STABLE EXPRESSION OF GP80 (TRPM-2, CLUSTERIN), A SECRETORY PROTEIN IMPLICATED IN PROGRAMMED CELL-DEATH, IN TRANSFECTED BHK-21-CELLS

The gp80 (TRPM-2, clusterin) cDNA cloned into an eucaryotic expression vector, was transfected into BHK-21 cells and stably transformed cell clones were obtained. Analysis of the gp80 glycoprotein complex produ ced in these cells demonstrated that the complex was glycosylated, pro teolytically processed and secreted in a way similar to the gp80 glyco protein complex expressed from the endogenous gene in MDCK cells. The analysis of the viability of the cells, the morphology and the state o f the DNA in the transfected cells was unchanged when compared with th e untransformed cells, demonstrating that the expression of the protei n failed to elicit any signs of apoptosis in this system.