Protein kinase C involvement in aloe‐emodin‐ and emodin‐induced apoptosis in lung carcinoma cell

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Abstract
This study demonstrated aloe‐emodin‐ and emodin‐induced apoptosis in lung carcinoma cell lines CH27 (human lung squamous carcinoma cell) and H460 (human lung non‐small cell carcinoma cell). Aloe‐emodin‐ and emodin‐induced apoptosis was characterized by nuclear morphological changes and DNA fragmentation. During apoptosis, an increase in cytochrome c of cytosolic fraction and activation of caspase‐3, identified by the cleavage of its proform, were observed. To elucidate whether the expression of protein kinase C (PKC) isozymes are involved in aloe‐emodin‐ and emodin‐induced apoptosis, this study examined the changes of PKC isozymes by Western blotting techniques during aloe‐emodin‐ and emodin‐induced apoptosis. The expression of PKC isozymes involved in aloe‐emodin‐ and emodin‐induced apoptosis of CH27 and H460 cells. In this study, aloe‐emodin and emodin induced the changes of each of PKC isozymes in CH27 and H460 cells. The decrease in the expression of PKCδ and ε may play a critical role in aloe‐emodin‐ and emodin‐induced apoptosis in CH27 and H460 cells. The present study also demonstrated that PKC stimulation occurs at a site downstream of caspase‐3 in the emodin‐mediated apoptotic pathway. British Journal of Pharmacology (2001) 134, 1093–1103; doi:10.1038/sj.bjp.0704342