Increase of the glycolytic rate in human resting fibroblasts following serum stimulation

Bruni, Paola; Farnararo, Marta; Vasta, Valeria; D'Alessandro, Antonino

doi:10.1016/0014-5793(83)80412-8

Cited by 25 publications

(12 citation statements)

References 11 publications

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“…A stimulation of glycolysis can also be observed following exposure of quiescent cells to growth factors (3,4) and tumor promoters such as phorbol esters (5,6). The mechanism of this stimulation is unknown.…”

mentioning

confidence: 98%

Phorbol 12-myristate 13-acetate and insulin increase the concentration of fructose 2,6-bisphosphate and stimulate glycolysis in chicken embryo fibroblasts.

Boscá¹,

Rousseau²,

Hue³

1985

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

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mentioning

confidence: 98%

Phorbol 12-myristate 13-acetate and insulin increase the concentration of fructose 2,6-bisphosphate and stimulate glycolysis in chicken embryo fibroblasts.

Boscá¹,

Rousseau²,

Hue³

1985

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

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“…One of these biochemical changes is an increased rate of glycolysis, which is also typical of many tumours and established lines of transformed cells (Weinhouse, 1976), and is observed after exposure of quiescent cells to mitogens (Diamond et al, 1978;Bruni et al, 1983) and tumour promoters (Driedger & Blumberg, 1977;O'Brien et al, 1979). This results in part from a stimulation of 6-phosphofructo-1-kinase (PFK-1) (Singh et al, 1974).…”

Section: Introductionmentioning

confidence: 99%

Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts. Novel mechanism for the stimulation of glycolysis by retroviruses

Boscá¹,

Mojena²,

Ghysdael³

et al. 1986

Biochemical Journal

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The concentration of fructose 2,6-bisphosphate and the activity of 6-phosphofructo-2-kinase are increased after infection of chick-embryo fibroblasts with the Rous sarcoma virus, or with a temperature-sensitive mutant of this virus at the permissive, but not at the non-permissive, temperature. This is observed after transformation by retroviruses carrying either the v-src or v-fps, but not the v-mil and/or v-myc, oncogenes.Comparison of the effects of the Rous sarcoma virus with those of phorbol myristate acetate on fructose 2,6-bisphosphate suggests that both result from the stimulation of a step which is rate-limiting for 6-phosphofructo-2-kinase activation and which is also controlled by protein kinase C.

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“…The levels of this metabolite increase in different proliferative states (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)39), and this change has been correlated with an increase in 6-phosphofructo-2-kinase activity (18 -24) and recently with an increase in mRNA levels (40,41). However, the mechanisms by which growth factors regulate 6PF2K/Fru-2,6-P 2 ase are still unclear.…”

Section: Discussionmentioning

confidence: 99%

“…Although extensive studies have been performed on the regulation of liver and muscle isoforms, this is not the case of F-type. Different reports have demonstrated that Fru-2,6-P 2 levels increase after stimulation of fibroblasts with fetal bovine serum, insulin, epidermal growth factor (EGF), or tumor promoter phorbol esters (12)(13)(14)(15)(16)(17)(18)(19)(20)(21). In some cases, the increase in this metabolite has been correlated with an increase in the V max of 6-phosphofructo-2-kinase activity (19 -24).…”

mentioning

confidence: 99%

Effect of Growth Factors on the Expression of 6-Phosphofructo2-kinase/Fructose-2,6-bisphosphatase in Rat-1 Fibroblasts

Joaquin

Salvadó

Bellosillo

et al. 1997

Journal of Biological Chemistry

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The activation of glycolytic flux is a biochemical characteristic of growing cells. Several reports have demonstrated the role of fructose 2,6-bisphosphate in this process. In this paper we show that the levels of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (6PF2K/Fru-2,6-P 2 ase) mRNA are modulated in response to serum and growth factors and this effect is due to regulation of its transcription rate. The modulation of the expression of this enzyme by growth factors differs according their mitogenic effect; both lysophosphatidic acid and epidermal growth factor, when added alone, increased the mRNA levels, but endothelin had no effect. Furthermore, cAMP, which acts as an antimitogenic signal in Rat-1 fibroblasts, produced a decrease in 6PF2K/ Fru-2,6-P 2 ase mRNA and inhibited the effects of lysophosphatidic acid and epidermal growth factor on 6PF2K/Fru-2,6-P 2 ase expression. PD 098059, a specific inhibitor of the activation of the mitogen-activated protein kinase, was able to prevent the effect of EGF on 6PF2K/Fru-2,6-P 2 ase gene expression. These results imply that activation of mitogen-activated protein kinase is required for the stimulation of the transcription of 6PF2K/Fru-2,6-P 2 ase by EGF.

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Increase of the glycolytic rate in human resting fibroblasts following serum stimulation

Cited by 25 publications

References 11 publications

Phorbol 12-myristate 13-acetate and insulin increase the concentration of fructose 2,6-bisphosphate and stimulate glycolysis in chicken embryo fibroblasts.

Phorbol 12-myristate 13-acetate and insulin increase the concentration of fructose 2,6-bisphosphate and stimulate glycolysis in chicken embryo fibroblasts.

Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts. Novel mechanism for the stimulation of glycolysis by retroviruses

Effect of Growth Factors on the Expression of 6-Phosphofructo2-kinase/Fructose-2,6-bisphosphatase in Rat-1 Fibroblasts

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