The relationship between purines, pyrimidines, nucleosides, and glutamine for fibroblast cell proliferation

Engström, Wilhelm; Zetterberg, Anders

doi:10.1002/jcp.1041200218

Cited by 58 publications

(26 citation statements)

References 40 publications

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“…Such changes could contribute to the differences in cell kinetics observed by us and others (6,18). Purine supplementation has been shown to accelerate and sharpen the kinetics of entry into S phase in 3T3 cells (8,17), and we have confirmed this effect (data not shown). In the medium that we used, the purine requirement is satisfied by the addition of Ham F12 medium, which contains hypoxanthine.…”

Section: Growth-dependent Synthesis Of C-myc Proteinssupporting

confidence: 82%

Growth-dependent synthesis of c-myc-encoded proteins: early stimulation by serum factors in synchronized mouse 3T3 cells.

Persson¹,

Gray²,

Godeau³

1985

Mol. Cell. Biol.

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Synthesis of the c-myc gene product was measured during the entire cell cycle of subconfluent mouse 3T3 cells with an antibody raised against a human c-myc synthetic peptide. The antiserum recognized two mouse c-myc-encoded proteins with apparent molecular weights in sodium dodecyl sulfate-polyacrylamide gels of 62,000 and 60,000. Cell-derived p62 was compared with the mouse c-myc gene product synthesized in vitro. Immunoprecipitation, electrophoretic analyses, and peptide mapping provided evidence that p62 is encoded by the mouse c-myc gene. The rate of synthesis of the c-myc proteins was tightly coupled to the cellular growth state of nontransformed A31 3T3 cells, but not to that of their benzo(a)pyrene-transformed derivative (BPA31). Furthermore, the synthesis of the c-myc proteins was stimulated by the exposure of confluent, density-arrested A31 cells to platelet-derived growth factor or fibroblast growth factor. Tightly synchronized cell populations were obtained on the addition of serum factors to subconfluent, serum-deprived A31 cells, and c-myc expression could be monitored for more than one complete cell cycle. One hour after stimulation the steady-state level of the 2.2 kilobase c-myc transcript increased 30-fold relative to that of quiescent cells and decreased thereafter to the level observed during exponential growth. The rate of synthesis of c-myc-encoded proteins was determined by immunoprecipitation after a 2-h labeling period. After an initial sevenfold increase detectable 2 h after serum addition, the rate of synthesis remained constant throughout the rest of the cell cycle. No further changes associated with the late prereplicative period, S phase, G2, or mitosis could be demonstrated. Pulse-chase and long-term labeling experiments revealed different half-lives for the two c-myc-encoded proteins. The half-lives of the c-myc proteins, however, were independent of the cellular growth state. The sustained expression observed throughout the cell cycle suggests that the growth-related function of c-myc may be required during the GO-GI transition and in all phases of the cycle of the growing cell.

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Section: Growth-dependent Synthesis Of C-myc Proteinssupporting

confidence: 82%

Growth-dependent synthesis of c-myc-encoded proteins: early stimulation by serum factors in synchronized mouse 3T3 cells.

Persson¹,

Gray²,

Godeau³

1985

Mol. Cell. Biol.

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“…Glutamine is required for proliferation of many cell types in culture (Engstrom and Zetterberg, 1984). Such a requirement for A549 cells was first tested in the present study.…”

Section: Resultsmentioning

confidence: 99%

Glutathione stimulates A549 cell proliferation in glutamine‐deficient culture: The effect of glutamate supplementation

Kang

Feng

Hatcher

1994

Journal Cellular Physiology

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Extracellular glutathione (GSH) is degraded by an external cell-surface enzyme, gamma-glutamyltranspeptidase (gamma-GT). The products are transported into cells to participate in important cellular processes. In the present study, we tested the hypothesis that extracellular GSH is a source of glutamic acid for cells that express gamma-GT. Under a glutamine-deficient culture condition, the extracellular GSH-supplemented glutamic acid would enhance intracellular glutamine synthesis, thereby stimulating cell proliferation. Human lung carcinoma A549 cells were cultured in glutamine-deficient Dulbecco's modified Eagle medium, and they did not proliferate unless glutamine was supplemented. Extracellular GSH, however, provoked a partial proliferation. The GSH effect correlated with a high level of gamma-GT activity and an increased intracellular level of glutamic acid. A constituent amino acid of GSH, glutamic acid but not cysteine, produced the same growth-stimulatory effect as GSH. Furthermore, neither oxothiazolidine-4-carboxylate (OTC), a cellular cysteine-delivery compound, nor cysteinylglycine, a dipeptide released from the gamma-GT reaction, stimulated cell proliferation. Moreover, buthionine sulfoximine (BSO), a selective inhibitor of gamma-glutamylcysteine synthetase, enhanced the GSH growth stimulatory effect, suggesting that increased cellular GSH synthesis does not correlate with cell growth stimulation. The results obtained demonstrated that glutamine is required for A549 cell proliferation and exogenous GSH partially substitutes for the growth stimulatory action of glutamine. It also suggests that the glutamic acid rather than the cysteine released from the GSH is responsible for the cell proliferation.

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“…Our results-that nucleotides did not influence Caco-2 cells proliferation under normal culture conditions and that they did promote cell proliferation under glutamine-depleted conditions-were consistent with their fi nding. Glutamine depletion from culture medium markedly inhibits DNA synthe sis and cell proliferation because of the retardation in ATP production (14,22). Therefore the level of glutamine in the medium seems to be important for cell proliferation and differentiation.…”

Section: Discussionmentioning

confidence: 99%

In Vitro and In Vivo Effects of Exogenous Nucleotides on the Proliferation and Maturation of Intestinal Epithelial Cells.

Sato

Nakano

Kawakami

et al. 1999

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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The relationship between purines, pyrimidines, nucleosides, and glutamine for fibroblast cell proliferation

Cited by 58 publications

References 40 publications

Growth-dependent synthesis of c-myc-encoded proteins: early stimulation by serum factors in synchronized mouse 3T3 cells.

Growth-dependent synthesis of c-myc-encoded proteins: early stimulation by serum factors in synchronized mouse 3T3 cells.

Glutathione stimulates A549 cell proliferation in glutamine‐deficient culture: The effect of glutamate supplementation

In Vitro and In Vivo Effects of Exogenous Nucleotides on the Proliferation and Maturation of Intestinal Epithelial Cells.

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