Alpha-hydroxylation of lignoceroyl-CoA in rat brain microsomes: involvement of NADPH-cytochrome c reductase and topical distribution

The International Journal of Biochemistry
H ShigematsuY Kishimoto

Abstract

1. The enzymatic mechanism of the alpha-hydroxylation of lignoceroyl-CoA, an intermediate in the synthesis of hydroxyceramide, was studied. In the presence of NADPH, sphingosine and microsomes from 20-day-old rat brain, 14C from [1-14C]lignoceroyl-CoA was incorporated into hydroxyceramide. 2. The alpha-hydroxylation of lignoceroyl-CoA in rat brain microsomes was strongly inhibited by a rabbit anti-immunoglobulin G which was prepared against rat liver microsomal NADPH-cytochrome c reductase. However, anti-immunoglobulin G against cytochrome b5 did not inhibit the alpha-hydroxylase activity. 3. The alpha-hydroxylation activity was more sensitive to trypsin treatment than was NADPH-cytochrome c reductase in rat brain microsomes. This indicates that either alpha-hydroxylase itself or an unknown factor essential in alpha-hydroxylation is highly exposed to the surface of brain microsomes.

References

Jan 1, 1978·Methods in Enzymology·R W Estabrook
Dec 14, 1979·Molecular and Cellular Biochemistry·Y KishimotoI Singh
Nov 1, 1975·Archives of Biochemistry and Biophysics·K TatsumiY Kishimoto
Jan 1, 1987·The International Journal of Biochemistry·H Shigematsu, Y Kishimoto
Jan 1, 1971·Journal of Biochemistry·N OshinoR Sato
Jan 1, 1984·Neurochemical Research·J L TrotterW W Tourtellotte
Mar 12, 1963·Biochimica Et Biophysica Acta·H NISHIBAYASHIR SATO
Jan 1, 1966·Lipids·Y Kishimoto, N S Radin

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Citations

Sep 26, 2006·Journal of Lipid Research·Nathan L AldersonHiroko Hama
Sep 1, 2004·The Journal of Biological Chemistry·Nathan L AldersonHiroko Hama
Dec 23, 2009·Biochimica Et Biophysica Acta·Hiroko Hama

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