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This Article Full Text Full Text (PDF) All Versions of this Article: 288/3/E564    most recent 00198.2004v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (1) Citing Articles via Google Scholar Google Scholar Articles by Clowes, E. J. Articles by Baracos, V. E. Search for Related Content PubMed PubMed Citation Articles by Clowes, E. J. Articles by Baracos, V. E.

Skeletal muscle protein mobilization during the progression of lactation

Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada

Submitted 5 May 2004 ; accepted in final form 19 October 2004

To investigate changes in muscle metabolism during lactation, serial biopsy of the triceps brachii was conducted in first-parity sows subjected to three degrees of selective protein mobilization through restriction of dietary protein intake (see Clowes EJ, Aherne FX, Foxcroft GR, and Baracos VE. J Anim Sci 81: 753–764, 2003). Muscle biopsies were taken 7 days before parturition and at 12 and 23 days of lactation. The following changes occurred after parturition, were progressive, and were significantly magnified in animals under the greatest degree of dietary protein restriction and hence of protein mobilization. Decreased RNA-to-DNA ratio (capacity for protein synthesis) was observed. The presence of increased expression of several elements of the ubiquitin proteasome proteolytic pathway suggested a robust catabolic response. However, as lactation progressed, and especially under conditions of increased dietary protein restriction, protein mobilization increased, muscle RNA-to-DNA ratio fell further, protease gene expression continued to rise, tissue free glutamine levels rose dramatically, and essential amino acid levels, especially branched-chain amino acids and threonine, fell to below prepartum levels.

ATP-ubiquitin proteasome proteolytic pathway; muscle free amino acids; muscle RNA, DNA, and protein concentration

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