In situ expression of beta 1, beta 3 and beta 4 integrin subunits in non-neoplastic endothelium and vascular tumours.

Endothelial cells play an important role in adhesive interactions between circulating cells and extracellular matrix proteins. In vitro studies have shown that many of these processes are mediated by a superfamily of alpha beta heterodimeric transmembrane glycoproteins called integrins. The distribution patterns of beta 1, beta 3 and beta 4 integrin subunits in endothelial cells (EC) in situ were examined immunohistochemically on serial frozen sections of a wide range of non-neoplastic tissues and of vascular tumours, both benign and malignant. Expression of the beta 1 subunit was a constitutive feature of EC. Among the beta 1-associated alpha subunits, alpha 5 and alpha 6 were broadly distributed in EC, irrespective of vessel size and microenvironment. The alpha 3 subunit displayed intermediate levels of expression with a slight preference for small vessel EC. Presence of alpha 1 was confined to EC of capillaries and venules/small veins. Expression of alpha 2 in EC was inconsistent. With rare exceptions, the alpha 4 chain was absent in EC. The beta 3 and alpha v subunits were expressed in most EC, though not always concomitantly. In contrast to the beta 1 chain, however, these integrin subunits were absent in EC of glomerular capillaries and were expressed variably in sinusoidal EC. The beta 4 chain was evenly present in the great majority of EC, except for those of large vessels. In vascular tumours, the patterns of beta 1 and alpha 1 to alpha 6 subunit expression generally corresponded to those found in their non-neoplastic counterparts. Expression of beta 3, alpha v and beta 4 chains, however, decreased in neoplasia, especially in angiosarcomas. These data show that EC dispose of broad and at the same time differential repertoires of integrin subunits that presumably reflect vessel-type associated functional differences among these cells. In vascular tumours, the orthologous distribution patterns of beta 1 and alpha 1 to alpha 6 chains are conserved in most instances while the amounts of beta 3, alpha v and beta 4 subunits expressed in EC tend to decrease in the course of malignant transformation.