Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Alvin I. Goodman"'
Autor:
Shuo Quan, David E. Stec, Liming Yang, S. Omura, Rafał Olszanecki, M. Li, Alvin I. Goodman, Nader G. Abraham
Publikováno v:
Kidney International. 72:945-953
Radiocontrast agents are thought to induce acute kidney injury in part through increased production of reactive oxygen species and increased cellular apoptosis. In this study we determined whether heme oxygenase-1 could prevent or reduce radiocontras
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::265fe53f9f329ed764e31c46c6cddb6e
https://doi.org/10.1038/sj.ki.5002447
https://doi.org/10.1038/sj.ki.5002447
Publikováno v:
Drug Discovery Today: Disease Mechanisms. 4:41-46
Heme oxygenase (HO) has been shown to be critical for attenuating reactive oxygen species (ROS) through its ability to degrade heme and produce carbon monoxide (CO) and bilirubin. Excess free heme and proinflammatory growth factors are major contribu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::804984d24e02cf077a757dec543a5fc9
https://doi.org/10.1016/j.ddmec.2007.06.006
https://doi.org/10.1016/j.ddmec.2007.06.006
Autor:
Michael S. Goligorsky, Sylvia Shenouda, Heidi Fusco, Stephen J. Peterson, John A. McClung, Atallah Kappas, Adam Kruger, Alvin I. Goodman, Melvin B. Weiss, Nader G. Abraham, Michal L. Schwartzman
Publikováno v:
Journal of Pharmacology and Experimental Therapeutics. 319:1144-1152
Heme oxygenase (HO) plays a critical role in the regulation of cellular oxidative stress. The effects of the reactive oxygen species scavenger ebselen and the HO inducers cobalt protoporphyrin and stannous chloride (SnCl(2)) on HO protein levels and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb408d5eb8a5b6f75fbddb1861825bbb
https://doi.org/10.1124/jpet.106.107482
https://doi.org/10.1124/jpet.106.107482
Autor:
Liming Yang, Maria Antonietta Di Noia, Nader G. Abraham, Ferdinando Palmieri, Alvin I. Goodman, Sarah Van Driesche, Shuo Quan
Publikováno v:
Journal of Biological Chemistry. 281:15687-15693
Up-regulation of heme oxygenase (HO-1) by either cobalt protoporphyrin (CoPP) or human gene transfer improves vascular and renal function by several mechanisms, including increases in antioxidant levels and decreases in reactive oxygen species (ROS)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfa92eb6f5e50de465b2a96bf0762f31
https://doi.org/10.1074/jbc.m510595200
https://doi.org/10.1074/jbc.m510595200
Autor:
Nader G. Abraham, Luigi Fabrizio Rodella, Raymond F. Regan, Praveen N. Chander, Phyllis A. Dennery, Alvin I. Goodman, Rita Rezzani, Elias A. Lianos, Michal L. Schwartzman, Saadet Turkseven
Publikováno v:
Journal of the American Society of Nephrology. 17:1073-1081
Heme oxygenase-1 (HO-1) and -2 play an important role in cytoprotection and are physiologic regulators of heme-dependent protein synthesis in renal tissues. The impact of HO-2 deletion comparing hyperglycemic HO-2 (+/+) mice and HO-2 knockout (-/-) m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f08b926fe10b7d6990a6727685c889e
https://doi.org/10.1681/asn.2004121082
https://doi.org/10.1681/asn.2004121082
Publikováno v:
Current Neurovascular Research. 2:157-161
Cyclosporine A (CsA) is the immunosuppressant of first choice in allotransplantation. Its use is associated with side effects of nephrotoxicity and neurotoxicity, which are among the most prominent. This study was undertaken to explore whether expres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8bebeab961d9a3a26b5410eaf32d451
https://doi.org/10.2174/1567202053586730
https://doi.org/10.2174/1567202053586730
Autor:
Sylvia Shnouda, Michal L. Schwartzman, Shuo Quan, Alberto Nasjletti, Nader G. Abraham, Liming Yang, Alvin I. Goodman
Publikováno v:
Kidney International. 65(5):1628-1639
Expression of human heme oxygenase-1 in the thick ascending limb attenuates angiotensin II–mediated increase in oxidative injury. Background Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dcb8b08a28fc3f8e0377113dc7e9662
Publikováno v:
Experimental Biology and Medicine. 228:576-583
Heme oxygenase (HO) catalyzes the conversion of heme to biliverdin with the release of iron and carbon monoxide. HO-1 is inducible by inflammatory conditions, which cause oxidative stress in endothelial cells. Overexpression of human HO-1 in endothel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1652e38edbfaa14fcc42a2d359fdec19
https://doi.org/10.1177/15353702-0322805-31
https://doi.org/10.1177/15353702-0322805-31
Modulation of cGMP by human HO-1 retrovirus gene transfer in pulmonary microvessel endothelial cells
Autor:
Nader G. Abraham, Alberto Nasjletti, Alvin I. Goodman, T. Burke-Wolin, Christopher J. Mingone, Liming Yang, Paul A. Mieyal, Michael S. Wolin, Shuo Quan
Publikováno v:
American Journal of Physiology-Lung Cellular and Molecular Physiology. 283:L1117-L1124
Carbon monoxide (CO) stimulates guanylate cyclase (GC) and increases guanosine 3′,5′-cyclic monophosphate (cGMP) levels. We transfected rat-lung pulmonary endothelial cells with a retrovirus-mediated human heme oxygenase (hHO)-1 gene. Pulmonary c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::549d19c66f63fedf4109952e603cca40
https://doi.org/10.1152/ajplung.00365.2001
https://doi.org/10.1152/ajplung.00365.2001
Publikováno v:
Journal of Cellular Biochemistry. 87:377-385
Heme oxygenase (HO) is the rate-limiting enzyme in the formation of bilirubin, an antioxidant, and carbon monoxide (CO), a cell cycle modulator and a vasodilator. Cyclooxygenase (COX) is a hemeprotein that catalyzes the conversion of arachidonic acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee3df68152287bdc030dbdb7d6db57fe
https://doi.org/10.1002/jcb.10316
https://doi.org/10.1002/jcb.10316