PMID- 17330943
OWN - NLM
STAT- MEDLINE
DCOM- 20070606
LR  - 20071203
IS  - 1535-3893 (Print)
IS  - 1535-3893 (Linking)
VI  - 6
IP  - 3
DP  - 2007 Mar
TI  - BDNF induces widespread changes in synaptic protein content and up-regulates 
      components of the translation machinery: an analysis using high-throughput 
      proteomics.
PG  - 1059-71
AB  - The brain-derived neurotrophic factor (BDNF) plays an important role in neuronal 
      development, and in the formation and plasticity of synaptic connections. These 
      effects of BDNF are at least partially due to the ability of the neurotrophin to 
      increase protein synthesis both globally and locally. However, only a few 
      proteins have been shown to be up-regulated at the synapse by BDNF. Using 
      multidimensional protein identification technology (MudPIT) and relative 
      quantification by spectra counting, we found that several hundred proteins are 
      up-regulated in a synaptoneurosome preparation derived from cultured cortical 
      neurons that were treated with BDNF. These proteins fall into diverse functional 
      categories, including those involved in synaptic vesicle formation and movement, 
      maintenance or remodeling of synaptic structure, mRNA processing, transcription, 
      and translation. A number of translation factors, ribosomal proteins, and tRNA 
      synthetases were rapidly up-regulated by BDNF. This up-regulation of translation 
      components was sensitive to protein synthesis inhibitors and dependent on the 
      activation of the mammalian target of rapamycin (mTOR), a regulator of 
      cap-dependent mRNA translation. The presence of a subset of these proteins and 
      their mRNAs in neuronal processes was corroborated by immunocytochemistry and in 
      situ hybridization, and their up-regulation was confirmed by Western blotting. 
      The data demonstrate that BDNF increases the synthesis of a wide variety of 
      synaptic proteins and suggest that the neurotrophin may enhance the translational 
      capacity of synapses.
FAU - Liao, Lujian
AU  - Liao L
AD  - Departments of Cell Biology and Neurobiology, The Scripps Research Institute, 
      10550 North Torrey Pines Road, La Jolla, California 92037, USA.
FAU - Pilotte, Julie
AU  - Pilotte J
FAU - Xu, Tao
AU  - Xu T
FAU - Wong, Catherine C L
AU  - Wong CC
FAU - Edelman, Gerald M
AU  - Edelman GM
FAU - Vanderklish, Peter
AU  - Vanderklish P
FAU - Yates, John R 3rd
AU  - Yates JR 3rd
LA  - eng
GR  - 5R01MH067880/MH/NIMH NIH HHS/United States
GR  - P41RR11823-10/RR/NCRR NIH HHS/United States
GR  - U01DE016267-03/DE/NIDCR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Proteome Res
JT  - Journal of proteome research
JID - 101128775
RN  - 0 (Brain-Derived Neurotrophic Factor)
RN  - 0 (Nerve Growth Factors)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (RNA, Messenger)
SB  - IM
MH  - Animals
MH  - Brain-Derived Neurotrophic Factor/*physiology
MH  - Cells, Cultured
MH  - Nerve Growth Factors/physiology
MH  - Nerve Tissue Proteins/*analysis/genetics
MH  - Neurons/*cytology
MH  - Protein Biosynthesis
MH  - Proteomics/*methods
MH  - RNA, Messenger/analysis
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Synapses/*chemistry/metabolism
MH  - *Up-Regulation
EDAT- 2007/03/03 09:00
MHDA- 2007/06/07 09:00
CRDT- 2007/03/03 09:00
PHST- 2007/03/03 09:00 [pubmed]
PHST- 2007/06/07 09:00 [medline]
PHST- 2007/03/03 09:00 [entrez]
AID - 10.1021/pr060358f [doi]
PST - ppublish
SO  - J Proteome Res. 2007 Mar;6(3):1059-71. doi: 10.1021/pr060358f.