Prostaglandin biosynthesis can be triggered by lipid peroxides
dc.contributor.author | Hemler, Martin E. | en_US |
dc.contributor.author | Cook, Harold W. | en_US |
dc.contributor.author | Lands, William E. M. | en_US |
dc.date.accessioned | 2006-04-07T17:36:09Z | |
dc.date.available | 2006-04-07T17:36:09Z | |
dc.date.issued | 1979-04-01 | en_US |
dc.identifier.citation | Hemler, Martin E., Cook, Harold W., Lands, William E. M. (1979/04/01)."Prostaglandin biosynthesis can be triggered by lipid peroxides." Archives of Biochemistry and Biophysics 193(2): 340-345. <http://hdl.handle.net/2027.42/23604> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DW2MY4-2FY/2/7f72c84eeeb272ca3103deb6d20eaedf | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23604 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=111619&dopt=citation | en_US |
dc.description.abstract | Studies of ferriheme cyclooxygenase, using two different assay systems, show that a variety of peroxides can trigger a rapid acceleration of cyclooxygenase activity to produce prostaglandins. Lipid hydroperoxides formed by lipoxygenase were the most potent activators tested, followed by prostaglandin G2, which was slightly less potent. Peroxides nonspeciflcally generated during arachidonate autoxidation were as potent as the enzymatically formed lipid peroxides. These findings have important implications for cell function since any process which generates peroxides may activate the cyclooxygenase. Thus the balance between formation and removal of cellular lipid peroxides sets a peroxide tone that can regulate the rate of prostaglandin formation in cells. | en_US |
dc.format.extent | 522856 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Prostaglandin biosynthesis can be triggered by lipid peroxides | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.identifier.pmid | 111619 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23604/1/0000566.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(79)90038-9 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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