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Alterations in the Mitochondrial Proteome in Broilers fed a Lysine‐Deficient Diet
Author(s) -
Pomeroy Stephanie Katherine,
Williams Patricia M,
Webb Kenny E,
Blemings Kenneth P
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.738.10
Subject(s) - lysine , biochemistry , biology , beta oxidation , dehydrogenase , metabolism , mitochondrion , amino acid , chemistry , enzyme
In liver, the primary site of lysine degradation is the mitochondrial matrix, but the protein(s) responsible for lysine uptake to the matrix is(are) unknown. Changes in inner mitochondrial membrane protein abundances were observed in broilers fed lysine‐adequate (LA) or lysine‐deficient (LD) diets for 14 days. Two transport proteins were affected by the LD diet. Broilers consuming the LD diet expressed only 50% of a voltage‐gated anion‐selective and a voltage‐gated potassium channel compared to those consuming a LA diet, although presumably lysine is not transported via either of these proteins. The consumption of the LD diet impacted many aspects of metabolism. Glutamine synthase expression was decreased over 95% in the chickens consuming the LD diet. Electron transport chain (ETC) components were also altered. Broilers consuming the LD diet had over a 30% reduction in NADH dehydrogenase expression and almost a 90% decrease in the expression of ATP sythase. Proteins involved in fatty acid oxidation were also affected by the LD diet, as Acyl CoA dehydrogenase was reduced about 75%. These data indicate that a LD diet affects many aspects of metabolism that may contribute to the reduction of growth typically seen with a lysine deficiency. (Support USDA‐NRI 2004‐35206‐14160)