Insulin-mediated reduction of whole body protein breakdown. Dose-response effects on leucine metabolism in postabsorptive men. 1985

N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young

In vivo effects of insulin on plasma leucine and alanine kinetics were determined in healthy postabsorptive young men (n = 5) employing 360-min primed, constant infusions of L-[1-13C]leucine and L-[15N]alanine during separate single rate euglycemic insulin infusions. Serum insulin concentrations of 16.4 +/- 0.8, 29.1 +/- 2.7, 75.3 +/- 5.0, and 2,407 +/- 56 microU/ml were achieved. Changes in plasma 3-methyl-histidine (3-MeHis) were obtained as an independent qualitative indicator of insulin-mediated reduction in proteolysis. Hepatic glucose output was evaluated at the lowest insulin level using D-[6,6-2H2]glucose. The data demonstrate a dose-response effect of insulin to reduce leucine flux, from basal values of 77 +/- 1 to 70 +/- 2, 64 +/- 3, 57 +/- 3, and 52 +/- 4 mumol(kg X h)-1 at the 16, 29, 75, and 2,407 microU/ml insulin levels, respectively (P less than 0.01). A parallel, progressive reduction in 3-MeHis from 5.8 +/- 0.3 to 4.3 +/- 0.3 microM was revealed. Leucine oxidation estimated from the 13C-enrichment of expired CO2 and plasma leucine (12 +/- 1 mumol[kg X h]-1) and from the 13C-enrichment of CO2 and plasma alpha-ketoisocaproate (19 +/- 2 mumol[kg X h]-1) increased at the 16 microU/ml insulin level to 16 +/- 1 and 24 +/- 2 mumol(kg X h)-1, respectively (P less than 0.05 for each), but did not increase at higher insulin levels. Alanine flux (206 +/- 13 mumol(kg X h)-1) did not increase during the clamp, but alanine de novo synthesis increased in all studies from basal rates of 150 +/- 13 to 168 +/- 23, 185 +/- 21, 213 +/- 29, and 187 +/- 15 mumol(kg X h)-1 at 16, 29, 75, and 2,407 microU/ml insulin levels, respectively (P less than 0.05). These data indicate the presence of insulin-dependent suppression of leucine entry into the plasma compartment in man secondary to a reduction in proteolysis and the stimulation of alanine synthesis during euglycemic hyperinsulinemia.

UI MeSH Term Description Entries
D007328 Insulin A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1). Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin
D007930 Leucine An essential branched-chain amino acid important for hemoglobin formation. L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
D008297 Male Males
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D005947 Glucose A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement. Dextrose,Anhydrous Dextrose,D-Glucose,Glucose Monohydrate,Glucose, (DL)-Isomer,Glucose, (alpha-D)-Isomer,Glucose, (beta-D)-Isomer,D Glucose,Dextrose, Anhydrous,Monohydrate, Glucose
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000328 Adult A person having attained full growth or maturity. Adults are of 19 through 44 years of age. For a person between 19 and 24 years of age, YOUNG ADULT is available. Adults
D000409 Alanine A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM. Abufène,Alanine, L-Isomer,L-Alanine,Alanine, L Isomer,L Alanine,L-Isomer Alanine
D000597 Amino Acids, Branched-Chain Amino acids which have a branched carbon chain. Branched-Chain Amino Acid,Amino Acids, Branched Chain,Acid, Branched-Chain Amino,Acids, Branched-Chain Amino,Amino Acid, Branched-Chain,Branched Chain Amino Acid,Branched-Chain Amino Acids

Related Publications

N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
June 1981, The American journal of physiology,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
June 1997, The American journal of physiology,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
July 1990, The American journal of physiology,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
November 1987, The British journal of nutrition,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
August 2003, The Journal of clinical endocrinology and metabolism,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
September 1986, The American journal of physiology,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
April 1994, The Journal of clinical investigation,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
January 1985, The British journal of nutrition,
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
September 1988, Clinical science (London, England : 1979),
N K Fukagawa, and K L Minaker, and J W Rowe, and M N Goodman, and D E Matthews, and D M Bier, and V R Young
December 2012, The Journal of clinical endocrinology and metabolism,
Copied contents to your clipboard!