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Occurrence of nonenzymatic N‐acetylation of sphinganine with acetyl coenzyme a producing C2‐H2‐ceramide and its inconvertibility to apoptotic C2‐ceramide
Author(s) -
Kashiwagi Motoi,
Mikami Takeshi,
Chiba Masahiko,
Chiba Susumu,
Matsumoto Hiroyuki,
Akino Toyoaki,
Gasaa Shinsei
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203531
Subject(s) - ceramide , acetylation , chemistry , residue (chemistry) , biochemistry , acetyl coa , enzyme , apoptosis , stereochemistry , gene
Sphinganine, a biosynthetic precursor of ceramide, was non‐enzymatically acetylated with acetyl coenzyme A at the C‐2‐amino residue to produce C2‐H2‐ceramide (N‐acetyl sphinganine) in an organic solvent and in an aqueous solution with a high yield, where as sphingenine was only acetylated slightly. The structure of the N‐acetyl sphinganine was identified with mass spectrum, and with chromatography using an authentic N‐acetylated substance. Furthermore, the C2‐H2‐ceramide was examined for enzymatic desaturation to determine whether C2‐ceramide, a cell‐permeable ceramide responsible for apoptosis of cells, was produced, revealing an inferior substrate for H2‐ceramide desaturase of horse brain microsomes.