ABSTRACT
The identification of surface structures involved in tumor cell recognition by LGL/NK cells of rIL-2-activated Natural Killer (NK) cells has been an area of active investigation. In vitro testing has shown that lymphokine activated killer (LAK) cells are fully capable of efficient lysis of fresh syngeneic solid tumor cells, leukemic blasts, or allogeneic or xenogeneic tumor cells while sparing, for the most part, fresh, uncultured normal cells. Laminin is a high molecular weight glycoprotein which constitutes approximately 30 to 50% of the noncollagenous glycoproteins in the matrix of the basement membrane. Immunoprecipitation of radiolabeled A-LAK cells, using laminin coupled to sepharose, again identified the p48 protein, indicating that the binding of matrix laminin to A-LAK cells was mediated through p48. Although adhesion and primary binding may occur in a weak and nonspecific fashion, upon secondary interaction of the T cell receptor with antigen, the target is said to be "recognized" and cytotoxicity proceeds.
