Ferrous iron release from transferrin by human neutrophil-derived superoxide anion: Effect of pH and iron saturation
dc.contributor.author | Brieland, Joan K. | en_US |
dc.contributor.author | Fantone, Joseph C. | en_US |
dc.date.accessioned | 2006-04-10T14:51:37Z | |
dc.date.available | 2006-04-10T14:51:37Z | |
dc.date.issued | 1991-01 | en_US |
dc.identifier.citation | Brieland, Joan K., Fantone, Joseph C. (1991/01)."Ferrous iron release from transferrin by human neutrophil-derived superoxide anion: Effect of pH and iron saturation." Archives of Biochemistry and Biophysics 284(1): 78-83. <http://hdl.handle.net/2027.42/29537> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DN9V0C-DB/2/fa09b5c21226ff2ee3bffd72bc1097da | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/29537 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1846518&dopt=citation | en_US |
dc.description.abstract | The ability of superoxide anion (O2-) from stimulated human neutrophils (PMNs) to release ferrous iron (Fe2+) from transferrin was assessed. At pH 7.4, unstimulated PMNs released minimal amounts of O2- and failed to facilitate the release of Fe2+ from holosaturated transferrin. In contrast, incubation of phorbol myristate acetate (PMA)-stimulated PMNs with holosaturated transferrin at pH 7.4 enhanced the release of Fe2+ from transferrin eightfold in association with marked generation of O2-. The release of Fe2+ was inhibited by addition of superoxide dismutase (SOD), indicating that the release of Fe2+ was dependent on PMN-derived extracellular O2-. In contrast, at physiologic pH (7.4), incubation of transferrin at physiological levels of iron saturation (e.g. 32%) with unstimulated or PMA stimulated PMNs failed to facilitate the release of Fe2+. The effect of decreasing the pH on the release of Fe2+ from transferrin by PMN-derived O2- was determined. Decreasing the pH greatly facilitated the release of Fe2+ from both holosaturated transferrin and from transferrin at physiological levels of iron saturation by PMN-derived O2-. Release of Fe2+ occurred despite a decrease in the amount of extracellular O2- generated by PMNs in an acidic environment. These results suggest that transferrin at physiologic levels of iron saturation may serve as a source of Fe2+ for biological reactions in disease states where activated phagocytes are present and there is a decrease in tissue pH. The unbound iron could participate in biological reactions including promoting propagation of lipid peroxidation reactions or hydroxyl radical formation following reaction with phagocytic cell-derived hydrogen peroxide. | en_US |
dc.format.extent | 664984 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 | Ferrous iron release from transferrin by human neutrophil-derived superoxide anion: Effect of pH and iron saturation | 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 | Unit for Laboratory Animal Medicine and the Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Unit for Laboratory Animal Medicine and the Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA | en_US |
dc.identifier.pmid | 1846518 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/29537/1/0000625.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(91)90266-L | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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