Expression and function of beta 1 integrins on adherent and nonadherent Ehrlich ascites tumor cells

Experimental Cell Research
Z SongI J Goldstein

Abstract

Differences in integrin-mediated cell-matrix adhesion between two types of Ehrlich ascites tumor (EAT) cells, adherent and nonadherent EAT cells, have been studied. The adherent EAT (a-EAT) cells adhere to and spread on laminin- or fibronectin-coated plates, whereas the nonadherent EAT (na-EAT) cells do not. The adhesion of a-EAT cells to laminin or fibronectin requires the presence of both Ca2+ and Mg2+. Anti-human fibronectin receptor (alpha 5 beta 1 integrin) antiserum blocks a-EAT cells from adhering to both laminin- and fibronectin-coated plates. An RGD-containing peptide (GRGDSP) inhibits the adhesion of a-EAT cells to fibronectin-coated but not to laminin-coated plates. Taken together, these data suggest that a-EAT cells interact with laminin and fibronectin via different beta 1 integrins. As determined by immunofluorescence flow cytometry assay, both a-EAT and na-EAT cells express similar amounts of surface antigen(s) recognized by the same anti-alpha 5 beta 1 integrin polyclonal antibody that blocks a-EAT cells from adhering to laminin and fibronectin. The alpha 5 and beta 1 subunits expressed on both types of EAT cells appear to have the same molecular weight when analyzed by immunoblotting. The same amount of 125I-la...Continue Reading

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