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Iron dextran treatment does not induce serum protein carbonyls in the newborn pig*

Published online by Cambridge University Press:  19 August 2011

T. J. Caperna*
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
A. E. Shannon
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
L. A. Blomberg
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
W. M. Garrett
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
T. G. Ramsay
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
*
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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.

Type
Full Paper
Copyright
Copyright © The Animal Consortium 2011

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Footnotes

*

Mention of trade name, proprietary product or vendor does not constitute a guarantee or warranty of the product by the U.S. Department of Agriculture or imply its approval to the exclusion of other products or vendors that also may be suitable.

References

Adams, S, Green, P, Claxton, R, Simcox, S, Williams, MV, Walsh, K, Leeuwenburgh, C 2001. Reactive carbonyl formation by oxidative and non-oxidative pathways. Frontiers in Bioscience 6, a17a24.CrossRefGoogle ScholarPubMed
Caperna, TJ, Shannon, AE, Garrett, WM 2008. A gel-based reference map of the porcine hepatocyte proteome. Domestic Animal Endocrinology 35, 142156.CrossRefGoogle ScholarPubMed
Caperna, TJ, Failla, ML, Steele, NC, Richards, MP 1987. Accumulation and metabolism of iron-dextran by hepatocytes, Kupffer cells and endothelial cells in the neonatal pig liver. Journal of Nutrition 117, 312320.CrossRefGoogle ScholarPubMed
Caperna, TJ, Shannon, AE, Blomberg, LA, Garrett, WM, Ramsay, TG 2010. Identification of protein carbonyls in serum of the fetal and neonatal pig. Comparative Biochemistry and Physiology Part B 156, 189196.CrossRefGoogle ScholarPubMed
Egeli, AK, Framstad, T 1999. An evaluation of iron-dextran supplementation in piglets administered by injection on the first, third or fourth day after birth. Research in Veterinary Science 66, 179184.CrossRefGoogle ScholarPubMed
Jahnen-Dechent, W, Schäfer, C, Ketteler, M, McKee, MD 2008. Mineral chaperones: a role for fetuin-A and osteopontin in the inhibition and regression of pathologic calcification. Journal of Molecular Medicine 86, 379389.CrossRefGoogle ScholarPubMed
Knight, CD, Klasing, KC, Forsyth, DM 1983. E. coli growth in serum of iron dextran-supplemented pigs. Journal of Animal Science 57, 387395.CrossRefGoogle Scholar
Koos, R, Brandenburg, V, Mahnken, AH, Mühlenbruch, G, Stanzel, S, Günther, RW, Floege, J, Jahnen-Dechent, W, Kelm, M, Kühl, HP 2009. Association of fetuin-A levels with the progression of aortic valve calcification in non-dialyzed patients. European Heart Journal 30, 20542061.CrossRefGoogle ScholarPubMed
Levine, RL, Garland, D, Oliver, CN, Amici, A, Climent, I, Lenz, A-G, Ahn, B-W, Shaltiel, S, Stadtman, ER 1990. Determination of carbonyl content in oxidatively modified proteins. Methods in Enzymology 186, 464478.CrossRefGoogle ScholarPubMed
Lipiński, P, Starzyński, RR, Canonne-Hergaux, F, Tudek, B, Oliński, R, Kowalczyk, P, Dziaman, T, Thibaudeau, O, Gralak, MA, Smuda, E, Woliński, J, Usińska, A, Zabielski, R 2010. Benefits and risks of iron supplementation in anemic neonatal pigs. American Journal of Pathology 177, 12331243.CrossRefGoogle ScholarPubMed
Moe, SM, Chen, NX 2005. Inflammation and vascular calcification. Blood Purification 23, 6471.CrossRefGoogle ScholarPubMed
Nakamura, M, Tsumoto, K, Ishimura, K, Kumagai, I 2002. Detection of biotinylated proteins in polyacrylamide gels using an avidin-fluorescein conjugate. Analytical Biochemistry 304, 231235.CrossRefGoogle ScholarPubMed
Nerurkar, LS, Marino, PA, Adams, DO 1981. Quantification of selected intracellular and secreted hydrolases of macrophages. In Manual of macrophage methodology (ed. HB Herscowitz, HT Holden, JA Bellanti and A Ghaffer), pp. 229247. Marcel Dekker, Inc., New York, NY, USA.Google Scholar
Nyström, T 2005. Role of oxidative carbonylation in protein quality control and senescence. EMBO Journal 24, 13111317.CrossRefGoogle ScholarPubMed
Pandur, E, Nagy, J, Poór, VS, Sarnyai, Á, Huszár, A, Miseta, A, Sipos, K 2009. Alpha-1 antitrypsin binds preprohepcidin intracellularly and prohepcidin in the serum. FEBS Journal 276, 20122021.CrossRefGoogle ScholarPubMed
Pardo Andreu, GL, Inada, NM, Vercesi, AE, Curti, C 2009. Uncoupling and oxidative stress in liver mitochondria isolated from rats with acute iron overload. Archives of Toxicology 83, 4753.CrossRefGoogle ScholarPubMed
Perkins, DN, Pappin, DJC, Creasy, DM, Cottrell, JS 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 35513567.3.0.CO;2-2>CrossRefGoogle ScholarPubMed
Robinson, CE, Keshavarzian, A, Pasco, DS, Frommel, TO, Winship, DH, Holmes, EW 1999. Determination of protein carbonyl groups by immunoblotting. Analytical Biochemistry 266, 4857.CrossRefGoogle ScholarPubMed
Schlosser, A, Volkmer-Engert, R 2003. Volatile polydimethylcyclosiloxanes in the ambient laboratory air identified as source of extreme background signals in nanoelectrospray mass spectrometry. Journal of Mass Spectrometry 38, 523525.CrossRefGoogle ScholarPubMed
Stadtman, ER, Levine, RL 2000. Protein oxidation. Annals of the New York Academy of Sciences 899, 191208.CrossRefGoogle ScholarPubMed
Szabo, P, Bilkei, G 2002. Iron deficiency in outdoor pig production. Journal of Veterinary Medicine A 49, 390391.CrossRefGoogle ScholarPubMed
Yoo, B-S, Regnier, FE 2004. Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-flourescein affinity staining. Electrophoresis 25, 13341341.CrossRefGoogle ScholarPubMed
Zimmerman, DR 1980. Iron in swine nutritionNFIA literature review on iron in animals and poultry nutrition (ed. HR Conrad, DR Zimmerman and GF Combs), pp. 561NFIA, West Des Moines, IA, USA.Google Scholar