Expression of glycolytic isozymes in rat thymocytes during cell cycle progression

Netzker, Roland; Hermfisse, Ulrich; Wein, Karl-Heinz; Brand, Karl

doi:10.1016/0167-4889(94)90270-4

Cited by 20 publications

(11 citation statements)

References 23 publications

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“…The parallel increases of both the activities [1] and the mRNA levels [5,6] of aldolase A and pyruvate kinase M2 observed in mitogen-stimulated rat thymocytes during the Sphase of the cell cycle (44-48 h after stimulation) suggest that the induction of these enzymes is caused by enhanced transcription (Fig. 1).…”

Section: Resultsmentioning

confidence: 90%

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Differences in DNA‐binding efficiency of Sp1 to aldolase and pyruvate kinase promoter correlate with altered redox states in resting and proliferating rat thymocytes

et al. 1996

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Thymocytes induce their glycolytie enzymes as they undergo transition from the resting to the proliferating state. Corresponding increases in mRNA levels point to a transcriptional regulation. Electrophoretic mobility shift assays revealed that the DNA-binding efficiency of Spl is increased when nuclear extracts from proliferating compared to resting rat thymocytes were used. Here we demonstrate that hydrogen peroxide, added to nuclear extract from proliferating cells, decreases the Spl DNA-binding activity, whereas in nuclear extracts from resting cells dithioerythritol fully restores DNA-binding efficiency. Moreover we show that in contrast to resting thymocytes, production of reactive peroxide anions upon priming with phorbol 12-myristate 13-acetate is nearly abolished in the proliferating cells. From these results we propose that reactive oxygen intermediates affect the interaction of the Spl transcription factor with its consensus sequence and subsequently regulate glycolytic gene expression.

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Section: Resultsmentioning

confidence: 90%

“…Cell division is completed after 72 h of culture with the S-phase peaking between 44 h and 48 h. Induction of glycolytic enzymes has been shown to be well correlated with controlled proliferation [2]. In addition, similar increases in the mRNA levels of these enzymes have been reported [5,6], pointing to a transcriptional regulation.…”

Section: Introductionmentioning

confidence: 99%

Differences in DNA‐binding efficiency of Sp1 to aldolase and pyruvate kinase promoter correlate with altered redox states in resting and proliferating rat thymocytes

et al. 1996

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“…Indeed, the GAPDH gene and protein are actively regulated on cell proliferation. [19][20][21] GAPDH is the target of different transcription factors, and various control regions have been identified in its promoter, including hypoxia and insulinresponsive elements 22,23 ( Figure 1). In the context of cancer, hypoxia is of particular interest.…”

Section: Mechanisms Of Gapdh Regulationmentioning

confidence: 99%

Novel roles for GAPDH in cell death and carcinogenesis

2009

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Growing evidence points to the fact that glucose metabolism has a central role in carcinogenesis. Among the enzymes controlling this energy production pathway, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is of particular interest. Initially identified as a glycolytic enzyme and considered as a housekeeping gene, this enzyme is actually tightly regulated and is involved in numerous cellular functions. Particularly intriguing are recent reports describing GAPDH as a regulator of cell death. However, its role in cell death is unclear; whereas some studies point toward a proapoptotic function, others describe a protective role and suggest its participation in tumor progression. In this study, we highlight recent findings and discuss potential mechanisms through which cells regulate GAPDH to fulfill its diverse functions to influence cell fate.

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“…The activity of PK, the key enzyme controlling the exit of the glycolytic pathway, determines the relative amount of glucose that is channeled into synthetic processes or used for glycolytic energy production (6,8). Proliferating mammalian cells express the M 2 type isoenzyme of PK (M2-PK) (9), and expression of M2-PK is cell cycle regulated in proliferating rat thymocytes (10). M2-PK occurs in an active tetrameric and a less active dimeric form (8,11,12), and the switch between both forms, which is controlled by the glycolytic phosphometabolite fructose 1,6-bisphosphate (FBP) (8), regulates the glycolytic flux in tumor cells.…”

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Modulation of type M ₂ pyruvate kinase activity by the human papillomavirus type 16 E7 oncoprotein

Zwerschke

Mazurek

Massimi

et al. 1999

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

241

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We report here that the E7 oncoprotein encoded by the oncogenic human papillomavirus (HPV) type 16 binds to the glycolytic enzyme type M 2 pyruvate kinase (M2-PK). M2-PK occurs in a tetrameric form with a high affinity to its substrate phosphoenolpyruvate and a dimeric form with a low affinity to phosphoenolpyruvate, and the transition between both conformations regulates the glycolytic f lux in tumor cells. The glycolytic intermediate fructose 1,6-bisphosphate induces the reassociation of the dimeric to the tetrameric form of M2-PK. The expression of E7 in an experimental cell line shifts the equilibrium to the dimeric state despite a significant increase in the fructose 1,6-bisphosphate levels. Investigations of HPV-16 E7 mutants and the nononcogenic HPV-11 subtype suggest that the interaction of HPV-16 E7 with M2-PK may be linked to the transforming potential of the viral oncoprotein.Unicellular organisms have a variety of sensing mechanisms to adapt the cell proliferation rate to variations in their environmental nutrient supply. Several gene products, like the ras or cdc kinase proteins, which are involved in nutrient sensing in yeast (1, 2), are conserved during the evolution of multicellular organisms, and in mammals, these gene products often are altered in tumors. Despite our knowledge about the protein machinery regulating cell proliferation increasing tremendously over the recent years, we are still at the beginning to understand how nutrients contribute to proliferation control in multicellular organisms. There is, however, quite good evidence that phosphometabolites derived from both glycolysis (for recent review, see ref.3) and the pentose phosphate pathway (ref. 4 and references therein) provide some of the signals linking metabolic conditions to cell proliferation. The glycolytic phosphometabolites, which are necessary for the biosynthesis of nucleic acids, phospholipids, and complex carbohydrates, are up-regulated in the G 1 phase of the cell cycle (for recent review, see

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Expression of glycolytic isozymes in rat thymocytes during cell cycle progression

Cited by 20 publications

References 23 publications

Differences in DNA‐binding efficiency of Sp1 to aldolase and pyruvate kinase promoter correlate with altered redox states in resting and proliferating rat thymocytes

Differences in DNA‐binding efficiency of Sp1 to aldolase and pyruvate kinase promoter correlate with altered redox states in resting and proliferating rat thymocytes

Novel roles for GAPDH in cell death and carcinogenesis

Modulation of type M ₂ pyruvate kinase activity by the human papillomavirus type 16 E7 oncoprotein

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Expression of glycolytic isozymes in rat thymocytes during cell cycle progression

Cited by 20 publications

References 23 publications

Differences in DNA‐binding efficiency of Sp1 to aldolase and pyruvate kinase promoter correlate with altered redox states in resting and proliferating rat thymocytes

Differences in DNA‐binding efficiency of Sp1 to aldolase and pyruvate kinase promoter correlate with altered redox states in resting and proliferating rat thymocytes

Novel roles for GAPDH in cell death and carcinogenesis

Modulation of type M 2 pyruvate kinase activity by the human papillomavirus type 16 E7 oncoprotein

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Modulation of type M ₂ pyruvate kinase activity by the human papillomavirus type 16 E7 oncoprotein