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1 Institut de recheches cliniques de Montreal, Montreal, Quebec, Canada
2 Medical Molecular Biology, University of Lubeck, Lubeck, Germany
* To whom correspondence should be addressed. E-mail: thibaug{at}ircm.qc.ca.
Fibrillin-1 localization in the myocardium and the modulation of its expression in cardiac fibrosis was examined. In normal rat hearts, fibrillin-1 was abundant throughout the myocardium as thin fibers that crossed over the perimysium and around arteries. After inducing cardiac fibrosis in rats either by 14-day angiotensin II (Ang II) infusion or 21-day deoxycorticosterone (DOCA) acetate-salt treatment (a high endothelin-1 (ET-1) model), fibrillin-1 immunostaining was stronger in the interstitium (2.8-fold and 4.4-fold increases respectively in each model), extended between myocytes, and accumulated in microscopic scars and in the perivascular area of both ventricles. mRNA analysis confirmed its enhanced ventricular expression in both groups of rats (2.5-fold and 6.6-fold increments respectively in each model). In 1B normotensive and 2C hypertensive transgenic mice, 2 lines expressing an Ang II fusion protein in cardiac myocytes, strong fibrillin-1 immunoreactivity was observed in the interstitium and around arteries (3.7-fold and 7-fold increases respectively). Ang II and transforming growth factor-
1 enhanced fibrillin-1 synthesis by cardiac fibroblasts. Some fibrillin-1 fragments interacted with RGD-dependent integrins, including 
81 integrin, of cardiac fibroblasts, but not necessarily through the RGD motif. Our findings illustrate that fibrillin-1 is an important constituent of the myocardium. In vitro and in vivo evidence suggests that Ang II can directly induce fibrillin-1 expression in cardiac fibroblasts. This protein can thus contribute to reactive and reparative processes.
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