PMID- 20227452
OWN - NLM
STAT- MEDLINE
DCOM- 20101129
LR  - 20151119
IS  - 1872-9754 (Electronic)
IS  - 0197-0186 (Linking)
VI  - 56
IP  - 8
DP  - 2010 Jul
TI  - A long hangover from party drugs: residual proteomic changes in the hippocampus 
      of rats 8 weeks after gamma-hydroxybutyrate (GHB), 3,4-methylenedioxymethamphetamine 
      (MDMA) or their combination.
PG  - 871-7
LID - 10.1016/j.neuint.2010.03.002 [doi]
AB  - 3,4-Methylenedioxymethamphetamine (MDMA) and gamma-hydroxybutyrate (GHB) are 
      popular party drugs that are used for their euphoric and prosocial effects, and 
      sometimes in combination. Both drugs increase markers of oxidative stress in the 
      hippocampus and can cause lasting impairments in hippocampal-dependent forms of 
      memory. To gain further information on the biochemical mechanisms underlying 
      these effects, the current study examined residual changes in hippocampal protein 
      expression measured 8 weeks after chronic administration of GHB (500mg/kg), MDMA 
      (5mg/kg) or their combination (GHB/MDMA). The drugs were administered once a day 
      for 10 days in an environment with an elevated ambient temperature of 28 degrees 
      C. Results showed significant changes in protein expression, relative to 
      controls, in all three groups: MDMA and GHB given alone caused residual changes 
      in 8 and 5 proteins respectively, while the GHB/MDMA combination significantly 
      changed 6 proteins. The altered proteins had roles in neuroplasticity, 
      neuroprotection, intracellular signalling and cytoskeletal function. The largest 
      change (-4.3-fold) was seen in the MDMA group with the protein C-crk: a protein 
      implicated in learning-related neuroplasticity. The second largest change 
      (3.0-fold) was seen in the GHB group in Glutathione-S-transferase (GST), a 
      protein that protects against oxidative stress. Two cytoskeletal proteins 
      (Tubulin Folding Cofactor B and Tropomyosin-alpha-3 chain) and one plasticity 
      related protein (Neuronal Pentraxin-1 NP1) were similarly changed in both the 
      MDMA and the GHB groups, while two intracellular signalling proteins 
      (alpha-soluble NSF-attachment protein and subunits of the V-type proton ATPase) 
      were changed in both the MDMA/GHB and the MDMA groups. These results provide some 
      insight into the molecular pathways possibly underlying the lasting cognitive 
      deficits arising from GHB and/or MDMA use.
CI  - 2010. Published by Elsevier Ltd.
FAU - van Nieuwenhuijzen, Petra S
AU  - van Nieuwenhuijzen PS
AD  - School of Psychology, University of Sydney, Camperdown, Sydney, NSW 2006, 
      Australia.
FAU - Kashem, Mohammed A
AU  - Kashem MA
FAU - Matsumoto, Izuru
AU  - Matsumoto I
FAU - Hunt, Glenn E
AU  - Hunt GE
FAU - McGregor, Iain S
AU  - McGregor IS
LA  - eng
PT  - Journal Article
DEP - 20100319
PL  - England
TA  - Neurochem Int
JT  - Neurochemistry international
JID - 8006959
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Pharmaceutical Vehicles)
RN  - 7G33012534 (Sodium Oxybate)
RN  - KE1SEN21RM (N-Methyl-3,4-methylenedioxyamphetamine)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Drug Synergism
MH  - Electrophoresis, Gel, Two-Dimensional
MH  - Hippocampus/*drug effects/*metabolism/physiopathology
MH  - Male
MH  - N-Methyl-3,4-methylenedioxyamphetamine/administration & dosage/*toxicity
MH  - Nerve Tissue Proteins/biosynthesis/*metabolism
MH  - Pharmaceutical Vehicles/administration & dosage
MH  - Proteomics/*methods
MH  - Rats
MH  - Rats, Wistar
MH  - Signal Transduction/drug effects/physiology
MH  - Sodium Oxybate/administration & dosage/*toxicity
MH  - Time Factors
MH  - Up-Regulation/drug effects
EDAT- 2010/03/17 06:00
MHDA- 2010/12/14 06:00
CRDT- 2010/03/16 06:00
PHST- 2010/02/15 00:00 [received]
PHST- 2010/03/05 00:00 [accepted]
PHST- 2010/03/16 06:00 [entrez]
PHST- 2010/03/17 06:00 [pubmed]
PHST- 2010/12/14 06:00 [medline]
AID - S0197-0186(10)00088-4 [pii]
AID - 10.1016/j.neuint.2010.03.002 [doi]
PST - ppublish
SO  - Neurochem Int. 2010 Jul;56(8):871-7. doi: 10.1016/j.neuint.2010.03.002. Epub 2010 
      Mar 19.