Lecithin:Cholesterol acyltransferase reduces the adverse effects of oxidized low-density lipoprotein while incurring damage itself

Zakir H. Howlader, Shin Kamiyama, Yohei Murakami, Michiko Ito, Michio Komai, Yuji Furukawa

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

In this study, we tried to determine (a) whether there is any permanent effect of oxLDL on the LCAT molecule and its activator lipoprotein apoA-I, and (b) the fate of oxLDL after its exposure to LCAT and apoA-I. Purified LCAT and LDL/oxLDL was incubated at 37°C for 1h, and separated by gel-permeation chromatography. Its activity was significantly less (30% less) after separating from oxLDL compared to that of LDL. Cofactor activity of isolated apoA-I (incubated with LDL/oxLDL) was found affected by oxLDL. These results indicate modification of the LCAT and apoA-I molecule. But LCAT was found more affected compared to apoA-I in terms of LCAT activity. We are also reporting a novel function of LCAT. It was found to reduce the adverse effects of oxLDL, for example, ability to affect the LCAT activity and TBARS value. This ability of LCAT to repair oxLDL was dose-dependent. But there was no change in its REM values or fluorescence intensity.

Original languageEnglish
Pages (from-to)2496-2503
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Volume65
Issue number11
DOIs
Publication statusPublished - 2001 Nov 1

Keywords

  • Adverse effects of oxLDL
  • Apolipoprotein A-I
  • Irreversible modification
  • Lecithin:Cholesterol acyltransferase
  • Oxidized LDL

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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