Effects of Hypoxia and Thyroid Hormone on mRNA Levels and Activity of Phosphoglycerate Mutase in Rabbit Tissues

González-Cinca, Nuria; Rivera, Francisca; Carreras, José; Climent, F.

doi:10.1159/000067934

Cited by 7 publications

(9 citation statements)

References 32 publications

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“…Subsequent research confirmed that hypoxia increases the PGAM1 activity in liver and brain, but does not affect the PGAM2 activity in muscle. 53 These results suggested that under reduced oxygen tension, the induction of PGAM1 may contribute to the regulation of the glycolytic flux and play a role in the adaptation of cells to hypoxia. 52,54 Moreover, hypoxia-inducible factor 1 (HIF-1), a master regulator of transcriptional responses to hypoxia, has been found to have a close connection with the Warburg effect, 55 hence functioning as a coactivator of HIF-1, PKM2 can promote cancer glycolysis.…”

Section: Regulation Of Pgam1mentioning

confidence: 83%

“…PGAM1 expression is regulated mainly at the transcriptional step. Subsequent research confirmed that hypoxia increases the PGAM1 activity in liver and brain, but does not affect the PGAM2 activity in muscle . These results suggested that under reduced oxygen tension, the induction of PGAM1 may contribute to the regulation of the glycolytic flux and play a role in the adaptation of cells to hypoxia .…”

Section: Regulation Of Pgam1mentioning

confidence: 90%

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The role of phosphoglycerate mutase 1 in tumor aerobic glycolysis and its potential therapeutic implications

Jiang

Sun

et al. 2013

Intl Journal of Cancer

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A significant characteristic of cancer cell metabolism is the high level of aerobic glycolysis with high glucose consumption and lactate production. Phophoglycerate mutase 1 (PGAM1) is an enzyme that catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate during glycolysis. It has been reported that this enzyme is commonly upregulated in many human cancers. PGAM1 plays an important role in coordinating glycolysis and anabolic activity to promote cancer cell proliferation. However, the mechanisms under these effects are still poorly understood. This review focuses on the most recent advances in the structure and functions of PGAM1, and PGAM1's role in glycolysis in cancer cells and regulators that modulate PGAM1's effects. Progress in understanding of PGAM1 will provide the rationale to support the development of new hypothesis-driven studies to define PGAM1's potential therapeutic implications for cancer treatment.In the early 1920s, German scientist Otto Warburg and his coworkers discovered that under aerobic conditions tumor tissues metabolize nearly tenfold more glucose to lactate in a given time than normal tissues. Thus, even in the nonhypoxia environment tumor cells prefer the metabolic pathway of glycolysis to the more efficient oxidative phosphorylation for energy production.1 This observation was named as the "Warburg effect" 2 or aerobic glycolysis, which has been supported by many studies performed later on. Although early beliefs considered aerobic glycolysis (the metabolic signature of cancer cells) as primitive and inefficient, advances in cancer research over the last decade have provided concise evidence that metabolic reprogramming of cancer cells is oncogene-directed and essential for tumor progression.3 This unique metabolic signature produces the energy and biological synthesis that accommodates the rapid proliferation of cancer cells. Therefore, this altered metabolism is now included as a hallmark of cancer. 3,4

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Section: Regulation Of Pgam1mentioning

confidence: 83%

Section: Regulation Of Pgam1mentioning

confidence: 90%

The role of phosphoglycerate mutase 1 in tumor aerobic glycolysis and its potential therapeutic implications

Jiang

Sun

et al. 2013

Intl Journal of Cancer

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“…We previously showed that both T 3 and hypoxia increased PGAM expression and activity levels in different rabbit tissues in vivo [6, 18], although not all tissues respond in the same manner. In both erythroblasts and reticulocytes, T 3 and hypoxia increase PGAM activity and mRNA levels.…”

Section: Discussionmentioning

confidence: 99%

“…Control animals drank only water. Hypoxia was induced in a methacrylate cage with a mixture of 90% nitrogen and 10% oxygen at a flux of 2–3 l/min, as previously described [6]. Rabbits were kept in hypoxia conditions for 10 days and euthanized.…”

Section: Methodsmentioning

confidence: 99%

“…We have previously reported the effects of 3,3′,5-triiodo- L -thyronine (T 3 ) and hypoxia on PGAM expression and activity in different rabbit tissues in vivo and showed that they are tissue-dependent. Thus, T 3 increases PGAM expression in the muscle and liver but not in the brain, while hypoxia increases the expression in the liver and brain but not in the muscle [6]. …”

Section: Introductionmentioning

confidence: 99%

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Effects of Thyroid Hormone and Hypoxia on 2,3-Bisphosphoglycerate, Bisphosphoglycerate Synthase and Phosphoglycerate Mutase in Rabbit Erythroblasts and Reticulocytes in vivo

González-Cinca

Ossa²,

Carreras³

et al. 2004

Horm Res Paediatr

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Objectives: The effects of triiodothyronine (T₃) and hypoxia on 2,3-bisphosphoglycerate (2,3-BPG) studied in vitro are unclear. To clarify these effects we selected a more physiologic approach: the in vivo study in rabbits. We also present the changes produced by T₃ and hypoxia on phosphoglycerate mutase (PGAM), which requires 2,3-BPG as a cofactor, and 2,3-BPG synthase (BPGS), the enzyme responsible for 2,3-BPG synthesis in erythroblasts and reticulocytes. Methods: Hyperthyroidism was induced by daily T₃ injection (250 µg/kg), hypoxia by a mixture of 90% nitrogen and 10% oxygen and hypothyroidism by propylthiouracil (PTU) added to drinking water. Results: Both T₃ administration and hypoxic conditions increased 2,3-BPG levels and BPGS mRNA levels and activity in erythroblasts but not in reticulocytes. Unlike BPGS, both PGAM mRNA levels and activity were increased in erythroblasts and reticulocytes under hyperthyrodism and hypoxia. The antihormone PTU produced opposite effects to T₃. Conclusion: The results presented here suggest that both hyperthyroidism and hypoxia modulate in vivo red cell 2,3-BPG content by changes in the expression of BPGS. Similarly, the changes in PGAM activity are also explained by changes in its expression.

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Mitochondrial superoxide anion radicals mediate induction of apoptosis in cardiac myoblasts exposed to chronic hypoxia

Kolamunne

Clare

Griffiths

2011

Archives of Biochemistry and Biophysics

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Effects of Hypoxia and Thyroid Hormone on mRNA Levels and Activity of Phosphoglycerate Mutase in Rabbit Tissues

Cited by 7 publications

References 32 publications

The role of phosphoglycerate mutase 1 in tumor aerobic glycolysis and its potential therapeutic implications

The role of phosphoglycerate mutase 1 in tumor aerobic glycolysis and its potential therapeutic implications

Effects of Thyroid Hormone and Hypoxia on 2,3-Bisphosphoglycerate, Bisphosphoglycerate Synthase and Phosphoglycerate Mutase in Rabbit Erythroblasts and Reticulocytes in vivo

Mitochondrial superoxide anion radicals mediate induction of apoptosis in cardiac myoblasts exposed to chronic hypoxia

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