Liver and skeletal muscle mitochondria proteomes are altered in pigs divergently selected for residual feed intake1,2
Author(s) -
J. K. Grubbs,
E. HuffLonergan,
Nicholas K Gabler,
Jack C. M. Dekkers,
Steven M. Lonergan
Publication year - 2014
Publication title -
journal of animal science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.928
H-Index - 156
eISSN - 1525-3015
pISSN - 0021-8812
DOI - 10.2527/jas.2013-7391
Subject(s) - mitochondrion , biology , hsp70 , heat shock protein , residual feed intake , proteome , proteomics , protein subunit , phenotype , biochemistry , feed conversion ratio , endocrinology , gene , body weight
Animals selected for residual feed intake (RFI) can be used as a model to elucidate molecular explanations for differences in growth efficiency. The objective of this study was to determine the extent to which the protein profile and posttranslational modifications of mitochondria from skeletal muscle and liver relate to feed efficiency gains in pigs divergently selected for RFI. Mitochondria were isolated from the longissimus dorsi (LD) muscle and the liver from pigs (n = 9 each for the high and low RFI line; BW = 95.8 kg). Mitochondria protein profile differences were determined using two-dimensional difference in gel electrophoresis. Proteins were identified using electrospray ionization mass spectrometry. In the line comparison, the β subunit of ATP synthase, heat shock protein (HSP) 60, and HSP70, were identified as being increased in mitochondria from the liver of the low RFI line (23 to 50%; P < 0.1). These differences were not observed in the other comparisons. In the LD, proteins identified as being different between RFI phenotypes included HSP70 and subunit 1 of the cytochrome bc1 complex. These data indicate that genetic selection for RFI tends to result in a consistent change in mitochondrial protein profile. In contrast, classification by phenotype demonstrates that phenotypic differences in RFI are not specifically associated with alterations of the mitochondria protein profile.
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