Profiling of the soluble proteome in rat hippocampus post propofol anesthesia.

The current study was designed to initially observe the changes in soluble proteome in rat hippocampus post anesthesia, trying to explore possible clues for elucidating the effects of propofol. Soluble proteins were separated by 2-dimensional electrophoresis (2-DE). Their expressions were observed at 1, 6, 24 h and 7 days after 3 h of propofol anesthesia. Spots exhibiting significant changes among different time-points were submitted to matrix-assisted laser desorption/ionization time of flight mass spectrometer (MALDI-TOF MS) assay and peptide mass fingerprinting identification. The expression changes of selected proteins were further assayed using Western blot and RT-PCR. Twenty-six differentially expressed proteins were found and 19 were successfully identified with MALDI-TOF MS. Gene ontology analysis revealed these identified proteins were mainly cytosol (5) and/or cytoskeleton fractions (5). According to biological processes category, 9 proteins take part in development process, 12 are involved in metabolic process and 6 in regulatory function. Functionally, 17 proteins were involved in binding activities among which 12 possessed catalytic activities. Most changes took place within 24 h. Change patterns of selected proteins were identical in 2-DE and Western blot. Three mRNA of 5 selected proteins exhibited similar change patterns with those of their protein expressions. Soluble proteome in rat hippocampus are dynamically affected by propofol, with multiple processes being involved. They are possible explanations for propofol effects but further investigations are required.