Transduced human copper chaperone for Cu,Zn-SOD (PEP-1-CCS) protects against neuronal cell death

Mol Cells. 2005 Dec 31;20(3):401-8.

Abstract

Reactive oxygen species (ROS) contribute to the development of various human diseases. Cu,Zn-superoxide dismutase (SOD) is one of the major means by which cells counteract the deleterious effects of ROS. SOD activity is dependent upon bound copper ions supplied by its partner metallochaperone protein, copper chaperone for SOD (CCS). In the present study, we investigated the protective effects of PEP-1-CCS against neuronal cell death and ischemic insults. When PEP-1-CCS was added to the culture medium of neuronal cells, it rapidly entered the cells and protected them against paraquat-induced cell death. Moreover, transduced PEP-1-CCS markedly increased endogenous SOD activity in the cells. Immunohistochemical analysis revealed that it prevented neuronal cell death in the hippocampus in response to transient forebrain ischemia. These results suggest that CCS is essential to activate SOD, and that transduction of PEP-1-CCS provides a potential strategy for therapeutic delivery in various human diseases including stroke related to SOD or ROS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Astrocytes / metabolism
  • Brain Ischemia / chemically induced
  • Brain Ischemia / metabolism
  • Brain Ischemia / pathology
  • Cell Death / drug effects
  • Copper / metabolism*
  • Gerbillinae
  • Hippocampus / drug effects
  • Humans
  • Immunoenzyme Techniques
  • Male
  • Molecular Chaperones / therapeutic use*
  • Neurons / drug effects*
  • Neurons / metabolism
  • Oxidative Stress / physiology
  • Paraquat / toxicity
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Fusion Proteins / therapeutic use
  • Transfection

Substances

  • CCS protein, human
  • Molecular Chaperones
  • Recombinant Fusion Proteins
  • Copper
  • Paraquat