A quantitative proteomic analysis of long-term memory

Mol Brain. 2010 Mar 23;3:9. doi: 10.1186/1756-6606-3-9.

Abstract

Background: Memory is the ability to store, retain, and later retrieve learned information. Long-term memory (LTM) formation requires: DNA transcription, RNA translation, and the trafficking of newly synthesized proteins. Several components of these processes have already been identified. However, due to the complexity of the memory formation process, there likely remain many yet to be identified proteins involved in memory formation and persistence.

Results: Here we use a quantitative proteomic method to identify novel memory-associated proteins in neural tissue taken from animals that were trained in vivo to form a long-term memory. We identified 8 proteins that were significantly up-regulated, and 13 that were significantly down-regulated in the LTM trained animals as compared to two different control groups. In addition we found 19 proteins unique to the trained animals, and 12 unique proteins found only in the control animals.

Conclusions: These results both confirm the involvement of previously identified memory proteins such as: protein kinase C (PKC), adenylate cyclase (AC), and proteins in the mitogen-activated protein kinase (MAPK) pathway. In addition these results provide novel protein candidates (e.g. UHRF1 binding protein) on which to base future studies.

MeSH terms

  • Adenylyl Cyclases / metabolism
  • Animals
  • Blotting, Western
  • Central Nervous System / anatomy & histology
  • Chromatography, Liquid
  • Down-Regulation
  • Lymnaea / enzymology
  • Lymnaea / physiology*
  • Mass Spectrometry
  • Memory / physiology*
  • Proteomics* / methods
  • Up-Regulation

Substances

  • Adenylyl Cyclases
  • adenylyl cyclase 8