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Stimulation of Muscle Protein Synthesis by Glucose in Neonates Is AMP Kinase Independent
Author(s) -
Jeyapalan Asumpthia S,
Orellana Renan A,
Suryawan Agus,
Nguyen Hanh V,
Escobar Jeffery,
Frank Jason,
Davis Teresa A
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a1046-b
Subject(s) - medicine , endocrinology , ampk , postprandial , protein kinase a , insulin , amino acid , somatostatin , protein biosynthesis , amp activated protein kinase , biology , chemistry , kinase , biochemistry
Muscle protein synthesis is elevated in the neonate, in part due to an elevated response to the rise in amino acids and insulin after a meal. Recent evidence suggests that glucose may also play a role in the regulation of protein synthesis. AMP kinase has been recognized as an energy sensor and a regulator of protein synthesis. To determine whether the postprandial rise in glucose plays a role in the regulation of muscle protein synthesis in the neonate and whether this is modulated by AMP‐activated protein kinase (AMPK), we performed pancreatic substrate clamps in fasted 5–6 day old pigs. Pigs (n=4–5/group) were infused with somatostatin to block insulin secretion, glucose to achieve fasting or fed levels, insulin to achieve fasting or fed levels, while amino acids were maintained at either fasting or fed levels. Raising glucose alone to fed levels increased muscle protein synthesis by 42%. Raising glucose, amino acids, and insulin to fed levels increased muscle protein synthesis by 64%. AMPK activation did not change with any treatment. This suggests that glucose increases muscle protein synthesis in the neonate through an AMPK‐independent mechanism. Supported by NIH AR44474, USDA 58‐6250‐6‐001, and NIH AR51563