The activity of receptors specific for human transcobalamin II-Cobalamin (TC II-Cbl) were measured in virus-transformed lymphoblasts, hepatocytes (hepatoma) and diploid fibro lasts. In all three types of human cells the receptor activity increased as cells went from a resting phase to the most actively dividing phase. Receptor activity declined as cell division slowed. The changes in activity of lymphoblasts and hepatocytes were produced by changes in receptor number and not by changes in affinity between receptors and TC II-Cbl. The basis of the change in fibroblasts was not clear. The Cbl-dependent methionine synthetase activity of fibroblasts, in contrast, tended to be greatest when the cultures were confluent and replication had slowed. As the fibroblasts became senescent the receptor activity for TC II-Cbl declined and the fluctuations with the phase of the cell were blunted. However, the release of apo TC II from the cells was maintained. These observations must be taken into consideration when the respective cells are used as models. Even more important are the implications of the observations of the changes in receptor activity for TC II-Cbl for the regulation of the entry of Cbl into cells.

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We show that hydroxocobalamin bound to human serum albumin can dissociate and bind to transcobalamin II present in serum. Human liver cells in culture exposed to hydroxocobalamin bound to albumin incorporated less of the vitamin than when similar amounts of unbound hydroxocobalamin or cyanocobalamin were present. In the presence of transcobalamin II, a 4.5-fold increase in cellular uptake occurred, but this amount was less than when hydroxocobalamin or cyanocobalamin were added to transcobalamin II. These results indicate that albumin, by binding hydroxocobalamin, can alter the dynamics of binding to transcobalamin II and the subsequent cellular incorporation of this form of the vitamin.