G. Biolo et al., Growth hormone decreases muscle glutamine production and stimulates protein synthesis in hypercatabolic patients, AM J P-ENDO, 279(2), 2000, pp. E323-E332
Citations number
38
Categorie Soggetti
Endocrinology, Nutrition & Metabolism
Journal title
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM
We determined the effects of 24-h recombinant human growth hormone (rhGH) i
nfusion into a femoral artery on leg muscle protein kinetics, amino acid tr
ansport, and glutamine metabolism in eight adult hypercatabolic trauma pati
ents. Metabolic pathways were assessed by leg arteriovenous catheterization
and muscle biopsies with the use of stable amino acid isotopes. Muscle mRN
A levels of selected enzymes were determined by competitive PCR. rhGH infus
ion significantly accelerated the inward transport rates of phenylalanine a
nd leucine and protein synthesis, whereas the muscle protein degradation ra
te and cathepsin B and UbB polyubiquitin mRNA levels were not significantly
modified by rhGH. rhGH infusion decreased the rate of glutamine de novo sy
nthesis and glutamine precursor availability, total branched-chain amino ac
id catabolism, and nonprotein glutamate utilization. Thus net glutamine rel
ease from muscle into circulation significantly decreased after rhGH admini
stration (similar to 50%), whereas glutamine synthetase mRNA levels increas
ed after rhGH infusion, possibly to compensate for reduced glutamine precur
sor availability. We conclude that, after trauma, the anticatabolic action
of rhGH is associated with a potentially harmful decrease in muscle glutami
ne production.