The synthesis of folate-binding protein in lymphocytes during transformation.
The blast transformation of human lymphocytes exposed to phytohaemagglutinin was associated with an increase in the intracellular concentration of a folate-binding protein. The protein was measured by a radioimmunoassay and by immunofluorescent microscopy using an antiserum raised against purified folate-binding protein prepared from chronic myelogenous leukaemia cells. Because it has been previously shown that protein-bound folate cannot function as a cofactor or substrate, the synthesis of this binder during some phase of the replicative cycle may serve to modulate folate-dependent RNA and DNA synthesis by controlling the concentration of free folate.
D002352:Carrier Proteins / Q000096:biosynthesis*; D002478:Cells, Cultured; D004247:DNA / Q000096:biosynthesis; D005455:Fluorescent Antibody Technique; D058973:Folate Receptors, GPI-Anchored; D005492:Folic Acid / Q000096:biosynthesis*; D006801:Humans; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000378:metabolism*; D010835:Phytohemagglutinins / Q000494:pharmacology; D011956:Receptors, Cell Surface
D002352:Carrier Proteins; D058973:Folate Receptors, GPI-Anchored; D010835:Phytohemagglutinins; D011956:Receptors, Cell Surface; D004247:DNA; D005492:Folic Acid