Diabetes alters contraction-induced mitogen activated protein kinase activation in the rat soleus and plantaris

Exp Diabetes Res. 2008:2008:738101. doi: 10.1155/2008/738101.

Abstract

The prescription of anaerobic exercise has recently been advocated for the management of diabetes; however exercise-induced signaling in diabetic muscle remains largely unexplored. Evidence from exercise studies in nondiabetics suggests that the extracellular-signal-regulated kinases (Erk1/2), p38, and c-JUN NH2-terminal kinase (Jnk) mitogen-activated protein kinases (MAPKs) are important regulators of muscle adaptation. Here, we compare the basal and the in situ contraction-induced phosphorylation of Erk1/2- p38- and Jnk-MAPK and their downstream targets (p90rsk and MAPKAP-K2) in the plantaris and soleus muscles of normal and obese (fa/fa) Zucker rats. Compared to lean animals, the time course and magnitude of Erk1/2, p90rsk and p38 phosphorylation to a single bout of contractile stimuli were greater in the plantaris of obese animals. Jnk phosphorylation in response to contractile stimuli was muscle-type dependent with greater increases in the plantaris than the soleus. These results suggest that diabetes alters intramuscular signaling processes in response to a contractile stimulus.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Diabetes Mellitus / enzymology
  • Diabetes Mellitus / pathology*
  • Diabetes Mellitus, Experimental / enzymology
  • Diabetes Mellitus, Experimental / pathology*
  • Gene Expression Regulation, Enzymologic*
  • MAP Kinase Signaling System*
  • Male
  • Muscle Contraction*
  • Muscle, Skeletal / metabolism*
  • Muscle, Skeletal / pathology*
  • Phosphorylation
  • Physical Conditioning, Animal
  • Rats
  • Rats, Zucker
  • Signal Transduction