Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation.
A plastic adherent variant line (ESb-M) of a highly invasive and metastatic murine T cell lymphoma (ESb) was found to have lost its metastatic potential while still being tumorigenic in normal syngeneic hosts. The variant retained most of its ESb-derived antigenic and biochemical characteristics but differed at binding sites for certain lectins with specificity for terminal N-acetylgalactosamine residues. Whereas such sites were masked by sialic acid on metastatic ESb cells, they became unmasked on the adherent variant line. Metastatic revertants of ESb-M cells did not express the respective lectin receptor sites because these were again masked by sialic acid. It is suggested that the masking of specific lectin receptors sites on the tumor cell surface is of crucial importance for metastatis. If freely exposed, these sites may change adherence characteristics of the cells possibly not only in vitro (to plastic) but also in vivo.
D000818:Animals; D002448:Cell Adhesion; D002460:Cell Line; D006023:Glycoproteins / Q000032:analysis; D008223:Lymphoma / Q000473:pathology*; D008565:Membrane Proteins / Q000032:analysis; D051379:Mice; D009362:Neoplasm Metastasis; D009363:Neoplasm Proteins / Q000032:analysis; D012794:Sialic Acids / Q000502:physiology*
D006023:Glycoproteins; D008565:Membrane Proteins; D009363:Neoplasm Proteins; D012794:Sialic Acids