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Am J Physiol Cell Physiol 281: C1457-C1467, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 5, C1457-C1467, November 2001

Upregulation of alpha 8beta 1-integrin in cardiac fibroblast by angiotensin II and transforming growth factor-beta 1

Gaétan Thibault1, Marie-Josée Lacombe1, Lynn M. Schnapp2, Alexandre Lacasse1, Fatiha Bouzeghrane1, and Geneviève Lapalme1

1 Laboratory of Cell Biology of Hypertension, Multidisciplinary Research Group in Hypertension of the Canadian Institutes of Health Research, Institut de Recherches Cliniques de Montréal and Université de Montréal, Montreal, Quebec, Canada H2W 1R7; and 2 Pulmonary and Critical Care Medicine, University of Washington, Harborview Medical Center, Seattle, Washington 98104

Using a novel pharmacological tool with 125I-echistatin to detect integrins on the cell, we have observed that cardiac fibroblasts harbor five different RGD-binding integrins: alpha 8beta 1, alpha 3beta 1, alpha 5beta 1, alpha vbeta 1, and alpha vbeta 3. Stimulation of cardiac fibroblasts by angiotensin II (ANG II) or transforming growth factor-beta 1 (TGF-beta 1) resulted in an increase of protein and heightening by 50% of the receptor density of alpha 8beta 1-integrin. The effect of ANG II was blocked by an AT1, but not an AT2, receptor antagonist, or by an anti-TGF-beta 1 antibody. ANG II and TGF-beta 1 increased fibronectin secretion, smooth muscle alpha -actin synthesis, and formation of actin stress fibers and enhanced attachment of fibroblasts to a fibronectin matrix. The alpha 8- and beta 1-subunits were colocalized by immunocytochemistry with vinculin or beta 3-integrin at focal adhesion sites. These results indicate that alpha 8beta 1-integrin is an abundant integrin on rat cardiac fibroblasts. Its positive modulation by ANG II and TGF-beta 1 in a myofibroblast-like phenotype suggests the involvement of alpha 8beta 1-integrin in extracellular matrix protein deposition and cardiac fibroblast adhesion.

adhesion molecules; vinculin; fibronectin; AT1 receptor; actin


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