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1 Myocardial Biology Unit, Whitaker Cardiovascular Institute, Boston University School of Medicine, and Cardiovascular Division, Boston Medical Center, Boston, Massachusetts 02118; and 2 Division of Hypertension and Vascular Research, Henry Ford Hospital, Detroit, Michigan 48202
Oxidative
stress has been implicated in the pathophysiology of myocardial
failure. We tested the hypothesis that oxidative stress can regulate
extracellular matrix in cardiac fibroblasts. Neonatal and adult rat
cardiac fibroblasts in vitro were exposed to
H2O2 (0.05-5 µM) or the
superoxide-generating system xanthine (500 µM) plus xanthine oxidase
(0.001-0.1 mU/ml) (XXO) for 24 h. In-gel zymography
demonstrated that H2O2 and XXO each increased gelatinase activity corresponding to matrix metalloproteinases (MMP)
MMP-13, MMP-2, and MMP-9. H2O2 and XXO
decreased collagen synthesis (collagenase-sensitive
[3H]proline incorporation) without affecting total
protein synthesis ([3H]leucine incorporation).
H2O2 and XXO decreased the expression of
procollagen 
1(I), 2(I), and
1(III) mRNA but increased the expression of fibronectin
mRNA, suggesting a selective transcriptional effect on collagen
synthesis. H2O2, but not XXO, also decreased the expression of nonfibrillar procollagen 1(IV) and
2(IV) mRNA. To determine the role of endogenous
antioxidant systems, cells were treated with the superoxide dismutase
(SOD) inhibitor diethyldithiocarbamic acid (DDC, 100 µM) to increase
intracellular superoxide or with the glucose-6-phosphate dehydrogenase
inhibitor dehydroisoandrosterone 3-acetate (DHEA; 10 µM) to increase
intracellular H2O2. DDC and DHEA decreased
collagen synthesis and increased MMP activity, and both effects were
inhibited by an SOD/catalase mimetic. Thus increased oxidative stress
activates MMPs and decreases fibrillar collagen synthesis in cardiac
fibroblasts. Oxidative stress may play a role in the pathogenesis of
myocardial remodeling by regulating the quantity and quality of
extracellular matrix.
reactive oxygen species; H2O2; superoxide; superoxide dismutase; glucose-6-phosphate dehydrogenase; in vitro
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