Negative control of hemoglobin production in somatic cell hybrids due to heme deficiency.

Benoff, Susan; Bruce, Sarah A.; Skoultchi, Arthur I.

doi:10.1073/pnas.75.9.4354

Proc. Natl. Acad. Sci. U.S.A.

1978

DOI: 10.1073/pnas.75.9.4354

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Negative control of hemoglobin production in somatic cell hybrids due to heme deficiency.

Susan Benoff¹,

Sarah A. Bruce²,

Arthur I. Skoultchi³

Abstract: In somatic cell hybrids formed by the fusion of mouse erythroleukemic cells with mouse primary bone marrow cells, retention of the X chromosome contributed by the bone marrow parent is correlated with inhibition of hemoglobin accumulation in response to dimethyl sulfoxide. The inhibition of hemoglobin accumulation is not due to the absence of globin mRNA. Dimethyl sulfoxide-treated hybrid cells accumulate polyribosomal globin mRNA to levels comparable to those of the parental erythroleukemic cells under the sa… Show more

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Cited by 18 publications

(1 citation statement)

References 25 publications

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“…Besides its role in translational control in reticulocytes (1)(2)(3) it also participates in the induction of globin mRNA and in erythroid differentiation (14)(15)(16)(17)(18). Recently it was reported that hemin enhances the differentiation of mouse 3T3 cells to adipocytes (19).…”

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confidence: 99%

Translational control of catalase synthesis by hemin in the yeast Saccharomyces cerevisiae

Hamilton¹,

Hofbauer²,

Ruis³

1982

Proc. Natl. Acad. Sci. U.S.A.

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mRNA-dependent cell-free protein synthesis systems were prepared from a heme-deficient ole3 mutant of the yeast Saccharomyces cerevisiae grown either in the absence or in the presence of the heme precursor δ-aminolevulinate. When supplemented with total yeast mRNA, the two systems—from heme-deficient and from heme-containing cells—translate most mRNAs with comparable efficiencies. mRNAs coding for the hemoproteins catalase T and catalase A, however, are translated at a low rate by the system from heme-deficient cells whereas their translation in the system from heme-containing cells is comparable to that observed in a heterologous in vitro system from wheat germ. Addition of 10 μM hemin to the system from heme-deficient cells stimulates translation of catalase mRNAs significantly. Control experiments showed that the results obtained cannot be explained by specific proteinase or nuclease action. Together with previous findings indicating lack of translation of catalase T mRNA in heme-deficient cells in vivo , the results demonstrate that specific control of yeast catalase formation occurs at the level of translation.

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mentioning

confidence: 99%

Translational control of catalase synthesis by hemin in the yeast Saccharomyces cerevisiae

Hamilton¹,

Hofbauer²,

Ruis³

1982

Proc. Natl. Acad. Sci. U.S.A.

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The role of Heme in the regulation of the late program of friend cell erythroid differentiation

Mager

Bernstein

1979

Journal Cellular Physiology

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The addition of a chemical inducer, such as dimethylsulfoxide (DMSO), to cultures of mouse Friend erythroleukemic cells results in the induction of a number of late erythroid events, including the accumulation of globin mRNA, the inducation of hemoglobin synthesis, the appearance of erythrocyte membrane antigens (EMA), and the cessation of cell division. The experiments presented in this study demonstrate that heme is necessary but not sufficient for the loss of proliferative capacity associated with DMSO-induced Friend cell differentiation, whereas the accumulation of globin mRNA and EMA can occur in the absence of heme synthesis or heme itself. These conclusions were reached by selectively inhibiting heme synthesis in DMSO-treated cells in two independent ways: (i) Inducible cells were treated with 3-amino-1,2,4-triazole (AT), a drug which inhibits the induction of heme synthesis in Friend cells in a dose-dependent manner. Treatment of inducible Friend cells with 1.5% DMSO for five days caused the plating efficiency in methyl cellulose to decrease to 1% of that in untreated cultures. However, treatment of the cells with DMSO plus AT almost totally prevented this decrease in plating efficiency. The addition of exogenous hemin, which alone had no significant effect on plating efficiency, largely reversed the effect of AT in DMSO-treated cells, reducing the plating efficiency to below 5%. In contrast to the marked effects of AT on the proliferative capacity of differentiating Friend cells, the levels of globin mRNA and EMA were only partially decreased in cells treated with DMSO plus AT, compared to cells treated with DMSO alone. (ii) The relationship between heme synthesis, terminal cell division, and the induction of globin mRNA was investigated further through the use of non-inducible Friend cell variant clones. One such non-inducible clone, M18, appears to be a phenotypic analog of inducible cells treated with DMSO plus AT. Clone M18 did not accumulate heme or hemoglobin, as detected by benzidine staining, nor lose its proliferative capacity in response to DMSO. However, globin mRNA was induced by DMSO in this clone. Treatment of clone M18 with DMSO plus hemin overcame the block in hemoglobin accumulation suggesting that M18 has a defect in the induction of heme biosynthesis. In addition, exposure of M18 cells to DMSO plus hemin caused a gradual decrease in plating efficiency which was not due to non-specific toxicity. Prior incubation of M18 cells in DMSO for three to five days was necessary before hemin caused a rapid loss of proliferative capacity. Thus, these results, in agreement with the AT studies on inducible Friend cells and previous studies on the induction of EMA in clone M18, indicate that there may be both heme-dependent and heme-independent events in the program of Friend cell differentiation.

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Phorbol ester tumor promoters block the transition from the early to the heme‐dependent late program of friend cell differentiation

Mager

Bernstein

1980

Journal Cellular Physiology

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In this study, the mechanism of inhibition of differentiation of Friend erythroleukemia cells by the phorbol ester tumor promoter, 12-O-tetradecanoylphorbol-13-acetate (TPA), has been examined. These studies indicate that some early events associated with Friend cell differentiation, including an early change in 86Rb+ transport and a decrease in cell volume, still occur in the presence of TPA. However, several late events in the program of Friend cell differentiation, including the induction of heme synthesis and the loss of proliferative capacity, are inhibited by TPA. These effects of TPA can be reversed by hemin, which alone does not induce Friend cells to differentiate. The addition of hemin to cultures grown in the presence of inducer plus TPA for several days results in the rapid restoration of hemoglobin synthesis, and also causes a parallel decrease in colony-forming ability. These results suggest that tumor promoters may inhibit only heme-dependent events, rather than the entire program of Friend cell differentiation.

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Negative control of hemoglobin production in somatic cell hybrids due to heme deficiency.

Cited by 18 publications

References 25 publications

Translational control of catalase synthesis by hemin in the yeast Saccharomyces cerevisiae

Translational control of catalase synthesis by hemin in the yeast Saccharomyces cerevisiae

The role of Heme in the regulation of the late program of friend cell erythroid differentiation

Phorbol ester tumor promoters block the transition from the early to the heme‐dependent late program of friend cell differentiation

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