Differentiation of human myeloid leukemia cell lines induced by tumor-promoting phorbol ester (TPA). II. Electrophoretic patterns of metabolically- and cell surface radiolabeled proteins and glycoproteins.

Electrophoretic patterns of cell surface proteins and cell surface sialogalactoproteins from human myeloid leukemia cell lines HL-60, ML-1, ML-2 and ML-3 before and after induction of morphological differentiation by 12-O-tetradecanoylphorbol-13-acetate (TPA), have been compared. Minor quantitative cell surface protein alterations associated with TPA-induced differentiation have been observed as follows: decrease of a 150-160k glycoprotein on some TPA-induced myeloid cell lines, increase of a 50k glycoprotein and alteration of a 95k glycoprotein associated with the induction of differentiation by TPA. Electrophoretic patterns of 35S-methionine metabolically radiolabeled cell proteins revealed minor but distinct quantitative differences in several proteins, such as increased labeling of 180k, 160k and 130k proteins and decreased expression of 83k, 76k and 63k proteins on TPA-induced HL-60 cells. Two-dimensional electrophoretic analysis of 35S-methionine metabolically radiolabeled cell proteins revealed at least 17 proteins more intensively labeled and 13 proteins with decreased intensity of labeling on TPA-induced HL-60 cells compared to uninduced HL-60 cells.