Decrease in CuZn‐superoxide dismutase mRNA level during differentiation of human monocytic and promyelotic leukemia cells

Saito, Hiroyuki; Kuroki, Toshio; Nose, Kiyoshi

doi:10.1016/0014-5793(89)80634-9

Cited by 10 publications

(4 citation statements)

References 30 publications

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“…The decrease in the level of mRNA for Cu.Zn-SOD was accompanied by the development of myeloid dif ferentiation. Similar observations have recently been reported [31,32]. Considering the fact that macro phages and granulocytes generate large quantities of supcroxidc anion they would seem to require a high level of SOD to defend themselves.…”

Section: Discussionsupporting

confidence: 66%

Changes in CuZn-Superoxide Dismutase Gene during Induced Erythroid and Myeloid Differentiation

Tomoda

Nomura²,

Kurashige³

et al. 1991

Acta Haematol

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We investigated the alteration of CuZn-superoxide dismutase during erythroid and myeloid differentiation in order to elucidate its physiological significance in different types of cells. We measured enzyme activity and mRNA levels of superoxide dismutase in the process of differentiation to erythroid cells or myeloid cells. When human leukemia K562 cells are incubated in the presence of 80 μM hemin, benzidine-positive cells appear on day 1 and 80% of the cells become positive on day 5. During hemin-induced erythroid differentiation, CuZn-superoxide dismutase activity increases 3.5-fold of the initial value and mRNA for CuZn-superoxide dismutase increases prior to the activity to the same extent. On the other hand, when human pro-myelocytic leukemia HL-60 cells are incubated in the presence of 1.3% dimethyl sulfoxide, nitroblue tetrazoli-um-positive cells reach approximately 90% on day 5. During dimethyl sulfoxide-induced myeloid differentiation, the activity of CuZn-superoxide dismutase decreases below 15% of the initial value on day 5 and mRNA for CuZn-superoxide dismutase decreases as well. The results indicate that the synthesis of superoxide dismutase is linked with either the erythroid or myeloid differentiation program.

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Section: Discussionsupporting

confidence: 66%

Changes in CuZn-Superoxide Dismutase Gene during Induced Erythroid and Myeloid Differentiation

Tomoda

Nomura²,

Kurashige³

et al. 1991

Acta Haematol

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“…Diminished CuZnSOD mRNA may be a hallmark of differentiation in these cells. On the other hand, human B-cell leukaemia cells or normal diploid fibroblasts treated with phorbol retained their concentrations of CuZnSOD mRNA (Saito et al, 1989). Both CuZnSOD mRNA and MnSOD mRNA concentrations go down in Morris hepatomas, the decline correlating with the degree of differentiation (Galeotti et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Regulation of Cu,Zn superoxide dismutase with copper. Caeruloplasmin maintains levels of functional enzyme activity during differentiation of K562 cells

Percival

Harris

1991

Biochemical Journal

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K562 cells, a human erythroleukaemic cell line blocked for differentiation, commit towards erythrocytes when exposed to haemin (20 microM). The cells synthesize fetal haemoglobins and show site-specific binding of caeruloplasmin, a plasma copper protein. These events are set into motion by haemin. On the assumption that the binding of caeruloplasmin could reflect a greater need for copper, we sought to determine whether the transfer of 67Cu from caeruloplasmin was accelerated in haemin-induced compared with non-induced K562 cells. Cu,Zn superoxide dismutase (CuZnSOD) was the recipient. Haemin induction caused the K562 cells to lose CuZnSOD activity. By 96 h, the level of SOD activity was less than 60% of that of non-induced cells. The loss was confined entirely to the CuZn form, MnSOD activity staying essentially unchanged. Although CuZnSOD activity declined with the haemin induction, the incorporation of [4,5-3H]lysine into immunoprecipitable CuZnSOD protein was unaffected. There was also no change in CuZnSOD mRNA concentration in haemin-induced cells. Thus a loss of enzyme did not correlate with a decline in the synthesis de novo of CuZnSOD protein. When 48 h-induced cells were transferred to a medium supplemented with 0.2 microM-caeruloplasmin, CuZnSOD activity was restored to control levels in 24 h. Caeruloplasmin also stimulated the incorporation of [3H]lysine into immunoprecipitable CuZnSOD protein. Caeruloplasmin addition may have affected a post-translational regulatory site for CuZnSOD biosynthesis, possibly by providing copper for the newly synthesized enzyme.

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“…Macrophage diVerentiation has also been shown to involve secretion and activation of collagenase MMP-9 (Xie et al, 1998), a zinc-and calcium-binding protein, and to require production and cell-surface display of 5 1 integrin (Laouar et al, 1999), whose activity is modulated by manganese (Davis and Camarillo, 1993). Intracellularly, enzymes such as CuZn-superoxide dismutase play a role (Saito et al, 1989), as do numerous transcription factors, many of which contain zinc-Wnger motifs (Ventura and Maioli, 2001). By understanding how endogenous trace metal concentrations and distributions change as the diVerentiation process proceeds, it may be possible to more fully understand how metals are involved in the acquisition of the mature phenotype.…”

Section: Introductionmentioning

confidence: 99%

Regulatory properties and cellular redistribution of zinc during macrophage differentiation of human leukemia cells

Glesne

Vogt

Mäser

et al. 2006

Journal of Structural Biology

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Decrease in CuZn‐superoxide dismutase mRNA level during differentiation of human monocytic and promyelotic leukemia cells

Cited by 10 publications

References 30 publications

Changes in CuZn-Superoxide Dismutase Gene during Induced Erythroid and Myeloid Differentiation

Changes in CuZn-Superoxide Dismutase Gene during Induced Erythroid and Myeloid Differentiation

Regulation of Cu,Zn superoxide dismutase with copper. Caeruloplasmin maintains levels of functional enzyme activity during differentiation of K562 cells

Regulatory properties and cellular redistribution of zinc during macrophage differentiation of human leukemia cells

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