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Metabolism Unit, Shriners Burns Institute and Departments of Surgery and Anesthesiology, The University of Texas Medical Branch, Galveston, Texas 77550
We have measured
skin and muscle protein kinetics and amino acid (AA) transport in
anesthetized rabbits during 1) 64-h
fast, 2) AA infusion,
3) AA plus fat emulsion infusion,
and 4) AA plus hyperinsulinemia.
L-[ring-13C6]phenylalanine
was infused as the tracer, and the ear and hindlimb were used as
arteriovenous units to reflect skin and muscle protein kinetics,
respectively. Skin protein net balance was not different from zero in
all groups, indicating a maintenance of protein mass. In contrast, the
muscle net balance differed over a range from
1.6 ± 0.6 after fasting to 0.2 ± 0.2 µmol · 100 g
1 · h
1
during hyperinsulinemia. In the skin, 59-66% of intracellular free phenylalanine came from proteolysis, and phenylalanine
availability from proteolysis was positively correlated to the protein
synthesis rate. In conclusion, normal skin maintains its constant
protein mass by efficient reutilization of AAs from proteolysis. In
contrast to muscle, skin protein is relatively insensitive to control
by nutritional and hormonal factors. Because of the metabolic
differences, when limb models are used for muscle protein metabolism,
the potential contribution by limb skin should be considered.
stable isotopes; mass spectrometry; arteriovenous balance; rabbits
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