PMID- 11001323
OWN - NLM
STAT- MEDLINE
DCOM- 20010208
LR  - 20061115
IS  - 0173-0835 (Print)
IS  - 0173-0835 (Linking)
VI  - 21
IP  - 14
DP  - 2000 Aug
TI  - Identification of differentially expressed proteins between human hepatoma and 
      normal liver cell lines by two-dimensional electrophoresis and liquid 
      chromatography-ion trap mass spectrometry.
PG  - 3058-68
AB  - In the previous study, the proteomes of the human hepatoma cell line BEL-7404 and 
      the normal human liver cell line L-02 were separated by high resolution 
      two-dimensional electrophoresis (2-DE). Image analysis revealed that 99 protein 
      spots showed quantitative and qualitative variations that were significant (P < 
      0.01) and reproducible. Here we report the identification results of some of 
      these protein spots. Protein spots excised from 2-D gels were subjected to in-gel 
      digestion with trypsin, and the resulting peptides were measured by microbore 
      high performance liquid chromatography - ion trap - mass spectrometry (LC-IT-MS) 
      to obtain the tandem mass (MS/MS) spectra. Twelve protein spots were identified 
      with high confidence using SEQUEST with uninterpreted MS/MS raw data. Besides 
      inosine-5'-monophosphate dehydrogenase 2, heat shock 27 kDa protein, calreticulin 
      and calmodulin, whose expression was elevated in hepatoma cells, 
      glutathione-S-transferase P was identified from hepatoma cells in which its level 
      was 18-fold higher compared to human liver cells. Two spots were identified as 
      the homologs of reticulocalbin for the first time in hepatoma cells and their 
      expression increased compared to liver cells. However, tubulin beta-1 chain and 
      natural killer cell enhancing factor B were downregulated in hepatoma cells. A 
      tumor suppressing serpin, maspin precursor, was identified from one spot whose 
      quantity was much higher in the normal liver cell line. More interestingly, 
      epidermal fatty acid-binding protein (E-FABP) and fatty acid-binding protein, 
      adipocyte-type (A-FABP), were detected in liver cells but not in hepatoma cells. 
      The functional implication of the identified proteins was discussed.
FAU - Yu, L R
AU  - Yu LR
AD  - Shanghai Institute of Biochemistry, Chinese Academy of Sciences.
FAU - Zeng, R
AU  - Zeng R
FAU - Shao, X X
AU  - Shao XX
FAU - Wang, N
AU  - Wang N
FAU - Xu, Y H
AU  - Xu YH
FAU - Xia, Q C
AU  - Xia QC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Electrophoresis
JT  - Electrophoresis
JID - 8204476
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteins)
SB  - IM
MH  - Chromatography, Liquid/methods
MH  - Electrophoresis, Gel, Two-Dimensional/methods
MH  - Humans
MH  - Liver/*metabolism
MH  - Liver Neoplasms/*metabolism
MH  - Mass Spectrometry/methods
MH  - Neoplasm Proteins/*analysis/*biosynthesis
MH  - Protein Biosynthesis
MH  - Proteins/analysis
MH  - Tumor Cells, Cultured
EDAT- 2000/09/23 11:00
MHDA- 2001/03/03 10:01
CRDT- 2000/09/23 11:00
PHST- 2000/09/23 11:00 [pubmed]
PHST- 2001/03/03 10:01 [medline]
PHST- 2000/09/23 11:00 [entrez]
AID - 10.1002/1522-2683(20000801)21:14<3058::AID-ELPS3058>3.0.CO;2-U [pii]
AID - 10.1002/1522-2683(20000801)21:14<3058::AID-ELPS3058>3.0.CO;2-U [doi]
PST - ppublish
SO  - Electrophoresis. 2000 Aug;21(14):3058-68. doi: 
      10.1002/1522-2683(20000801)21:14<3058::AID-ELPS3058>3.0.CO;2-U.