Cationic ferritin binding sites and surface charge densities of transformed cells.
Bioelectric surface properties of the high and low tumor-producing cell lines, NCTC 2472 and NCTC 2555, respectively, were determined by cationic ferritin binding and the electrophoretic mobility of intact cells. Measurements of anionic sites were bases on the number of cationic ferritin particles per 0.01 mu 2 that were electronically tagged and counted by an image analyzer. The average particle count was 45 for the control "high" cells and 34 for the control "low" cells. The surface charge densities, expressed as electrostatic units per cm-2 x 10(-13) were 2.34 and 1.18 at 50 V (2 mA) for the "high" and "low" control cells, respectively. Enzymic cleavage of sialic acid and other carbohydrate moieties resulted in up to an 81% reduction in the charge densities and a 57% reduction of the anionic sites of the "high" cells. The electrophoretic mobility of cells with bound cationic ferritin showed that up to 50% of the exposed anionic sites fail to bind cationic ferritin. Preliminary findings on the particle size/distribution by image analysis showed wide ranges in both particle size and interparticle distances that may limit cationic ferritin binding.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology / Q000648:ultrastructure; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D003238:Connective Tissue; D004586:Electrophoresis; D005293:Ferritins / Q000378:metabolism*; D006026:Glycoside Hydrolases; D006651:Histocytochemistry; D033862:Iron-Binding Proteins; D051379:Mice; D008854:Microscopy, Electron; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013499:Surface Properties
D033862:Iron-Binding Proteins; D011956:Receptors, Cell Surface; C027293:ferritin receptor; D005293:Ferritins; D006026:Glycoside Hydrolases