Delays in insulin signaling towards glucose disposal in human skeletal muscle

J Endocrinol. 2002 Mar;172(3):645-51. doi: 10.1677/joe.0.1720645.

Abstract

We explored whether the delay that occurs between a rise in plasma insulin and the increase of glucose disposal occurs before, at, or downstream of steps that are believed to be part of the insulin signaling cascade. Skeletal muscle biopsies were obtained from 16 nondiabetic subjects before, and 20 and 180 min after plasma insulin levels had been augmented in euglycemic hyperinsulinemic glucose clamps. Although plasma insulin had reached 98% of its final concentration within 10 min, insulin receptor kinase (IRK) activity, p85 associated with insulin receptor substrate-1 (IRS-1), IRS-1-associated phosphatidylinositol 3-kinase (PI3K) activity, and Thr(308)-protein kinase B (PKB) phosphorylation in the muscle biopsies at 20 min had reached only 60, 48, 34 and 47% respectively of those at 180 min. This suggests a delay before the level of IRK and little or no delay between IRK and PKB activation. The observation that glycogen synthase activity and glucose disposal at 20 min had both only reached 25% of the respective values at 180 min suggests an additional delay downstream of the investigated signaling steps.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Analysis of Variance
  • Female
  • Glucose / metabolism*
  • Glucose Clamp Technique
  • Glycogen Synthase / metabolism
  • Humans
  • Insulin / blood
  • Insulin / metabolism*
  • Insulin Receptor Substrate Proteins
  • Male
  • Middle Aged
  • Muscle, Skeletal / metabolism*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Protein Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt
  • Receptor, Insulin / metabolism
  • Signal Transduction*
  • Thorium / metabolism
  • Time Factors

Substances

  • IRS1 protein, human
  • Insulin
  • Insulin Receptor Substrate Proteins
  • Phosphoproteins
  • Proto-Oncogene Proteins
  • Thorium
  • Glycogen Synthase
  • Receptor, Insulin
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • Glucose