme catabolism, and is induced by oxidative stress, foreign and endogenous chemicals, and many trace elements and heavy metals. This study examined the effect of the oxidative state of the heavy metal ti
Autor:
Richard D. Levere, Robert A. Stoltz, Teresa K. Neil, Nader G. Abraham, Samuel Jiang, Michael W. Dunn, Atallah Kappas, Michal Laniado-Schwartzman
Publikováno v:
Journal of Ocular Pharmacology and Therapeutics. 11:455-468
Heme oxygenase, the rate-limiting enzyme in the degradation of heme to bile-pigments and carbon monoxide, is induced in response to increased oxidative stress and is believed to provide a cytoprotective effect. We investigated the role of heme oxygen
Publikováno v:
Proceedings of the National Academy of Sciences. 91:5987-5991
Heme oxygenase (HO) is the rate-limiting enzyme in heme catabolism and its activity is induced by many agents, including its substrate heme, heavy metals, UV radiation, and other injurious oxidant conditions. We examined the presence of several regul
Autor:
Jean-Louis Da Silva, Michal L. Schwartzman, Richard D. Levere, Bruno Escalante, Eunkyue Park, Martin Tiefenthaler, Nader G. Abraham
Publikováno v:
The American Journal of the Medical Sciences. 307:173-181
The effect of SnCl2 on the transcription of the heme oxygenase gene in spontaneously hypertensive rats was examined using cDNA for the rat heme oxygenase (HO-1). An increase in renal HO-1 mRNA levels was observed in response to SnCl2 treatment. Quant
Autor:
J. L. Chertkov, Attallah Kappas, Richard D. Levere, Shanlong Jiang, Nader G. Abraham, Jonathan S. Harrison, J. D. Lutton
Publikováno v:
Blood. 82:3574-3579
The ability of combination treatment with erythropoietin (Epo) and heme to rescue hematopoietic activity in mice from the suppressive effect of azidothymidine (AZT) was determined. Exposure of mice to AZT for 5 weeks produced marked anemia, thrombocy
Autor:
Shigeki Shibahara, Richard D. Levere, Attallah Kappas, Margaret O. Griffin, Nader G. Abraham, J. D. Lutton, Miki Nishimura
Publikováno v:
Hepatology. 17:861-868
Exposure of Hep3B cells to metalloporphyrins (tinprotoporphyrin and heme) or cobalt chloride resulted in the production of a significant number of heme oxygenase transcripts, erythropoietin transcripts or both, as indicated by in situ hybridization.
Autor:
Dietmar Fuchs, Richard D. Levere, Günter Weiss, Attallah Kappas, Helmut Wachter, Nader G. Abraham, J. D. Lutton, Gunter Bock, Gabriele Werner-Felmayer
Publikováno v:
Experimental Biology and Medicine. 202:470-475
Previous results have demonstrated links between cell-mediated immunity, interferon (IFN)-gamma and neopterin production with heme, porphyrins, and iron metabolism. In this study, we compared the effects of heme, several metalloporphyrins, protoporph
Autor:
Jonathan S. Harrison, J. L. Chertkov, Nader G. Abraham, M. Tiefenthaler, J. D. Lutton, Richard D. Levere, Shanlong Jiang
Publikováno v:
STEM CELLS. 11:218-227
In this study we report on the establishment of novel conditions which permit efficient ret-rovirus-mediated gene transfer of human adenosine deaminase (ADA) into murine hematopoietic progenitors. Using Southern blot analysis and an ADA probe, we dem
Autor:
A. C. Brown, J. D. Lutton, Richard D. Levere, Satei T. Moqattash, N. G. Abraham, J.‐L. da Silva
Publikováno v:
Journal of Cellular Biochemistry. 49:259-265
In situ hybridization and Northern analysis of heme oxygenase (HO) mRNA was used to determine the induction and expression of HO by various environmental agents. Exposure of Hep3B cells to hemin (10 microM) for as little as 5 min resulted in signific