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Malondialdehyde binding to proteins dramatically alters fibroblast functions.
Laure Rittié1, Jean-Claude Monboisse, Marie-Claude Gorisse
1Laboratory of Biochemistry and Molecular Biology, CNR FRE, Faculty of Medicine IFR Biomolecules, University of Reims Champagne-Ardenne, France.
Journal of Cellular Physiology
|June 18, 2002
Summary
Malondialdehyde (MDA) binding to proteins impairs fibroblast function, inhibiting contraction and multiplication. MDA-modified proteins disrupt cell cycles and induce apoptosis, contributing to aging and oxidative stress-related diseases.
Area of Science:
- Biochemistry
- Cell Biology
- Aging Research
Background:
- Cell metabolism is regulated by extracellular protein modifications.
- Oxidative stress generates reactive compounds like malondialdehyde (MDA).
- MDA can form adducts with proteins, altering their function.
Purpose of the Study:
- To investigate the effects of MDA-binding to proteins on cultured fibroblast functions.
- To determine the impact of MDA-modified collagen and serum proteins on fibroblast behavior.
Main Methods:
- Fibroblast cultures (3D lattice and monolayer) were used.
- Type I collagen and serum proteins were incubated with varying concentrations of MDA.
- Effects on fibroblast contraction, adhesion, proliferation, cell cycle, and apoptosis were assessed.
Main Results:
- MDA-modified collagen inhibited fibroblast-mediated lattice contraction.
- MDA-modified serum proteins also inhibited lattice contraction and completely halted fibroblast multiplication in monolayer cultures.
- MDA-modified proteins reduced cell proliferation, blocked G2/M cell cycle progression, and induced apoptosis.
Conclusions:
- MDA-modified proteins exhibit deleterious effects on fibroblast functions, comparable to free MDA.
- These findings suggest a role for MDA-modified proteins in aging and degenerative diseases associated with oxidative stress, such as diabetes and atherosclerosis.