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Muscle Protein Synthesis Measured by Stable Isotope Techniques in Man: The Effects of Feeding and Fasting
Abstract
1. Measurements have been made of whole-body and skeletal muscle protein synthesis in fed and fasted adults with l-[1-13C]leucine. 2. The marked increase in whole-body synthesis on feeding largely reflects the changes in protein synthesis in muscle, which doubles on feeding, compared with a 40% increase in that of the rest of the body. 3. Skeletal muscle in fed man contributes more than half to total protein synthesis occurring in the whole body.
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“Administration of mixed amino acids (1) or dietary protein (2) increases skeletal muscle protein synthesis (MPS) rates in a dosedependent manner (3, 4) through activation of the mammalian target of rapamycin (mTOR) complex-1 (mTORC1) in vivo in humans (5).”
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Metadata
- Authors
- Rennie, M. J., Edwards, R. H. T., Halliday, D., Matthews, D. E., Wolman, S. L., & Millward, D. J.
- Venue
- Clinical Science
- Publisher
- Portland Press Ltd.
- Published
- 1982-12-01
- Volume
- 63
- Issue
- 6
- Pages
- 519-523
- ISSN
- 0143-5221 (ISSN-L)
- 1470-8736
- OpenAlex
- W71156707
- Cited by
- 455
- References
- 0
- FWCI
- 6.33
- Type
- journal article
- Language
- en
- Open access
- closed
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