Article: Studies by K. Kitatani and co-authors describe new findings in enzyme research.

"Activation of protein kinase C (PKC) by the phorbol ester (phorbol 12-myristate 13-acetate) induces ceramide formation through the salvage pathway involving, in part, acid beta-glucosidase 1 (GBA1), which cleaves glucosylceramide to ceramide. Here, we examine the role of the GBA1-ceramide pathway, in regulating a pro-inflammatory pathway initiated by PKC and leading to activation of p38 and induction of interleukin 6 (IL-6)," scientists in the United States report (see also Enzyme Research).

"Inhibition of ceramide formation by fumonisin B1 or down-regulation of PKC delta potentiated PMA-induced activation of p38 in human breast cancer MCF-7 cells. Similarly, ...

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