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1 Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen, Scotland, AB21 9SB
2 Department of Agriculture, University of Reading, Reading, England, RG6 2AT
Milk protein responses to protein nutrition are typically poor and, in part, may be due to the low efficiency (
25 to 30%) of converting dietary N into milk. Posthepatic availability of amino acids (AA) is not limited, yet only 30% is converted into milk. The poor capture of AA by the mammary gland may relate to the imbalanced and uncoordinated timing of nutrient delivery to the gland. The infusion of essential AA improves the efficiency of utilization (0.31); however, further catabolism of AA within the mammary gland suggests that AA transport is not a major limitation. These losses may serve ancillary or functional roles, but mammary oxidation of some AA occurs only when AA extraction exceeds the stoichiometric requirements for milk protein synthesis. Intracellular substrate supply may be more limiting than is the appartus for protein synthesis. Studies utilizing isotope labeling and conducted in vitro and in vivo now suggest that circulating peptides and proteins can serve as sources of perhaps all AA for casein synthesis, but the source of these remains elusive. Constitutive protein and casein turnover contribute significantly (42 to 72%) to mammary protein synthesis. All AA are extensively channeled through an intermediary protein pool or pools that have rapid turnover rates. The AA are then incorporated into casein, which appears to be fixed in association with protein turnover. The mammary gland is a major controller of its metabolism, and the mechanisms of AA extraction and conversion into milk protein are linked to secretion events. Blood flow may be a key point of regulation whereby mechanisms sense and respond to nutrient supply and balance to the gland via alterations in hemodynamics.
Key Words: amino acid • mammary gland • casein • lactation
Submitted on August 20, 1997
Accepted on March 23, 1998
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