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(Journal of Leukocyte Biology. 2001;69:651-658.)
© 2001 by Society for Leukocyte Biology

Involvement of PKA, PKC, and Ca²⁺ in LPS-activated expression of the chicken lysozyme gene

Petra Regenhard^*, Ralph Goethe^*, and Loc Phi-van^*

^* Institut für Tierzucht und Tierverhalten Celle (FAL), Celle, Germany; and
Institut für Mikrobiologie und Tierseuchen, Hannover, Germany

Correspondence: Dr. Loc Phi-van, Institut für Tierzucht und Tierverhalten, Dörnbergstr. 25-27, 29223 Celle, Germany. E-mail: loc.phi-van{at}fal.de

The lysozyme gene is activated in myelomonocytic HD11 cells in response to LPS. In this study, we described the involvement of LPS-activated signal transduction pathways in activation of the lysozyme gene. Pre-treatment of HD11 cells with H-89, H-7, TMB-8, or KN-93 resulted in inhibition of the LPS-enhanced lysozyme expression, suggesting that PKA, PKC, and Ca²⁺-dependent protein kinases participate in the LPS activation. CaMKII seems to be required for the processing of lysozyme transcripts. TPA and calcium ionophore A23187, when separately added to HD11 cells, stimulated the lysozyme expression effectively, and forskolin was ineffective. It is interesting that simultaneous treatment of cells with forskolin and calcium ionophore A23187 resulted in a potentiated increase in lysozyme mRNA expression, indicating a synergistic cooperation of PKA and Ca²⁺. This synergistic effect of PKA and Ca²⁺ was observed on the expression of a stably integrated CAT construct, controlled by the lysozyme promoter and the -6.1-kb enhancer containing binding sites for C/EBP and NF-B/Rel. Therefore, we discussed the role of C/EBPß(NF-M), CREB, and NF-B/Rel as possible targets for phosphorylation mediated by PKA, PKC, and Ca²⁺.

Key Words: myelomonocytes • inflammatory response • C/EBPß(NF-M) • CREB • NF-B/Rel

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