Journal of Leukocyte Biology
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(Journal of Leukocyte Biology. 2000;68:575-582.)
© 2000 by Society for Leukocyte Biology

Differential localization of protein kinase C isotypes in equine eosinophils and neutrophils

E. C. Greenaway, F. M. Cunningham* and N. T. Goode

Department of Veterinary Basic Sciences, The Royal Veterinary College, Royal College Street, London, NW1 OTU, UK; and
* Hawkshead Campus, Hawkshead Lane, Hatfield, Herts, AL9 7TA, UK

Correspondence: N. T. Goode, Department of Veterinary Basic Sciences, The Royal Veterinary College, Royal College Street, London, NW1 OTU, UK. E-mail: ngoode{at}rvc.ac.uk

Phorbol esters, which activate protein kinase C (PKC), stimulate equine eosinophil superoxide production and adherence. After showing that superoxide production could be inhibited by the nonselective PKC inhibitors, staurosporine and bisindolymaleimide I, the PKC isotypes in equine eosinophils were characterized, because evidence suggests that individual isotypes may play distinct roles in regulating eosinophil function. Western blots demonstrated that equine eosinophils expressed PKC {alpha}, ß, {delta}, {varepsilon}, {iota}, and {zeta}. However, unlike the equine neutrophil, the majority of the PKC was detected in the particulate fraction of the cell. Despite this unusual location, the PKC in equine eosinophils was activatable, suggesting that it is functionally competent. The regulatory role of PKC in equine eosinophils may reflect the association of activity with the particulate fraction and the profile of isotype expression.

Key Words: horse granulocytes • PKC isotypes • PKC inhibitors • superoxide






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