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Thiol-containing molecules interact with the myeloperoxidase/H2O2/chloride system to inhibit LDL oxidation.

Abstract：

:Oxidized low-density lipoproteins (LDL) accumulate in the vascular wall and promote a local inflammatory process contributing to the progression of atheromatous plaque. The key role of myeloperoxidase (MPO) in this process has been documented and the enzyme has been involved in the oxidative modification of apolipoprotein B-100 in the intima and at the surface of endothelial cells. As the inhibition of this last phenomenon could be of relevance in pharmacological interventions, thiol-containing molecules such as glutathione, captopril, and N-acetylcysteine (NAC) and its lysinate salt (NAL) were tested in this system and their properties were compared with those of flufenamic acid (control). This last compound already demonstrated an inhibition of the production of HOCl by MPO and a more intense inhibition of MPO activity than glutathione, NAC, NAL, and captopril. However, NAC and NAL inhibited the oxidative modification of LDL more intensively than captopril and glutathione whereas flufenamic acid had no comparable inhibiting effect. This could be related to the presence of LDL close to the catalytic site of the enzyme. NAC and NAL therefore appeared as the most efficient inhibitors probably as a consequence of their relatively small size. The relevance of such effects has to be documented by in vivo studies.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Van Antwerpen P,Boudjeltia KZ,Babar S,Legssyer I,Moreau P,Moguilevsky N,Vanhaeverbeek M,Ducobu J,Nève J

doi

10.1016/j.bbrc.2005.09.013

subject

Has Abstract

pub_date

2005-11-11 00:00:00

pages

82-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02011-5

journal_volume

337

pub_type

杂志文章

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