Donate Help Contact The AHA Sign In Home
American Heart Association
Arteriosclerosis, Thrombosis, and Vascular Biology
Search: search_blue_button Advanced Search
« Previous Article | Table of Contents | Next Article »
Arteriosclerosis, Thrombosis, and Vascular Biology. 1993;13:23-32

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lindstedt, K. A.
Right arrow Articles by Kovanen, P. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lindstedt, K. A.
Right arrow Articles by Kovanen, P. T.

Arteriosclerosis and Thrombosis, Vol 13, 23-32, Copyright © 1993 by American Heart Association

ARTICLES

Inhibition of copper-mediated oxidation of LDL by rat serosal mast cells. A novel cellular protective mechanism involving proteolysis of the substrate under oxidative stress

KA Lindstedt, JO Kokkonen and PT Kovanen
Wihuri Research Institute, Helsinki, Finland.

Rat serosal mast cells, when stimulated to exocytose their cytoplasmic granules, effectively blocked the copper-mediated oxidation of low density lipoproteins (LDLs) in vitro. This effect depended on the proteolytic activity of the formed extracellular granule remnants, since specific inhibition of chymase, the neutral protease that they contain, blocked the protective effect of the mast cells. The mechanism of this chymase-mediated inhibition of LDL oxidation was found to be binding of the copper ions present in the incubation medium by peptides released from LDL on proteolytic degradation of their apolipoprotein B (apoB) component. This was verified by demonstrating that addition of such peptides to LDL--copper ion mixtures completely prevented oxidation of LDL and that this protective effect could be overcome by adding copper ions in excess. Furthermore, proteolytic degradation of the apoB of LDL, with concomitant release of copper-containing peptides, left the partially degraded apoB without the copper ions necessary for propagation of LDL oxidation. These observations provide the first evidence for cell-mediated inhibition of LDL oxidation.


This article has been cited by other articles:


Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
A. Roland, R. A. Patterson, and D. S. Leake
Measurement of Copper-Binding Sites on Low Density Lipoprotein
Arterioscler Thromb Vasc Biol, April 1, 2001; 21(4): 594 - 602.
[Abstract] [Full Text] [PDF]

Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
J. L. Johnson, C. L. Jackson, G. D. Angelini, and S. J. George
Activation of Matrix-Degrading Metalloproteinases by Mast Cell Proteases in Atherosclerotic Plaques
Arterioscler Thromb Vasc Biol, November 1, 1998; 18(11): 1707 - 1715.
[Abstract] [Full Text] [PDF]

Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
Y. Wang, K. A. Lindstedt, and P. T. Kovanen
Mast Cell Granule Remnants Carry LDL Into Smooth Muscle Cells of the Synthetic Phenotype and Induce Their Conversion Into Foam Cells
Arterioscler Thromb Vasc Biol, June 1, 1995; 15(6): 801 - 810.
[Abstract] [Full Text]


ATVB Home | Subscriptions | Archives | Feedback | Authors | Help | AHA Journals Home | Search
Copyright © 1993 American Heart Association, Inc. All rights reserved. Unauthorized use prohibited.