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Inhibits Activation-Induced Expression of E- and P-Selectin on Endothelial Cells
Protein Design Labs, Mountain View, CA 94043
E- and P-selectin are cell surface lectins that mediate
leukocyte-endothelial cell adhesion and thereby participate in
neutrophil recruitment into inflammatory sites. E-selectin can be
induced on endothelial cells by various activators, including TNF-
,
IL-1ß, and PMA. Induction of E-selectin is blocked by pretreatment of
endothelial cells with IL-4 or TGF-ß, both of which have
antiinflammatory properties in vivo. In addition to its well-known
proinflammatory activities, IFN-
also has antiinflammatory effects
in vivo, one of which is inhibition of neutrophil recruitment. To
determine whether IFN- inhibits neutrophil recruitment by inhibiting
adhesion molecule expression, the effect of IFN- on
activation-induced cell adhesion molecule expression by cultured HUVEC
was evaluated. Pretreatment of endothelial cells with IFN- for 24 to
72 h before 6- to 24-h activation with IL-1ß, TNF-, or PMA
resulted in significantly reduced levels of cell surface E-selectin,
although levels of ICAM-1 and VCAM-1 were the same or increased. The
reduction of cell surface E-selectin levels under these conditions was
reflected in reduced levels of E-selectin mRNA, indicating an effect at
the transcription level or RNA stability. Interestingly, the increase
of cell surface P-selectin expression due to IL-4 treatment of HUVEC
was also inhibited by IFN-, while constitutive levels of P-selectin
were not. These results suggest that the inhibition of neutrophil
recruitment by IFN- in vivo may be due, in part, to the ability of
IFN- to inhibit E- and P-selectin up-regulation. Furthermore, these
findings emphasize the process of leukocyte recruitment as an important
step through which IFN- can direct the character of inflammatory
reactions.
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