Inhibition of de Novo Sphingolipid Biosynthesis by Geranyllinalool in LLC-PK1, Cells

Inhibition of de Novo Sphingolipid Biosynthesis by Geranyllinalool in LLC-PK1, Cells

YAKHAK HOEJI 1999;43(1):61-67

Published online February 27, 1999

조양혁(Yang Hyeok Cho);이용문(Yong Moon Lee)

Abstract: Geranyllinalool, a polyisoprenoid compound, was found to block the early biosynthetle pathway of sphingolipids in LLC-PK1 cells. Sphinganine, an intermediate in sphingolipid biosynthetic pathway, was abruptly accumulated in LLC-PK1 cells at 2mcM of fumonisin B1(FB1), a specific inhibitor of sphinganine N-acyltransferase, for 24 hr. Geranyllinalool lowered the FB1-induced elevation of intracellular sphinganine by 3.2% at the concentration of 2mcM FB1 and 50mcM geranyllinalool. l-Cycloserine, an inhibitor of serine-palmitoyl transferase, was used as a positive control to evaluate the inhibitory effect of geranyllinalool. These results suggest that geranyllinalool may inhibit the serine-palmitoyl transferase, the first enzyme in de novo sphingolipid biosynthesis, resulting in the altered regulation of sphingolipid metabolism.; Keywords : Geranyllinalool;sphinganine;fumonisin B1;LLC-PK1 cells.

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