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The Journal of Immunology, 2000, 165: 1395-1402.
Copyright © 2000 by The American Association of Immunologists

IL-4 Enhances Keratinocyte Expression of CXCR3 Agonistic Chemokines1

Cristina Albanesi2, Claudia Scarponi, Silvia Sebastiani, Andrea Cavani, Monica Federici, Ornella De Pità, Pietro Puddu and Giampiero Girolomoni

Istituto Dermopatico dell’Immacolata, IRCCS, Rome, Italy

IFN-induced protein of 10 kDa (IP-10), monokine induced by IFN-{gamma} (Mig), and IFN-inducible T-cell {alpha}-chemoattractant (I-TAC) belong to the non-glutamate-leucine-arginine motif CXC chemokine family and act solely through the CXCR3 receptor for potent attraction of T lymphocytes. In this study, we evaluated the capacity of the T cell-derived cytokines IL-4, IL-10, and IL-17 to modulate IP-10, Mig, and I-TAC in cultured human keratinocytes and CXCR3 expression in T cells from allergic contact dermatitis (ACD). IL-4, but not IL-10 or IL-17, significantly up-regulated IFN-{gamma}- or TNF-{alpha}-induced IP-10, Mig, and I-TAC mRNA accumulation in keratinocytes and increased the levels of IP-10 and Mig in keratinocyte supernatants. Immunohistochemistry of skin affected by ACD revealed that >70% of infiltrating cells were reactive for CXCR3 and that CXCR3 staining colocalized in CD4+ and CD8+ T cells. Nickel-specific CD4+ and CD8+ T cell lines established from ACD skin produced IFN-{gamma} and IL-4 and expressed moderate to high levels of CXCR3. Finally, CXCR3 agonistic chemokines released by stimulated keratinocytes triggered calcium mobilization in skin-derived nickel-specific CD4+ T cells and promoted their migration, with supernatant from keratinocyte cultures stimulated with IFN-{gamma} and IL-4 attracting more efficaciously than supernatant from keratinocytes activated with IFN-{gamma} alone. In conclusion, IL-4 exerts a proinflammatory function on keratinocytes by potentiating IFN-{gamma} and TNF-{alpha} induction of IP-10, Mig, and I-TAC, which in turn may determine a prominent recruitment of CXCR3+ T lymphocytes at inflammatory reaction sites.




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