Activation of stress-activated protein kinases correlates with neurite outgrowth induced by protease inhibition in PC12 cells

J Neurochem. 1999 Mar;72(3):1081-7. doi: 10.1046/j.1471-4159.1999.0721081.x.

Abstract

PC12 cells are well characterized for their ability to differentiate into neuronal-like cells when challenged with nerve growth factor. It has been reported that the calpain and proteasome inhibitor N-acetyl-Leu-Leu-norleucinal (CI) is also able to induce neurite outgrowth in PC12 cells. In this study, we report that the inhibitor of proteasomal chymotrypsin-like activity, carbobenzoxy-Ile-Glu-(O-tert-butyl)-Ala-Leu-aldehyde (PSI), can also induce differentiation of PC12 cells. Induction of neurite outgrowth with PSI, CI, or its close analogue, carbobenzoxy-Leu-Leu-leucinal (MG132), was associated with stress-activated protein kinase (SAPK) activation. Neurite formation induced by protease inhibition was independent of mitogen-activated protein kinase/extracellular signal-regulated kinase, p38/reactivating kinase, or phosphatidylinositol 3-kinase activities. The exact mechanism by which protease inhibition activates SAPKs remains to be elucidated; however, our results suggest that the SAPK signal transduction cascade may be an alternative and/or parallel pathway in the regulation of neuronal differentiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Cell Differentiation / drug effects
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Activation / physiology
  • Leupeptins / pharmacology
  • Mitogen-Activated Protein Kinase 12
  • Mitogen-Activated Protein Kinases*
  • Neurites / drug effects*
  • Neurites / enzymology
  • PC12 Cells
  • Phosphatidylinositol 3-Kinases / metabolism
  • Precipitin Tests
  • Protease Inhibitors / pharmacology*
  • Protein Kinase Inhibitors
  • Protein Kinases / metabolism*
  • Rats
  • Signal Transduction / drug effects
  • Signal Transduction / physiology
  • p38 Mitogen-Activated Protein Kinases

Substances

  • Leupeptins
  • Protease Inhibitors
  • Protein Kinase Inhibitors
  • Protein Kinases
  • Mitogen-Activated Protein Kinase 12
  • Phosphatidylinositol 3-Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde