Association between bcl-x(L) and 5-lipoxygenase activating protein (FLAP) levels in IL-3-dependent FL5.12 cells

S S Biswal1, K Datta, J P Kehrer

  • 1Division of Pharmacology and Toxicology, College of Pharmacy, The University of Texas, Austin TX 78712-1074, USA.

Toxicology
|March 14, 2001
PubMed

Insights

Overexpression of bcl-x(L) reduces 5-lipoxygenase activating protein (FLAP) levels in cells lacking apoptosis. Protease inhibitors partially prevent FLAP loss, suggesting a link between bcl-x(L) and FLAP regulation.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The expression of 5-lipoxygenase activating protein (FLAP) is altered in cells overexpressing bcl-x(L).
  • IL-3 withdrawal causes FLAP loss in bcl-x(L) overexpressing cells, but not apoptosis.
  • The mechanisms behind FLAP regulation by bcl-x(L) are not understood.

Purpose of the Study:

  • To investigate the mechanism of FLAP regulation in bcl-x(L) overexpressing cells.
  • To determine if FLAP loss is transcriptionally regulated.
  • To explore the role of proteolysis in FLAP degradation.

Main Methods:

  • Comparing FLAP expression in bcl-x(L) overexpressing cells versus control cells.
  • Analyzing FLAP mRNA levels after IL-3 withdrawal.
  • Assessing the effect of protease inhibitors (Boc-D-FMK, PMSF, pepstatin, leupeptin) on FLAP levels.

Main Results:

  • Basal FLAP mRNA levels were higher in bcl-x(L) cells, indicating a post-transcriptional regulation.
  • IL-3 withdrawal increased FLAP mRNA in both cell types, suggesting FLAP loss is not transcription-dependent.
  • Protease inhibitors, particularly PMSF, protected FLAP from degradation, implying a proteolytic mechanism.

Conclusions:

  • FLAP regulation by bcl-x(L) involves post-transcriptional mechanisms, likely proteolysis.
  • Protease activation can occur independently of apoptosis.
  • A connection between bcl-x(L) and FLAP expression is suggested.

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