PMID- 14676186
OWN - NLM
STAT- MEDLINE
DCOM- 20040503
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 279
IP  - 9
DP  - 2004 Feb 27
TI  - Stabilization of leukotriene A4 by epithelial fatty acid-binding protein in the 
      rat basophilic leukemia cell.
PG  - 7420-6
AB  - Leukotriene A(4) (LTA(4)) is a chemically unstable triene epoxide product of 
      5-lipoxygenase metabolism of arachidonic acid. Despite this chemical reactivity 
      and its synthesis at the perinuclear membrane, LTA(4) is enzymatically converted 
      into the cysteinyl leukotrienes and leukotriene B(4). Furthermore, LTA(4) 
      participates in transcellular biosynthesis and is thus transferred between cells 
      as an intact molecule. A cytosolic fatty acid-binding protein present in the rat 
      basophilic leukemia cells was identified using mass spectrometry. This protein 
      was determined to be the stabilizing factor present in the cell cytosol 
      responsible for increasing the effective chemical half-life of LTA(4). Rat 
      epithelial fatty acid-binding protein (E-FABP) was isolated using partial protein 
      purification and immunoprecipitation. In-gel digestion with trypsin followed by 
      peptide fingerprint analysis using matrix-assisted laser desorption ionization 
      mass spectrometry and sequencing the major tryptic peptide obtained from liquid 
      chromatography/mass spectrometry/mass spectrometry analysis identified E-FABP in 
      the active fraction. Semi-quantitative Western blot analysis indicated that 
      E-FABP in the cytosolic fraction of RBL-1 cells was present at approximately 1-3 
      pmol/10(6) cells. E-FABP (9 microm) was tested for its ability to stabilize 
      LTA(4), and at 37 degrees C E-FABP was able to increase the half-life of LTA(4) 
      from the previously reported half-life less than 3 s to a half-life of 
      approximately 7 min. These results present a novel function for the well studied 
      fatty acid-binding protein as a participant in leukotriene biosynthesis that 
      permits LTA(4) to be available for further enzymatic processing in various 
      cellular regions.
FAU - Dickinson Zimmer, Jennifer S
AU  - Dickinson Zimmer JS
AD  - Department of Pharmacology, University of Colorado Health Sciences Center, 
      Denver, Colorado 80262.
FAU - Voelker, Dennis R
AU  - Voelker DR
FAU - Bernlohr, David A
AU  - Bernlohr DA
FAU - Murphy, Robert C
AU  - Murphy RC
LA  - eng
GR  - DK53189/DK/NIDDK NIH HHS/United States
GR  - HL 25785/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20031215
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Eye Proteins)
RN  - 0 (Fabp5 protein, rat)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Leukotriene A4)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Fragments)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Carrier Proteins/analysis/pharmacology/*physiology
MH  - Chromatography, High Pressure Liquid
MH  - Cytosol/chemistry
MH  - Electrophoresis, Polyacrylamide Gel
MH  - *Eye Proteins
MH  - Fatty Acid-Binding Proteins
MH  - Half-Life
MH  - Immunosorbent Techniques
MH  - Leukemia, Basophilic, Acute/*metabolism
MH  - Leukotriene A4/chemistry/*metabolism
MH  - Mass Spectrometry
MH  - *Nerve Tissue Proteins
MH  - Peptide Fragments/chemistry/metabolism
MH  - Peptide Mapping
MH  - Rats
MH  - Sequence Analysis, Protein
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Trypsin/metabolism
MH  - Tumor Cells, Cultured
EDAT- 2003/12/17 05:00
MHDA- 2004/05/05 05:00
CRDT- 2003/12/17 05:00
PHST- 2003/12/17 05:00 [pubmed]
PHST- 2004/05/05 05:00 [medline]
PHST- 2003/12/17 05:00 [entrez]
AID - S0021-9258(18)44436-5 [pii]
AID - 10.1074/jbc.M311404200 [doi]
PST - ppublish
SO  - J Biol Chem. 2004 Feb 27;279(9):7420-6. doi: 10.1074/jbc.M311404200. Epub 2003 
      Dec 15.