title: Compromised liver mitochondrial function and complex activity in low feed efficient broilers are associated with higher oxidative stress and differential protein expression.
abstract: Variations in broiler growth and efficiency have been explained in part by differences in mitochondrial function and biochemistry in broilers. To further our knowledge in this regard, 2 experiments were carried out to determine the relationships of a) mitochondrial function and activities of various electron transport chain (ETC) complexes; b) production of H2O2, a reactive oxygen species (ROS), and its association with protein oxidation; and c) mitochondrial protein expression in liver of a single line male broilers with low or high feed efficiency (FE, n = 5 to 8 per group). Mitochondrial function and complex activities were measured polarographically and spectrophotometrically, respectively. H2O2 was measured fluorimetrically, whereas oxidized protein (carbonyls) and specific mitochondrial proteins were analyzed using Western blots. Mitochondrial function (ETC coupling) and activities of ETC complexes (I, II, III, and IV) were higher in high FE compared with low FE broilers. H2O2 and protein carbonyls were higher in the livers of low FE broilers than in high FE broilers. Whereas the expression of 4 immunoreactive proteins [NAD3 (complex I), subunit VII (complex III), cytochrome c oxidase subunits (COX) II, and COX IVb (complex IV)] were higher in low FE liver mitochondria and 2 proteins [subunit 70 (complex II) and a-ATP synthase (complex V)] were higher in high FE birds, there were no differences between groups in the expression of 18 other mitochondrial proteins. In conclusion, increases in oxidative stress in low FE broilers were caused by or may contribute to differences in mitochondrial function (ETC coupling and complex activities) or the differential expression of steady-state levels of some mitochondrial proteins in the liver. Understanding the role of oxidative stress in Low FE broilers will provide clues in understanding the cellular basis of feed efficiency.
authors.affiliation: Department of Poultry Science, Center of Excellence for Poultry Science, University of Arkansas, Fayetteville, Arkansas 72701, USA.
authors.forename: M
authors.initials: M
authors.lastname: Iqbal
authors.forename: N R
authors.initials: NR
authors.lastname: Pumford
authors.forename: Z X
authors.initials: ZX
authors.lastname: Tang
authors.forename: K
authors.initials: K
authors.lastname: Lassiter
authors.forename: C
authors.initials: C
authors.lastname: Ojano-Dirain
authors.forename: T
authors.initials: T
authors.lastname: Wing
authors.forename: M
authors.initials: M
authors.lastname: Cooper
authors.forename: W
authors.initials: W
authors.lastname: Bottje
mesh_terms: D000821:Animal Feed; D000824:Animal Nutritional Physiological Phenomena; D000818:Animals; D015153:Blotting, Western; D001947:Breeding; D002645:Chickens / Q000502:physiology*; D004272:DNA, Mitochondrial / Q000235:genetics; D004579:Electron Transport; D004591:Electrophoresis, Polyacrylamide Gel; D015870:Gene Expression; D006861:Hydrogen Peroxide / Q000378:metabolism; D008297:Male; D008930:Mitochondria, Liver / Q000502:physiology*; D024101:Mitochondrial Proteins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D010084:Oxidation-Reduction; D018384:Oxidative Stress
chemical_list: D004272:DNA, Mitochondrial; D024101:Mitochondrial Proteins; D006861:Hydrogen Peroxide