Premium
Enzymatic repair of oxidative damage to human apolipoprotein A‐I
Author(s) -
Sigalov Alexander B.,
Stern Lawrence J.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00908-9
Subject(s) - methionine sulfoxide reductase , apolipoprotein b , methionine , biochemistry , enzyme , chemistry , cholesterol , oxidative phosphorylation , efflux , amino acid
Oxidative damage to apolipoprotein A‐I that occurs in vivo commonly involves methionine oxidation, and is accompanied by alterations in structure, lipid association, and cholesterol efflux function. We have used the enzyme peptide methionine sulfoxide reductase (PMSR) to reverse this damage, and shown by a variety of criteria that enzyme treatment restores the primary, secondary, and tertiary structure and lipid association characteristic of the native unoxidized protein. Lipid‐associated as well as lipid‐free apolipoprotein A‐I reacts with PMSR, suggesting that enzymatic reduction of oxidized apolipoprotein A‐I in high density lipoproteins can result in restoration of biological activity and the ability to promote cholesterol efflux from cells.