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Astrocytes and neurons communicate via a monocarboxylic acid shuttle.

AIMS neuroscience

Roosterman D, Cottrell GS.
PMID: 32607414
AIMS Neurosci. 2020 Apr 20;7(2):94-106. doi: 10.3934/Neuroscience.2020007. eCollection 2020.

Since formulation of the Astrocyte-Neuron Lactate Shuttle (ANLS) hypothesis in 1994, the hypothesis has provoked criticism and debate. Our review does not criticise, but rather integrates experimental data characterizing proton-linked monocarboxylate transporters (MCTs) into the ANLS. MCTs have wide...

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Roosterman D, Cottrell GS. Astrocytes and neurons communicate via a monocarboxylic acid shuttle. AIMS Neurosci. 2020;7(2):94-106doi: 10.3934/Neuroscience.2020007.
Roosterman, D., & Cottrell, G. S. (2020). Astrocytes and neurons communicate via a monocarboxylic acid shuttle. AIMS neuroscience, 7(2), 94-106. https://doi.org/10.3934/Neuroscience.2020007
Roosterman, Dirk, and Cottrell, Graeme S. "Astrocytes and neurons communicate via a monocarboxylic acid shuttle." AIMS neuroscience vol. 7,2 (2020): 94-106. doi: https://doi.org/10.3934/Neuroscience.2020007
Roosterman D, Cottrell GS. Astrocytes and neurons communicate via a monocarboxylic acid shuttle. AIMS Neurosci. 2020 Apr 20;7(2):94-106. doi: 10.3934/Neuroscience.2020007. eCollection 2020. PMID: 32607414; PMCID: PMC7321766.
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Enhancement of wildlife disease surveillance using multiplex quantitative PCR: development of qPCR assays for major pathogens in UK squirrel populations.

European journal of wildlife research

Dale TD, Watts PC, Jones D, Pounder K, Everest DJ, Begon ME, Chantrey J.
PMID: 32214943
Eur J Wildl Res. 2016;62(5):589-599. doi: 10.1007/s10344-016-1031-z. Epub 2016 Jul 28.

Rapid development in polymerase chain reaction (PCR) technology has revolutionised the speed and accuracy of many diagnostic assays. However, comparatively few wildlife epidemiological studies use quantitative PCR (qPCR) for pathogen detection, even fewer employ an internal control, to ensure...

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Dale TD, Watts PC, Jones D, et al. Enhancement of wildlife disease surveillance using multiplex quantitative PCR: development of qPCR assays for major pathogens in UK squirrel populations. Eur J Wildl Res. 2016;62(5):589-599doi: 10.1007/s10344-016-1031-z.
Dale, T. D., Watts, P. C., Jones, D., Pounder, K., Everest, D. J., Begon, M. E., & Chantrey, J. (2016). Enhancement of wildlife disease surveillance using multiplex quantitative PCR: development of qPCR assays for major pathogens in UK squirrel populations. European journal of wildlife research, 62(5), 589-599. https://doi.org/10.1007/s10344-016-1031-z
Dale, Timothy D, et al. "Enhancement of wildlife disease surveillance using multiplex quantitative PCR: development of qPCR assays for major pathogens in UK squirrel populations." European journal of wildlife research vol. 62,5 (2016): 589-599. doi: https://doi.org/10.1007/s10344-016-1031-z
Dale TD, Watts PC, Jones D, Pounder K, Everest DJ, Begon ME, Chantrey J. Enhancement of wildlife disease surveillance using multiplex quantitative PCR: development of qPCR assays for major pathogens in UK squirrel populations. Eur J Wildl Res. 2016;62(5):589-599. doi: 10.1007/s10344-016-1031-z. Epub 2016 Jul 28. PMID: 32214943; PMCID: PMC7088385.
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Metabolic protein phosphoglycerate kinase 1 confers lung cancer migration by directly binding HIV Tat specific factor 1.

Cell death discovery

Chang YC, Chan MH, Li CH, Yang CJ, Tseng YW, Tsai HF, Chiou J, Hsiao M.
PMID: 34091600
Cell Death Discov. 2021 Jun 05;7(1):135. doi: 10.1038/s41420-021-00520-1.

Phosphoglycerate kinase (PGK) is involved in glycolytic and various metabolic events. Dysfunction of PGK may induce metabolic reprogramming and the Warburg effect. In this study, we demonstrated that PGK1, but not PGK2, may play a key role in tumorigenesis...

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Chang YC, Chan MH, Li CH, et al. Metabolic protein phosphoglycerate kinase 1 confers lung cancer migration by directly binding HIV Tat specific factor 1. Cell Death Discov. 2021;7(1):135doi: 10.1038/s41420-021-00520-1.
Chang, Y. C., Chan, M. H., Li, C. H., Yang, C. J., Tseng, Y. W., Tsai, H. F., Chiou, J., & Hsiao, M. (2021). Metabolic protein phosphoglycerate kinase 1 confers lung cancer migration by directly binding HIV Tat specific factor 1. Cell death discovery, 7(1), 135. https://doi.org/10.1038/s41420-021-00520-1
Chang, Yu-Chan, et al. "Metabolic protein phosphoglycerate kinase 1 confers lung cancer migration by directly binding HIV Tat specific factor 1." Cell death discovery vol. 7,1 (2021): 135. doi: https://doi.org/10.1038/s41420-021-00520-1
Chang YC, Chan MH, Li CH, Yang CJ, Tseng YW, Tsai HF, Chiou J, Hsiao M. Metabolic protein phosphoglycerate kinase 1 confers lung cancer migration by directly binding HIV Tat specific factor 1. Cell Death Discov. 2021 Jun 05;7(1):135. doi: 10.1038/s41420-021-00520-1. PMID: 34091600; PMCID: PMC8179927.
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Overexpression of glycolysis markers in placental tissue of pregnant women with chronic venous disease: a histological study.

International journal of medical sciences

Ortega MA, Sáez MA, Fraile-Martínez O, Álvarez-Mon MA, García-Montero C, Guijarro LG, Asúnsolo Á, Álvarez-Mon M, Bujan J, García-Honduvilla N, De León-Luis JA, Bravo C.
PMID: 34975312
Int J Med Sci. 2022 Jan 01;19(1):186-194. doi: 10.7150/ijms.65419. eCollection 2022.

Chronic Venous Disease (CVD) refers to a wide variety of venous disorders being the varicose veins its most common manifestation. It is well-established the link between pregnancy and the risk of suffering CVD, due to hormonal or haematological factors,...

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Ortega MA, Sáez MA, Fraile-Martínez O, et al. Overexpression of glycolysis markers in placental tissue of pregnant women with chronic venous disease: a histological study. Int J Med Sci. 2022;19(1):186-194doi: 10.7150/ijms.65419.
Ortega, M. A., Sáez, M. A., Fraile-Martínez, O., Álvarez-Mon, M. A., García-Montero, C., Guijarro, L. G., Asúnsolo, �. �., Álvarez-Mon, M., Bujan, J., García-Honduvilla, N., De León-Luis, J. A., & Bravo, C. (2022). Overexpression of glycolysis markers in placental tissue of pregnant women with chronic venous disease: a histological study. International journal of medical sciences, 19(1), 186-194. https://doi.org/10.7150/ijms.65419
Ortega, Miguel A, et al. "Overexpression of glycolysis markers in placental tissue of pregnant women with chronic venous disease: a histological study." International journal of medical sciences vol. 19,1 (2022): 186-194. doi: https://doi.org/10.7150/ijms.65419
Ortega MA, Sáez MA, Fraile-Martínez O, Álvarez-Mon MA, García-Montero C, Guijarro LG, Asúnsolo Á, Álvarez-Mon M, Bujan J, García-Honduvilla N, De León-Luis JA, Bravo C. Overexpression of glycolysis markers in placental tissue of pregnant women with chronic venous disease: a histological study. Int J Med Sci. 2022 Jan 01;19(1):186-194. doi: 10.7150/ijms.65419. eCollection 2022. PMID: 34975312; PMCID: PMC8692115.
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Impaired age-dependent increases in phosphoglycerate kinase activity in red blood cells of Parkinson's disease patients.

Parkinsonism & related disorders

Fujino Y, Kasai T, Kitani-Morii F, Ohmichi T, Shinomoto M, Menjo K, Mizuno T.
PMID: 34607089
Parkinsonism Relat Disord. 2021 Oct;91:128-134. doi: 10.1016/j.parkreldis.2021.09.016. Epub 2021 Sep 22.

BACKGROUND: Impaired bioenergetics are partially involved in the pathogenesis of Parkinson's disease (PD). Phosphoglycerate kinase (PGK), an essential enzyme for glycolysis, has recently attracted attention due to its pathogenic role in PD and as a target for disease-modifying therapies....

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Fujino Y, Kasai T, Kitani-Morii F, et al. Impaired age-dependent increases in phosphoglycerate kinase activity in red blood cells of Parkinson's disease patients. Parkinsonism Relat Disord. 2021;91:128-134doi: 10.1016/j.parkreldis.2021.09.016.
Fujino, Y., Kasai, T., Kitani-Morii, F., Ohmichi, T., Shinomoto, M., Menjo, K., & Mizuno, T. (2021). Impaired age-dependent increases in phosphoglycerate kinase activity in red blood cells of Parkinson's disease patients. Parkinsonism & related disorders, 91128-134. https://doi.org/10.1016/j.parkreldis.2021.09.016
Fujino, Yuzo, et al. "Impaired age-dependent increases in phosphoglycerate kinase activity in red blood cells of Parkinson's disease patients." Parkinsonism & related disorders vol. 91 (2021): 128-134. doi: https://doi.org/10.1016/j.parkreldis.2021.09.016
Fujino Y, Kasai T, Kitani-Morii F, Ohmichi T, Shinomoto M, Menjo K, Mizuno T. Impaired age-dependent increases in phosphoglycerate kinase activity in red blood cells of Parkinson's disease patients. Parkinsonism Relat Disord. 2021 Oct;91:128-134. doi: 10.1016/j.parkreldis.2021.09.016. Epub 2021 Sep 22. PMID: 34607089.
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PGK1-coupled HSP90 stabilizes GSK3β expression to regulate the stemness of breast cancer stem cells.

Cancer biology & medicine

Tang W, Wu Y, Qi X, Yu R, Lu Z, Chen A, Fan X, Li J.
PMID: 34403222
Cancer Biol Med. 2021 Aug 17; doi: 10.20892/j.issn.2095-3941.2020.0362. Epub 2021 Aug 17.

OBJECTIVE: Glycogen synthase kinase-3β (GSK3β) has been recognized as a suppressor of Wnt/β-catenin signaling, which is critical for the stemness maintenance of breast cancer stem cells. However, the regulatory mechanisms of GSK3β protein expression remain elusive.METHODS: Co-immunoprecipitation and mass...

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Tang W, Wu Y, Qi X, et al. PGK1-coupled HSP90 stabilizes GSK3β expression to regulate the stemness of breast cancer stem cells. Cancer Biol Med. 2021;doi: 10.20892/j.issn.2095-3941.2020.0362.
Tang, W., Wu, Y., Qi, X., Yu, R., Lu, Z., Chen, A., Fan, X., & Li, J. (2021). PGK1-coupled HSP90 stabilizes GSK3β expression to regulate the stemness of breast cancer stem cells. Cancer biology & medicine, . https://doi.org/10.20892/j.issn.2095-3941.2020.0362
Tang, Wei, et al. "PGK1-coupled HSP90 stabilizes GSK3β expression to regulate the stemness of breast cancer stem cells." Cancer biology & medicine vol. (2021). doi: https://doi.org/10.20892/j.issn.2095-3941.2020.0362
Tang W, Wu Y, Qi X, Yu R, Lu Z, Chen A, Fan X, Li J. PGK1-coupled HSP90 stabilizes GSK3β expression to regulate the stemness of breast cancer stem cells. Cancer Biol Med. 2021 Aug 17; doi: 10.20892/j.issn.2095-3941.2020.0362. Epub 2021 Aug 17. PMID: 34403222.
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Protein Stability, Folding and Misfolding in Human PGK1 Deficiency.

Biomolecules

Valentini G, Maggi M, Pey AL.
PMID: 24970202
Biomolecules. 2013 Dec 18;3(4):1030-52. doi: 10.3390/biom3041030.

Conformational diseases are often caused by mutations, altering protein folding and stability in vivo. We review here our recent work on the effects of mutations on the human phosphoglycerate kinase 1 (hPGK1), with a particular focus on thermodynamics and...

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Valentini G, Maggi M, Pey AL. Protein Stability, Folding and Misfolding in Human PGK1 Deficiency. Biomolecules. 2013;3(4):1030-52doi: 10.3390/biom3041030.
Valentini, G., Maggi, M., & Pey, A. L. (2013). Protein Stability, Folding and Misfolding in Human PGK1 Deficiency. Biomolecules, 3(4), 1030-52. https://doi.org/10.3390/biom3041030
Valentini, Giovanna, et al. "Protein Stability, Folding and Misfolding in Human PGK1 Deficiency." Biomolecules vol. 3,4 (2013): 1030-52. doi: https://doi.org/10.3390/biom3041030
Valentini G, Maggi M, Pey AL. Protein Stability, Folding and Misfolding in Human PGK1 Deficiency. Biomolecules. 2013 Dec 18;3(4):1030-52. doi: 10.3390/biom3041030. PMID: 24970202; PMCID: PMC4030965.
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The role of phosphoglycerate kinase in the metabolism of Pseudomonas putida.

FEBS letters

Aparicio ML, Ruiz-Amil M, Vicente M, Cánovas JL.
PMID: 11945789
FEBS Lett. 1971 May 20;14(5):326-328. doi: 10.1016/0014-5793(71)80292-2.

No abstract available.

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Aparicio ML, Ruiz-Amil M, Vicente M, et al. The role of phosphoglycerate kinase in the metabolism of Pseudomonas putida. FEBS Lett. 1971;14(5):326-328doi: 10.1016/0014-5793(71)80292-2.
Aparicio, M. L., Ruiz-Amil, M., Vicente, M., & Cánovas, J. L. (1971). The role of phosphoglycerate kinase in the metabolism of Pseudomonas putida. FEBS letters, 14(5), 326-328. https://doi.org/10.1016/0014-5793(71)80292-2
Aparicio, M L., et al. "The role of phosphoglycerate kinase in the metabolism of Pseudomonas putida." FEBS letters vol. 14,5 (1971): 326-328. doi: https://doi.org/10.1016/0014-5793(71)80292-2
Aparicio ML, Ruiz-Amil M, Vicente M, Cánovas JL. The role of phosphoglycerate kinase in the metabolism of Pseudomonas putida. FEBS Lett. 1971 May 20;14(5):326-328. doi: 10.1016/0014-5793(71)80292-2. PMID: 11945789.
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Improvement of in situ PCR by optimization of PCR cycle number and proteinase k concentration: localization of x chromosome-linked phosphoglycerate kinase-1 gene in mouse reproductive organs.

Acta histochemica et cytochemica

Hishikawa Y, An S, Yamamoto-Fukuda T, Shibata Y, Koji T.
PMID: 19492023
Acta Histochem Cytochem. 2009 Apr 28;42(2):15-21. doi: 10.1267/ahc.09011. Epub 2009 Apr 23.

In situ polymerase chain reaction (in situ PCR), which can detect a few copies of genes within a cell by amplifying the target gene, was developed to better understand the biological functions of tissues. In this study, we optimized...

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Hishikawa Y, An S, Yamamoto-Fukuda T, et al. Improvement of in situ PCR by optimization of PCR cycle number and proteinase k concentration: localization of x chromosome-linked phosphoglycerate kinase-1 gene in mouse reproductive organs. Acta Histochem Cytochem. 2009;42(2):15-21doi: 10.1267/ahc.09011.
Hishikawa, Y., An, S., Yamamoto-Fukuda, T., Shibata, Y., & Koji, T. (2009). Improvement of in situ PCR by optimization of PCR cycle number and proteinase k concentration: localization of x chromosome-linked phosphoglycerate kinase-1 gene in mouse reproductive organs. Acta histochemica et cytochemica, 42(2), 15-21. https://doi.org/10.1267/ahc.09011
Hishikawa, Yoshitaka, et al. "Improvement of in situ PCR by optimization of PCR cycle number and proteinase k concentration: localization of x chromosome-linked phosphoglycerate kinase-1 gene in mouse reproductive organs." Acta histochemica et cytochemica vol. 42,2 (2009): 15-21. doi: https://doi.org/10.1267/ahc.09011
Hishikawa Y, An S, Yamamoto-Fukuda T, Shibata Y, Koji T. Improvement of in situ PCR by optimization of PCR cycle number and proteinase k concentration: localization of x chromosome-linked phosphoglycerate kinase-1 gene in mouse reproductive organs. Acta Histochem Cytochem. 2009 Apr 28;42(2):15-21. doi: 10.1267/ahc.09011. Epub 2009 Apr 23. PMID: 19492023; PMCID: PMC2685019.
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The chicken hypersensitive site-4 insulator cannot fully shield the murine phosphoglycerate kinase-1 promoter from integration site effects in transgenic mice.

3 Biotech

Farzaneh F, Mirzapoor Z, Jahangirian E, Heidari F, Hashemi E, Rahim-Tayefeh A, Fatemi N, Jamshidizad A, Dashtizad M, Shamsara M.
PMID: 31192080
3 Biotech. 2019 Jul;9(7):255. doi: 10.1007/s13205-019-1786-5. Epub 2019 Jun 07.

Differential expression of transgenes in transgenic animals is one of the main drawbacks of pronuclear injection. To overwhelm this issue, the genetic constructs are equipped with insulators. In this study, the consensus of exerting chicken hypersensitive site-4 (

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Farzaneh F, Mirzapoor Z, Jahangirian E, et al. The chicken hypersensitive site-4 insulator cannot fully shield the murine phosphoglycerate kinase-1 promoter from integration site effects in transgenic mice. 3 Biotech. 2019;9(7):255doi: 10.1007/s13205-019-1786-5.
Farzaneh, F., Mirzapoor, Z., Jahangirian, E., Heidari, F., Hashemi, E., Rahim-Tayefeh, A., Fatemi, N., Jamshidizad, A., Dashtizad, M., & Shamsara, M. (2019). The chicken hypersensitive site-4 insulator cannot fully shield the murine phosphoglycerate kinase-1 promoter from integration site effects in transgenic mice. 3 Biotech, 9(7), 255. https://doi.org/10.1007/s13205-019-1786-5
Farzaneh, Fatemeh, et al. "The chicken hypersensitive site-4 insulator cannot fully shield the murine phosphoglycerate kinase-1 promoter from integration site effects in transgenic mice." 3 Biotech vol. 9,7 (2019): 255. doi: https://doi.org/10.1007/s13205-019-1786-5
Farzaneh F, Mirzapoor Z, Jahangirian E, Heidari F, Hashemi E, Rahim-Tayefeh A, Fatemi N, Jamshidizad A, Dashtizad M, Shamsara M. The chicken hypersensitive site-4 insulator cannot fully shield the murine phosphoglycerate kinase-1 promoter from integration site effects in transgenic mice. 3 Biotech. 2019 Jul;9(7):255. doi: 10.1007/s13205-019-1786-5. Epub 2019 Jun 07. PMID: 31192080; PMCID: PMC6555836.
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Reference Gene Selection for RT-qPCR Analysis of Flower Development in Chrysanthemum morifolium and Chrysanthemum lavandulifolium.

Frontiers in plant science

Qi S, Yang L, Wen X, Hong Y, Song X, Zhang M, Dai S.
PMID: 27014310
Front Plant Sci. 2016 Mar 11;7:287. doi: 10.3389/fpls.2016.00287. eCollection 2016.

Quantitative real-time PCR (qPCR) is a popular and powerful tool used to understand the molecular mechanisms of flower development. However, the accuracy of this approach depends on the stability of reference genes. The capitulum of chrysanthemums is very special,...

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Qi S, Yang L, Wen X, et al. Reference Gene Selection for RT-qPCR Analysis of Flower Development in Chrysanthemum morifolium and Chrysanthemum lavandulifolium. Front Plant Sci. 2016;7:287doi: 10.3389/fpls.2016.00287.
Qi, S., Yang, L., Wen, X., Hong, Y., Song, X., Zhang, M., & Dai, S. (2016). Reference Gene Selection for RT-qPCR Analysis of Flower Development in Chrysanthemum morifolium and Chrysanthemum lavandulifolium. Frontiers in plant science, 7287. https://doi.org/10.3389/fpls.2016.00287
Qi, Shuai, et al. "Reference Gene Selection for RT-qPCR Analysis of Flower Development in Chrysanthemum morifolium and Chrysanthemum lavandulifolium." Frontiers in plant science vol. 7 (2016): 287. doi: https://doi.org/10.3389/fpls.2016.00287
Qi S, Yang L, Wen X, Hong Y, Song X, Zhang M, Dai S. Reference Gene Selection for RT-qPCR Analysis of Flower Development in Chrysanthemum morifolium and Chrysanthemum lavandulifolium. Front Plant Sci. 2016 Mar 11;7:287. doi: 10.3389/fpls.2016.00287. eCollection 2016. PMID: 27014310; PMCID: PMC4786574.
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Phosphate Deficiency in Maize : III. Changes in Enzyme Activities during the Course of Phosphate Deprivation.

Plant physiology

Usuda H, Shimogawara K.
PMID: 16669091
Plant Physiol. 1992 Aug;99(4):1680-5. doi: 10.1104/pp.99.4.1680.

The effects of low concentrations of phosphate (low-P) on soluble protein content, the activities of 12 different enzymes, and the rates of photosynthesis and respiration on the basis of leaf area were investigated in maize (Zea mays L.) leaves...

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Usuda H, Shimogawara K. Phosphate Deficiency in Maize : III. Changes in Enzyme Activities during the Course of Phosphate Deprivation. Plant Physiol. 1992;99(4):1680-5doi: 10.1104/pp.99.4.1680.
Usuda, H., & Shimogawara, K. (1992). Phosphate Deficiency in Maize : III. Changes in Enzyme Activities during the Course of Phosphate Deprivation. Plant physiology, 99(4), 1680-5. https://doi.org/10.1104/pp.99.4.1680
Usuda, H, and Shimogawara, K. "Phosphate Deficiency in Maize : III. Changes in Enzyme Activities during the Course of Phosphate Deprivation." Plant physiology vol. 99,4 (1992): 1680-5. doi: https://doi.org/10.1104/pp.99.4.1680
Usuda H, Shimogawara K. Phosphate Deficiency in Maize : III. Changes in Enzyme Activities during the Course of Phosphate Deprivation. Plant Physiol. 1992 Aug;99(4):1680-5. doi: 10.1104/pp.99.4.1680. PMID: 16669091; PMCID: PMC1080681.
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