Association of phorbol ester-induced hyperphosphorylation and reversible regulation of transferrin membrane receptors in HL60 cells.
Phorbol diesters are tumor-promoting agents that cause differentiation of HL60 human leukemic cells and concomitantly alter surface transferrin-receptor expression [Rovera, G., Ferreo, D., Pagliardi, G. L., Vartikar, J., Pessano, S., Bottero, L., Abraham, S. & Lebman, D. (1982) Ann. N.Y. Acad. Sci. 397, 211-220]. Transferrin-receptor regulation is shown here to result from a rapid and reversible internalization process that is temporally associated with reversible increased phosphorylation (hyperphosphorylation) of the transferrin receptor. Such a reversible mechanism involving regulation of these surface proteins could result in the rapid generation of an early signal for HL60 cellular differentiation.
D002273:Carcinogens / Q000633:toxicity*; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D015470:Leukemia, Myeloid, Acute; D015240:Phorbol 12,13-Dibutyrate; D010703:Phorbol Esters / Q000633:toxicity*; D010704:Phorbols / Q000633:toxicity*; D010766:Phosphorylation; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D011990:Receptors, Transferrin; D014168:Transferrin / Q000378:metabolism*
D002273:Carcinogens; D010703:Phorbol Esters; D010704:Phorbols; D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin; D015240:Phorbol 12,13-Dibutyrate