Factors Controlling Intracellular Breakdown of Proteins

Mayer, R. John; Burgess, Rowland J.; Russell, S M

doi:10.1016/b978-0-408-10676-4.50007-0

Cited by 4 publications

(2 citation statements)

References 97 publications

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“…In so far as the latter proposal is based on A V determinations of amino acids in plasma samples before and after deproteinization, it depends on the assumption of complete deproteinization, which needs to be fully substantiated. A further dimension to the problem of identifying milk protein precursors is added by the claim that there is substantial intracellular degradation of protein prior to secretion (Mayer et al, 1980;Oddy et al, 1988). Despite the possible contribution of other sources, it remains likely that plasma free amino acids are usually the principal precursors of mammary-synthesized milk proteins: in some cases over 70% of an amino acid perfusing the gland is extracted from the blood plasma (see Mepham, 1982).…”

Section: Provisioning the Mammary Glands 1131mentioning

confidence: 98%

Physiology and Biochemistry of Lactation

Mepham¹,

Kuhn²

1994

Marshall’s Physiology of Reproduction

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Section: Provisioning the Mammary Glands 1131mentioning

confidence: 98%

Physiology and Biochemistry of Lactation

Mepham¹,

Kuhn²

1994

Marshall’s Physiology of Reproduction

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“…30, No. 3,1984 deposition (growth) in animals (13) . It has also been suggested that in smaller animals, protein synthesis in liver contributes the greater part to whole-body protein synthesis, but in muscle a smaller part (14).…”

Section: Discussionmentioning

confidence: 99%

The concerted effects of thyroid function and dietary protein on growth and protein metabolism in mice at different growth stages.

Hayashi

Akiba

Tomita

et al. 1984

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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Gene Expression of Muscle-Specific Ubiquitin Ligase, Atrogin-1/MAFbx, Positively Correlates with Skeletal Muscle Proteolysis in Food-Deprived Broiler Chickens

et al. 2011

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A relationship between skeletal muscle proteolysis and mRNA expression of atrogin-/MAFbx, a muscle-specific ubiquitin ligase, was examined in food-deprived broiler chickens. In response to food deprivation for and h, body and muscle weights decreased in a time-dependent manner. Muscle free N -methylhistidine content, an index of myofibrillar proteolysis, was . -fold and . -fold greater than that of fed controls following and h of food deprivation, respectively. Gene expression of atrogin-/MAFbx drastically increased in response to food deprivation in a time-dependent manner. At h of food deprivation, the induction of atrogin-/MAFbx mRNA expression level elevated up to -fold greater than that of fed controls. By contrast, mRNA expression levels of S proteasome C and C subunits tended to decrease with time. No significant di erence was seen in the change of ubiquitin mRNA expression. A highly significant linear negative relationship (r . , . ) was found between atrogin-/MAFbx expression and muscle mass, while a highly significant linear positive relationship (r . , . ) was found between atrogin-/MAFbx expression and muscle free N -methylhistidine content. These results indicate that atrogin-/MAFbx plays a critical role in the development of muscle proteolysis and its gene expression is a reliable index of muscle proteolysis in broiler chickens.: atrogin-/MAFbx, broiler chicken, food deprivation, myofibrillar proteolysis, skeletal muscle mass an increase in the overall rate of muscle protein breakdown leading to a rapid loss of muscle mass and myoSkeletal muscle mass is determined by the di erence fibrillar protein (Jagoe ). Enhancement of between the amount of protein synthesized and the overall proteolysis in atrophying muscles results mainly amount of protein degraded (Waterlow ). If from a general activation of the ubiquitin-proteasome the balance between synthesis and degradation changes pathway (UPP) (Lecker ). Among the UPP into catabolic state, muscle protein content decreases, components, atrogin-/MAFbx, a muscle-specific ubiqresulting in less muscle mass or muscle wasting (Mayer uitin ligase, plays a key role in the initiation and develop-) a cause of decreased productivity in broiler ment of muscle atrophy (Bodine ; Gomes farms. E orts are needed to prevent the loss of accu-). The atrogin-/MAFbx gene is rapidly induced mulated muscle protein as well as to increase the amount early on during the atrophy process, and a rise in its of muscle protein for the broiler production industry.expression precedes the loss of muscle weight (Gomes Muscle protein serves as a primary reserve of amino ). Atrogin-/MAFbx mRNA has been shown to acids that can be mobilized upon fasting and disease to linearly and positively correlate with the overall rate of provide a source of amino acids for hepatic gluconeprotein breakdown, as measured by the release of radioogenesis and energy production (Mitch and Goldberg, labeled tyrosine in glucocorticoid-treated C C myotube ). An important physiological adaptation to fasting is cell...

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Factors Controlling Intracellular Breakdown of Proteins

Cited by 4 publications

References 97 publications

Physiology and Biochemistry of Lactation

Physiology and Biochemistry of Lactation

The concerted effects of thyroid function and dietary protein on growth and protein metabolism in mice at different growth stages.

Gene Expression of Muscle-Specific Ubiquitin Ligase, Atrogin-1/MAFbx, Positively Correlates with Skeletal Muscle Proteolysis in Food-Deprived Broiler Chickens

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