Proteomic Data in Morphine Addiction Versus Real Protein Activity: Metabolic Enzymes

J Cell Biochem. 2017 Dec;118(12):4323-4330. doi: 10.1002/jcb.26085. Epub 2017 May 25.

Abstract

Drug dependence is an escalating problem worldwide and many efforts are being made to understand the molecular basis of addiction. The morphine model is widely used in these investigations. To date, at least 29 studies exploring the influence of morphine on mammals' proteomes have been published. Among various proteins indicated as up- or down-regulated, the expression changes of enzymes engaged in energy metabolism pathways have often been confirmed. To verify whether proteomics-indicated alterations in enzyme levels reflect changes in their activity, four enzymes: PK, MDH, Complex I, and Complex V were investigated in morphine addiction and abstinence models. After analyses of the rat brain mitochondria fraction in the model of morphine dependence, we found that one of the investigated enzymes (pyruvate kinase) showed statistically significant differences observed between morphine, control, and abstinence groups. J. Cell. Biochem. 118: 4323-4330, 2017. © 2017 Wiley Periodicals, Inc.

Keywords: DATABASE; ENZYME ACTIVITY; MORPHINE; PROTEOMICS.

MeSH terms

  • Animals
  • Electron Transport Complex I / metabolism*
  • Electron Transport Complex II / metabolism*
  • Malate Dehydrogenase / metabolism*
  • Male
  • Morphine Dependence / enzymology*
  • Proteomics*
  • Pyruvate Kinase / metabolism*
  • Rats
  • Rats, Wistar

Substances

  • Malate Dehydrogenase
  • Electron Transport Complex II
  • Pyruvate Kinase
  • Electron Transport Complex I