PMID- 23431444
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20130225
LR  - 20240324
IS  - 2090-2166 (Print)
IS  - 2090-2174 (Electronic)
IS  - 2090-2166 (Linking)
VI  - 2013
DP  - 2013
TI  - An Internal Standard-Assisted Synthesis and Degradation Proteomic Approach 
      Reveals the Potential Linkage between VPS4B Depletion and Activation of Fatty 
      Acid beta-Oxidation in Breast Cancer Cells.
PG  - 291415
LID - 10.1155/2013/291415 [doi]
LID - 291415
AB  - The endosomal/lysosomal system, in particular the endosomal sorting complexes 
      required for transport (ESCRTs), plays an essential role in regulating the 
      trafficking and destination of endocytosed receptors and their associated 
      signaling molecules. Recently, we have shown that dysfunction and down-regulation 
      of vacuolar protein sorting 4B (VPS4B), an ESCRT-III associated protein, under 
      hypoxic conditions can lead to the abnormal accumulation of epidermal growth 
      factor receptor (EGFR) and aberrant EGFR signaling in breast cancer. However, the 
      pathophysiological consequences of VPS4B dysfunction remain largely elusive. In 
      this study, we used an internal standard-assisted synthesis and degradation mass 
      spectrometry (iSDMS) method, which permits the direct measurement of protein 
      synthesis, degradation and protein dynamic expression, to address the effects of 
      VPS4B dysfunction in altering EGF-mediated protein expression. Our initial 
      results indicate that VPS4B down-regulation decreases the expression of many 
      proteins involved in glycolytic pathways, while increased the expression of 
      proteins with roles in mitochondrial fatty acid beta-oxidation were up-regulated in 
      VPS4B-depleted cells. This observation is also consistent with our previous 
      finding that hypoxia can induce VPS4B down-regulated, suggesting that the 
      adoption of fatty acid beta-oxidation could potentially serve as an alternative 
      energy source and survival mechanism for breast cancer cells in response to 
      hypoxia-mediated VPS4B dysfunction.
FAU - Liao, Zhongping
AU  - Liao Z
AD  - Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, 
      MD 21201, USA.
FAU - Thomas, Stefani N
AU  - Thomas SN
FAU - Wan, Yunhu
AU  - Wan Y
FAU - Lin, H Helen
AU  - Lin HH
FAU - Ann, David K
AU  - Ann DK
FAU - Yang, Austin J
AU  - Yang AJ
LA  - eng
GR  - R01 AG025323/AG/NIA NIH HHS/United States
GR  - R01 DE010742/DE/NIDCR NIH HHS/United States
GR  - R01 DE014183/DE/NIDCR NIH HHS/United States
PT  - Journal Article
DEP - 20130204
PL  - Egypt
TA  - Int J Proteomics
JT  - International journal of proteomics
JID - 101538205
PMC - PMC3575666
EDAT- 2013/02/23 06:00
MHDA- 2013/02/23 06:01
PMCR- 2013/02/04
CRDT- 2013/02/23 06:00
PHST- 2012/09/14 00:00 [received]
PHST- 2012/12/12 00:00 [accepted]
PHST- 2013/02/23 06:00 [entrez]
PHST- 2013/02/23 06:00 [pubmed]
PHST- 2013/02/23 06:01 [medline]
PHST- 2013/02/04 00:00 [pmc-release]
AID - 10.1155/2013/291415 [doi]
PST - ppublish
SO  - Int J Proteomics. 2013;2013:291415. doi: 10.1155/2013/291415. Epub 2013 Feb 4.