Thioredoxin reductase is one of the selenoproteins in both promyelocytic and granulocytic HL-60 cells |
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Authors: | Qiomg Liu JØrgen Clausen |
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Institution: | (1) Department of Life Sciences and Chemistry, Roskilde University, DK-4000 Roskilde, Denmark |
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Abstract: | Human leukemia promyelocytic HL-60 cells differentiate into granulocytes when cultured with 1.25% dimethyl sulfoxide for 3
d. The radioactive Na2
75SeO3 incorporation and the amount of total proteins were interrelated in both promyelocytic and granulocytic HL-60. Promyelocytic
cells had four times higher75Se incorporation and 34% more protein synthesis than the granulocytic cells on the fifth culturing day. The enzyme activities
of glutathione peroxidase (GSH-Px, E.C. 1.11.1.9) and thioredoxin reductase (TrxR, E.C. 1.6.4.5) in both types of cells increased
significantly and approached steady stage on the third day. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE)
analysis and autoradiography of the proteins from the cells revealed three proteins with molecular weights of57, 28, and 21 kDa, respectively. These three75Se-labeled proteins were present in both types of cells. The proteins from HL-60 cells were separated by DEAE-Sepharose and
2′5′-ADP-Sepharose columns. The purified 57-kDa protein had TrxR activity of 0.744 Μmol 5′-thionitrobenzoic acid (TNB) formed/min/mg
protein and two isoelectric points at pH 5.9 and 6.0. These results suggest that TrxR is one of the selenoproteins in both
promyelocytic and granulocytic HL-60 cells. |
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Keywords: | Selenoprotein promyelocytic HL-60 cells granulocytic HL-60 cells granulocytes thioredoxin reductase (TrxR) glutathione peroxidase (GSH-Px) phagocytosis |
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