The SPTLC3 Subunit of Serine Palmitoyltransferase Generates Short Chain Sphingoid Bases

作者: Thorsten Hornemann , Anke Penno , Markus F. Rütti , Daniela Ernst , Fatma Kivrak-Pfiffner

DOI: 10.1074/JBC.M109.023192

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摘要: The enzyme serine palmitoyltransferase (SPT) catalyzes the rate-limiting step in de novo synthesis of sphingolipids. Previously mammalian SPT was described as a heterodimer composed two subunits, SPTLC1 and SPTLC2. Recently we identified novel third subunit (SPTLC3). SPTLC3 shows about 68% identity to SPTLC2 also includes pyridoxal phosphate consensus motif. Here report that overexpression HEK293 cells leads formation new sphingoid base metabolites, namely C16-sphinganine C16-sphingosine. SPTLC3-expressing have higher vitro activities with lauryl- myristoyl-CoA than SPTLC2-expressing cells, mRNA expression levels correlate closely rates various human murine cell lines. Approximately 15% total sphingolipids plasma contain C16 backbone are found high density low but not very lipoprotein fraction. In conclusion, show generates C16-sphingoid bases constitute significant proportion

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