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Regulation of the CDP‐ethanolamine (Kennedy) pathway by oxysterols
Author(s) -
Zhu Lin,
Bakovic Marica
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a93-b
Subject(s) - ethanolamine , chemistry , phosphatidylethanolamine , biochemistry , phosphatidylserine , microbiology and biotechnology , biology , phospholipid , phosphatidylcholine , membrane
The CDP‐ethanolamine (Kennedy) pathway synthesizes phosphatidylethanolamine (PE) and PE plasmalogens de novo from ethanolamine and diacylglycerols or alkylacyl glycerols, respectively. The intermediate reaction in which CDP: ethanolaminephosphate cytidylyltransferase (Pcyt2) catalyzes the formation of CDP‐ethanolamine from CTP and ethanolaminephosphate is the main regulatory step in this pathway. Pulse‐chase radiolabeling experiments of the mouse embryonic cells C3H10T1/2 with 14C‐ethanolamine demonstrate that 14C‐CDP‐ethanolamine synthesis decreases 70% after 48h treatments with 25‐hydroxycholesterol. After radiolabeling with 14C‐ethanolamine and 3H‐glycerol PE synthesis decreases 2‐fold under the same conditions. The regulation is at the step catalyzed by Pcyt2. Analysis of the mouse Pcyt2 promoter demonstrates that two regions could be responsive to the oxysterol treatments. The promoter region between −475bp and ‐302 bp contains the consensus binding sites for Ap1, MyoD, cEBP transcription factors; the region located within the −252/−185 bp area contains bonding sites for Sp1.