The effect of histone deacetylase inhibitor trichostatin A (TSA) on the incorporation of 32P (Pi) and 3H-palmitic acid into the phospholipids of Tetrahymena.
Histone deacetylases (HDACs) are able to control also the acetylation of tubulin. In the present experiments the effect of trichostatin A (TSA), a HDAC inhibitor was studied on the incorporation of 3H-palmitic acid and 32P to the phospholipids (PI, PIP, PS, PC, PA, PE) of Tetrahymena pyriformis, considering earlier observations on the microtubular system's influence on signalling in this unicellular eukaryote. Treatment with 1, 5, or 10 microM TSA was studied. The incorporation of hydrophobic tail component, palmitic acid was inhibited in a concentration dependent manner into all the phospholipids, except for PA, where the incorporation was increased. 32P incorporation was also inhibited. The possible relation between the microtubular system and signalling is discussed.
Kovács
Péter
P
Department of Genetics, Cell and Immunobiology, Semmelweis University, Budapest, Hungary. kovpet@net.sote.hu
Csaba
György
G
D000818:Animals; D056572:Histone Deacetylase Inhibitors; D006877:Hydroxamic Acids / Q000494:pharmacology*; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism; D019308:Palmitic Acid / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*; D010743:Phospholipids / Q000037:antagonists & inhibitors / Q000096:biosynthesis*; D010761:Phosphorus Radioisotopes; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology; D013769:Tetrahymena pyriformis / Q000187:drug effects / Q000201:enzymology*; D014316:Tritium / Q000378:metabolism
D056572:Histone Deacetylase Inhibitors; D006877:Hydroxamic Acids; D010710:Phosphates; D010743:Phospholipids; D010761:Phosphorus Radioisotopes; D014316:Tritium; D019308:Palmitic Acid; C012589:trichostatin A