Apicidin decreases phospholipase C gamma-1 transcript and protein in Hut-78 T lymphoma cells

Phospholipase C gamma-1 (PLCgamma1) phosphorylation is a key step in intracellular signal transduction in T cells. We used Hut-78 T lymphoma cells to demonstrate the effect of apicidin on cellular levels of the PLCgamma1 molecule. Using reverse-transcription, real-time quantitative PCR and Western blot analysis, we observed that apicidin reduced the PLCgamma1 transcript and protein contents in Hut-78 T lymphoma cells. Our results indicate that protein synthesis appears to be crucial in the apicidin decrease of PLCgamma1 mRNA steadiness. Moreover, we determined that apicidin reduces the half-life of PLCgamma1 mRNAs from approximately 2 to 4h. Since PLCgamma1 is considered a key molecule in signal transduction in T cells, apicidin may be useful in the treatment of some autoimmune diseases in which autoreactive T cells occur.