title: Iron dextran treatment does not induce serum protein carbonyls in the newborn pig.
abstract: Oxidation of serum proteins can lead to carbonyl formation that alters their function and is often associated with stress-related diseases. As it is recommended that all pigs reared in modern production facilities be given supplemental iron at birth to prevent anemia, and metals can catalyze the carbonylation of proteins, the primary objective of this study was to determine whether standard iron dextran treatment was associated with enhanced serum protein oxidation in newborn piglets. Piglets were treated with 100 mg of iron dextran intramuscularly either on the day of birth, or on the third day after birth. Blood samples were collected from piglets 48 or 96 h after treatment and serum was harvested. For quantification, serum protein carbonyls were converted to hydrazones with dinitrophenyl hydrazine and analyzed spectrophotometrically. To identify and determine relative distribution of carbonylated proteins, serum protein carbonyls were derivatized with biotin hydrazide, separated by two-dimensional polyacrylamide gel electrophoresis, stained with avidin-fluorescein and identified by mass spectrometry. The standard iron dextran treatment was associated with no increase in total oxidized proteins if given either on the first or third day of life. In addition, with a few noted exceptions, the overall distribution and identification of oxidized proteins were similar between control and iron dextran-treated pigs. These results indicate that while iron dextran treatment is associated with a marked increase in circulating iron, it does not appear to specifically induce the oxidation of serum proteins.
authors.affiliation: U.S. Department of Agriculture, Animal Biosciences and Biotechnology Laboratory, Animal and Natural Resources Institute, Beltsville Agricultural Research Center, Building 200, Room 202, BARC-East, Beltsville, MD 20705, USA. thomas.caperna@ars.usda.gov
authors.forename: T J
authors.initials: TJ
authors.lastname: Caperna
authors.forename: A E
authors.initials: AE
authors.lastname: Shannon
authors.forename: L A
authors.initials: LA
authors.lastname: Blomberg
authors.forename: W M
authors.initials: WM
authors.lastname: Garrett
authors.forename: T G
authors.initials: TG
authors.lastname: Ramsay
mesh_terms: D000818:Animals; D000831:Animals, Newborn / Q000097:blood*; D001360:Avidin; D001798:Blood Proteins / Q000187:drug effects / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D016650:Fluorescein-5-isothiocyanate / Q000031:analogs & derivatives; D006397:Hematinics / Q000008:administration & dosage* / Q000009:adverse effects; D007202:Indicators and Reagents; D007501:Iron / Q000097:blood; D007505:Iron-Dextran Complex / Q000008:administration & dosage* / Q000009:adverse effects; D008297:Male; D010084:Oxidation-Reduction / Q000187:drug effects; D050050:Protein Carbonylation / Q000187:drug effects*; D012394:Rosaniline Dyes; D013552:Swine / Q000097:blood*
chemical_list: D001798:Blood Proteins; D006397:Hematinics; D007202:Indicators and Reagents; D012394:Rosaniline Dyes; C036963:fluorescein isothiocyante avidin; D001360:Avidin; C048139:Coomassie blue; D007505:Iron-Dextran Complex; D007501:Iron; D016650:Fluorescein-5-isothiocyanate