title: The heme oxygenases: important regulators of pregnancy and preeclampsia.
abstract: The heme oxygenase system has long been believed to act largely as a housekeeping unit, converting prooxidant free heme from heme protein degradation into the benign bilirubin for conjugation and safe excretion. In recent decades, however, heme oxygenases have emerged as important regulators of cardiovascular function, largely through the production of their biologically active metabolites: carbon monoxide, bilirubin, and elemental iron. Even more recently, a number of separate lines of evidence have demonstrated an important role for the heme oxygenases in the establishment and maintenance of pregnancy. Early preclinical and clinical studies have associated defects in the heme oxygenase with the obstetrical complication preeclampsia, as well as failure to establish adequate placental blood flow, an underlying mechanism of the disorder. Several recent preclinical studies have suggested, however, that the heme oxygenase system could serve as a valuable therapeutic tool for the management of preeclampsia, which currently has few pharmacological options. This review will summarize the role of heme oxygenases in pregnancy and highlight their potential in advancing the management of patients with preeclampsia.
authors.affiliation: Department of Physiology and Biophysics, The University of Mississippi Medical Center, Jackson, Mississippi; and Department of Biochemistry, The University of Mississippi Medical Center, Jackson, Mississippi.
authors.forename: Eric M
authors.initials: EM
authors.lastname: George
authors.affiliation: Department of Physiology and Biophysics, The University of Mississippi Medical Center, Jackson, Mississippi; and.
authors.forename: Junie P
authors.initials: JP
authors.lastname: Warrington
authors.affiliation: Department of Physiology and Biophysics, The University of Mississippi Medical Center, Jackson, Mississippi; and.
authors.forename: Frank T
authors.initials: FT
authors.lastname: Spradley
authors.affiliation: Department of Physiology and Biophysics, The University of Mississippi Medical Center, Jackson, Mississippi; and.
authors.forename: Ana C
authors.initials: AC
authors.lastname: Palei
authors.affiliation: Department of Physiology and Biophysics, The University of Mississippi Medical Center, Jackson, Mississippi; and jgranger@umc.edu.
authors.forename: Joey P
authors.initials: JP
authors.lastname: Granger
mesh_terms: D000818:Animals; D001663:Bilirubin / Q000378:metabolism; D002248:Carbon Monoxide / Q000378:metabolism; D005260:Female; D006418:Heme / Q000378:metabolism; D006419:Heme Oxygenase (Decyclizing) / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D010920:Placenta / Q000378:metabolism*; D011225:Pre-Eclampsia / Q000201:enzymology*; D011247:Pregnancy
chemical_list: D006418:Heme; D002248:Carbon Monoxide; D006419:Heme Oxygenase (Decyclizing); D001663:Bilirubin