The fatty acid-binding heterocomplex FA-p34 formed by S100A8 and S100A9 isthe major fatty acid carrier in neutrophils and translocates from the cytosol to the membrane upon stimulation
K. Roulin et al., The fatty acid-binding heterocomplex FA-p34 formed by S100A8 and S100A9 isthe major fatty acid carrier in neutrophils and translocates from the cytosol to the membrane upon stimulation, EXP CELL RE, 247(2), 1999, pp. 410-421
Since no data are available concerning fatty acid (FA) transport in neutrop
hils we studied the presence of possible FA carriers. The kFA-p34 complex,
composed of S100A8 and S100A9, has been implicated in the intracellular tra
nsport of arachidonic acid and its precursors in human keratinocytes. Here,
we show that FA-p34 is the major FA carrier in human neutrophils (nFA-p34)
. The complex is highly expressed in resting neutrophils (2.65% of cytosoli
c proteins) and translocates to the membrane fraction upon stimulation with
opsonized zymosan. Comparison of purified nFA-p34 with kFA-p34 shows that
both complexes are composed of nearly the same subunits and possess similar
binding properties for oleic acid. Densito-metrical analyses of 2D gels sh
ow that n and kFA-p34 contain twice as much S100A8 and S100A9 suggesting an
estimated stoichiometry of (S100A8),S100A9. A method is described allowing
to distinguish n and kFA-p34 from S100A8/S100A9 homo- and heteromer comple
xes that are devoid of FA-binding properties. After solvent extraction, we
find by GC analysis linoleic acid as major endogenous Ligand of purified kF
A-p34. Our results suggest that nFA-p34, might be involved in the shuttling
of unsaturated FA between the cytosol and the plasma membrane of neutrophi
ls. (C) 1999 Academic Press.