Cell surface biochemical and metastatic properties of Lens culinaris hemagglutinin-binding variants of a murine large cell lymphoma.

Using a low metastatic potential parental (P) line of the murine large cell lymphoma RAW117 and a highly metastatic in vivo-selected liver-colonizing subline (H10), we examined the relationship between cell surface glycoprotein expression and metastasis. The highly metastatic H10 cells showed loss of the major RNA tumor virus envelope glycoprotein gp70 and increased expression of a concanavalin A and Lens culinaris hemagglutinin (LcH)-binding glycoprotein of Mr approximately 15,000 (gp150) by lectin affinity chromatography and 125I-lectin staining of isolated RAW117 glycoproteins. When the amounts of cell surface LcH-binding components were determined on P and H10 cells, the mean amount of cell-bound LcH on H10 cells was significantly greater than on P cells. RAW117-P cells were sorted for low (PLcH-low) or high (PLcH-high) LcH binding using a fluorescence-activated cell sorter, or for binding to immobilized LcH, and the resulting cell sublines were analyzed for their metastatic properties by intravenous injection into BALB/c mice. The parental P cells formed few liver tumor nodules (median 0; range 0-8), as did the PLcH-low cells (median 0; range 0), whereas the high LcH-adherent P cells and the cells sorted for increased LcH binding, PLcH-high, were highly metastatic to the liver (median 200; range 156 to 200+). Analyses of gp150 and gp70 contents indicated higher amounts of gp150 but lower quantities of gp70 on PLcH-high cells than on PLcH-low or P cells. The results suggest that the amounts of cell surface gp150 and gp70 are important in determining the metastatic properties of RAW117 cells.