Year: 1998
Type: article
Abstract: 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.
Source: FEBS Letters
Authors: Alexander B. Sigalov, Lawrence J. Stern
Institution: Massachusetts Institute of Technology
Language: English
Subfield: Surgery
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Funders: CRDF Global, Hospital for Special Surgery
OpenAlex ID: W1977111582