Collagen interaction with apically expressed beta 1 integrins: loss of transepithelial resistance and reorganization of cultured thyroid cell monolayer.

We have cultured FRT rat thyroid cells to confluency on filters in bicameral systems and allowed a type I collagen solution to gel on their apical compartment. A dramatic drop in transepithelial resistance occurred within 2 h after collagen addition. This drop in transepithelial resistance was dependent upon collagen concentration. Cells interacting with the collagen lost their apical microvilli, formed pseudopods and displayed rearrangements in the distribution of actin and uvomorulin. After 24 h the cells had reorganized in two layers, one facing the other, with opposite orientations. We found that in approximately 15 to 20% of the cells within a confluent monolayer alpha 1 and beta 1 integrin subunits were localized in a subdomain of the apical plasma membrane, other than on the basolateral surface, as they normally are. By double immunofluorescence, after addition of diluted collagen solutions, we were able to detect collagen fibers that were bound to these integrin-containing apical subdomains. The addition of anti-beta 1 antibodies to the apical domain significantly delayed the drop in transepithelial resistance induced by the collagen gel. These data suggest that members of the beta 1 integrin family that are expressed on the apical domain may act as receptors for collagen fibers and may play a role in promoting changes in cell orientation