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, and Contact Sensitizers
*
Department of Dermatology, DHURVD,
Division of Immunology and Allergy,
Division of Endocrinology and Diabetology, and
Division of Hematology, University Hospital, Geneva, Switzerland; and
¶
L’Oréal Advanced Recherche, Aulnay-sous-bois, France
We investigated the involvement of mitogen-activated protein
kinases (MAPKs) in the maturation of CD83- dendritic cells
(DC) derived from human blood monocytes. Maturating agents such as LPS
and TNF-
induced the phosphorylation of members of the three
families of MAPK (extracellular signal-regulated kinase l/2, p46/54
c-Jun N-terminal kinase, and p38 MAPK). SB203580, an inhibitor of the
p38 MAPK, but not the extracellular signal-regulated kinase l/2 pathway
blocker PD98059, inhibited the up-regulation of CD1a, CD40, CD80, CD86,
HLA-DR, and the DC maturation marker CD83 induced by LPS and TNF-.
In addition, SB203580 inhibited the enhancement of the allostimulatory
capacity and partially prevented the down-regulation of FITC-dextran
uptake induced by LPS and TNF-. Likewise, SB203580 partially
prevented the up-regulation of IL-1, IL-1
, IL-lRa, and TNF-
mRNA upon stimulation with LPS and TNF-, as well as the release of
bioactive TNF- induced by LPS. DC maturation induced by the contact
sensitizers 2,4-dinitrofluorobenzene and NiSO4, as seen by
the up-regulation of CD80, CD86, and CD83, was also coupled to the
phosphorylation of p38 MAPK, and was inhibited by SB203580. The
irritants SDS and benzalkonium chloride that do not induce DC
maturation did not trigger p38 MAPK phosphorylation. Together, these
data indicate that phosphorylation of p38 MAPK is critical for the
maturation of immature DC. These results also suggest that p38 MAPK
phosphorylation in DC may become useful for the identification of
potential skin contact sensitizers.
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