Abstract.
Objective: To determine if protein kinase C (PKC) regulates equine eosinophil function.
Material or subjects: Blood eosinophils were obtained from healthy ponies.
Methods: IL-5- and histamine-induced adherence to serum-coated plastic was measured as the eosinophil peroxidase content of adherent cells and serum treated zymosan (STZ)-and IL-5-induced superoxide production by the reduction of cytochrome C. Eosinophil PKC activity was quantitated as the rate of transfer of 32P from ATP to substrate. The effects of Ro31-8220 (isotype non-selective PKC inhibitor), Gö6976 (conventional PKC inhibitor), and rottlerin (PKCδ inhibitor) were determined by ANOVA and Bonferroni’s or Dunnett’s test.
Results: Ro31-8220 and Gö6976 reduced superoxide production whereas only Gö6976 inhibited adherence. Rottlerin inhibited histamine-induced adherence and increased STZ-induced superoxide production. Ro31-8220 and Gö6976, but not rottlerin, inhibited PKC activity.
Conclusions: PKC is involved in regulating equine eosinophil adherence and superoxide production. The role of PKCδ appears to depend upon the stimulus used and response measured.
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Received 13 September 2004; returned for revision 19 October 2004; accepted by N. Boughton-Smith 4 November 2004
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Sepulveda, M.F., Greenaway, E.C., Avella, M. et al. The role of protein kinase C in regulating equine eosinophil adherence and superoxide production. Inflamm. res. 54, 97–105 (2005). https://doi.org/10.1007/s00011-004-1329-2
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DOI: https://doi.org/10.1007/s00011-004-1329-2