Greenaway E C, Cunningham F M, Goode N T
Department of Veterinary Basic Sciences, The Royal Veterinary College, London, UK.
J Leukoc Biol. 2000 Oct;68(4):575-82.
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, beta, delta, epsilon, 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.
佛波酯可激活蛋白激酶C（PKC），刺激马嗜酸性粒细胞产生超氧化物并促进其黏附。在用非选择性PKC抑制剂星形孢菌素和双吲哚马来酰胺I证明超氧化物的产生可被抑制后，对马嗜酸性粒细胞中的PKC同工型进行了表征，因为有证据表明，个别同工型可能在调节嗜酸性粒细胞功能中发挥不同作用。蛋白质印迹法表明，马嗜酸性粒细胞表达PKCα、β、δ、ε、ι和ζ。然而，与马中性粒细胞不同的是，大部分PKC存在于细胞的颗粒部分。尽管位置不同寻常，但马嗜酸性粒细胞中的PKC是可激活的，这表明它在功能上是有活性的。PKC在马嗜酸性粒细胞中的调节作用可能反映了其活性与颗粒部分的关联以及同工型表达情况。
