Regulation of 6-phosphofructo-1-kinase activity in ras-transformed rat-1 fibroblasts
Abstract
Fructose 2,6-bisphosphate (F-2,6-P2) stimulated glycolysis in cell-free extracts of both normal and ras-transfected rat-1 fibroblasts. The extract of the transformed cell glycolyzed more rapidly in both the absence and the presence of F-2,6-P2 than the extract of the parent fibroblast. Addition of mitochondrial ATPase (F1) or inorganic phosphate (Pi) further stimulated lactate production in both cell lines. F-2,6-P2 stimulated the 6-phosphofructo-1-kinase (PFK-1) activity in extracts of normal and transfected cells. The activity in extracts of transformed cells tested with a fructose 6-phosphate regenerating system was considerably higher than in the extract of normal cells. Stimulation of PFK-1 activity by cAMP of both cell lines was not as pronounced as that by F-2,6-P2. In the absence of F-2,6-P2 the PFK-1 activity was strongly inhibited in the transformed cell by ATP concentrations higher than 1 mM, whereas in the normal cell only a marginal inhibition was noted even at 2 or 3 mM ATP. F-2,6-P2 reversed the inhibition of PFK-1 by ATP. Nicotinamide adenine dinucleotide (NAD) at 100 microM (in the presence of 2 mM ATP and 1 microM F-2,6-P2) stimulated PFK-1 activity only in the transformed cell, whereas nicotinamide adenine dinucleotide phosphate (NADP) inhibited PFK-1 activity (in the presence or absence of 1 microM F-2,6-P2) in extracts of both cell lines. No previous observations of stimulation or inhibition by NAD or NADP on PFK-1 activity appear to have been reported. A threefold increase in the intracellular concentration of F-2,6-P2 was observed after transfection of rat-1 fibroblast by the ras oncogene. We conclude from these data that the PFK-1 activity of ras-transfected rat-1 fibroblasts shows a greater response to certain stimulating and inhibitory regulating factors than that of the parent cell.
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Oncogenic KRAS upregulates PFK1, ENO1, and LDHA, promoting glycolytic flux and production of intermediates that can enter anabolic pathways.
“Oncogenic KRAS also upregulates expression of other key glycolytic enzymes, such as PFK1, ENO1, and LDHA28,31–33, thereby promoting glycolytic flux and enabling the production of glycolytic intermediates that can be shunted into other anabolic pathways (Fig 2).”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [31]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Merritt, A. J. (1964) · Microchemical Journal · doi:10.1016/0026-265x(64)90139-0 · Cited by 5,180 · see citing works
Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes
Land, H., Parada, L. F., & Weinberg, R. A. (1983) · Nature · doi:10.1038/304596a0 · Cited by 2,804 · see citing works
A Kinetic Study of Pyrophosphate: Fructose‐6‐Phosphate Phosphotransferase from Potato Tubers
SCHAFTINGEN, E. V., Lederer, B., Bartrons, R., & Hers, H. G. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb07039.x · Cited by 652 · see citing works
Regulatory Mechanisms in Carbohydrate Metabolism
Wu, R., & Racker, E. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98124-x · Cited by 397 · see citing works
Self-citationDifferential activation of yeast adenylate cyclase by wild type and mutant RAS proteins
Broek, D., Samiy, N., Fasano, O., Fujiyama, A., Tamanoi, F., Northup, J. K., & Wigler, M. H. (1985) · Cell · doi:10.1016/s0092-8674(85)80057-x · Cited by 353 · see citing works
SCHAFTINGEN, E. V., Hue, L., & Hers, H. G. (1980) · Biochemical Journal · doi:10.1042/bj1920897 · Cited by 317 · see citing works
The Subunit Structure of Beef Heart Mitochondrial Adenosine Triphosphatase
Knowles, A. F., & Penefsky, H. S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44736-4 · Cited by 311 · see citing works
Mansour, T. E., & Mansour, J. M. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60345-x · Cited by 309 · see citing works
ras p21 and GAP inhibit coupling of muscarinic receptors to atrial K+ channels
Yatani, A., Okabe, K., Polakis, P. G., Halenbeck, R., McCormick, F. P., & Brown, A. M. (1990) · Cell · doi:10.1016/0092-8674(90)90187-j · Cited by 235 · see citing works
Regulatory Mechanisms in Carbohydrate Metabolism
Wu, R., & Racker, E. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98125-1 · Cited by 177 · see citing works
Self-citationDiamond, I., Legg, A., Schneider, J. A., & Rozengurt, E. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38184-x · Cited by 126 · see citing works
Vora, S., Halper, J. P., & Knowles, D. M. (1985) · PubMed · Cited by 89 · see citing works
Alterations in glucose metabolism in chick embryo cells transformed by Rous sarcoma virus
Singh, M., Singh, V. N., AUGUST, J. T., & Horecker, B. L. (1974) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(74)90160-x · Cited by 71 · see citing works
Boscá, L., Mojena, M., Ghysdael, J., Rousseau, G. G., & Hue, L. (1986) · Biochemical Journal · doi:10.1042/bj2360595 · Cited by 54 · see citing works
Determinants of glycolytic rate in normal and transformed chick embryo fibroblasts.
Fagan, J. B., & Racker, E. (1978) · PubMed · Cited by 40 · see citing works
Self-citationComparative studies of glucose metabolism in HTC, RLC, MH1C1, and Reuber H35 rat hepatoma cells.
Schamhart, D., van de Poll, K. W., & Wijk, R. V. (1979) · PubMed · Cited by 39 · see citing works
Differences in phosphofructokinase regulation in normal and tumor rat thyroid cells.
Meldolesi, M. F., Macchia, V., & Laccetti, P. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81851-1 · Cited by 30 · see citing works
Increase of the glycolytic rate in human resting fibroblasts following serum stimulation
Bruni, P., Farnararo, M., Vasta, V., & D'Alessandro, A. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80412-8 · Cited by 26 · see citing works
O’Brien, T. G., Saladik, D., & Diamond, L. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)91702-9 · Cited by 26 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
RAS oncogenes: weaving a tumorigenic web
Pylayeva-Gupta, Y., Grabocka, E., & Bar-Sagi, D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3106 · Cited by 1,789 · see citing works
Causes and Consequences of Increased Glucose Metabolism of Cancers
Gillies, R. J., Robey, I., & Gatenby, R. A. (2008) · Journal of Nuclear Medicine · doi:10.2967/jnumed.107.047258 · Cited by 617 · see citing works
Tumor glycolysis, an essential sweet tooth of tumor cells
Paul, S., Ghosh, S., & Kumar, S. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.09.007 · Cited by 449 · see citing works
Clem, B. F., Telang, S., Clem, A. L., Yalçın, A., Meier, J. B., Simmons, A. J., Rasku, M. A., Arumugam, S., Dean, W. L., Eaton, J. W., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0482 · Cited by 430 · see citing works
“Although PFK-1 is the second irreversible enzyme in glycolysis and is increased in neoplastic tissues and transformed cells (10, 34, 35), PFK-1 inhibitors that suppress”
BackgroundDynamics of the Cellular Metabolome during Human Cytomegalovirus Infection
Munger, J. C., Bajad, S. U., Coller, H. A., Shenk, T. E., & Rabinowitz, J. D. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020132 · Cited by 417 · see citing works
Regulation of glucose metabolism by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases in cancer
Yalçın, A., Telang, S., Clem, B. F., & Chesney, J. A. (2009) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2009.01.003 · Cited by 407 · see citing works
The metabolic landscape of RAS-driven cancers from biology to therapy
Mukhopadhyay, S., Vander Heiden, M. G., & McCormick, F. (2021) · Nature Cancer · doi:10.1038/s43018-021-00184-x · Cited by 315 · see citing works
The molecular determinants of de novo nucleotide biosynthesis in cancer cells
Tong, X., Zhao, F., & Thompson, C. B. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.01.002 · Cited by 351 · see citing works
Atsumi, T., Chesney, J. A., Metz, C. N., Leng, L., Donnelly, S. C., Makita, Z., Mitchell, R., & Bucala, R. (2002) · PubMed · Cited by 322 · see citing works
Control of Glycolysis through Regulation of PFK1: Old Friends and Recent AdditionsPreprint
Mor, I., Cheung, E. C., & Vousden, K. H. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010868 · Cited by 316 · see citing works
“Reciprocally, cells transformed by oncogenes such as v-src/vfps or ras showed elevated F2,6BP as well as increased glycolytic flux (Bosca et al. 1986; Kole et al. 1991), demonstrating the”
BackgroundThe Warburg Effect 97 Years after Its Discovery
Pascale, R. M., Calvisi, D. F., Simile, M. M., Feo, C. F., & Feo, F. (2020) · Cancers · doi:10.3390/cancers12102819 · Cited by 304 · see citing works
Shi, L., Pan, H., Liu, Z., Xie, J., & Han, W. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2017.44 · Cited by 287 · see citing works
Hypoxia, glucose metabolism and the Warburg’s effect
Bartrons, R., & Caro, J. (2007) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-007-9080-3 · Cited by 260 · see citing works
Metabolic transformation in cancer
Tennant, D. A., Durán, R. V., Boulahbel, H., & Gottlieb, E. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp070 · Cited by 226 · see citing works
Waves of gene regulation suppress and then restore oxidative phosphorylation in cancer cells
Smolková, K., Plecitá‐Hlavatá, L., Bellancé, N., Bénard, G., Rossignol, R., & Ježek, P. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.05.003 · Cited by 224 · see citing works
Is cancer a disease of abnormal cellular metabolism? New angles on an old idea
DeBerardinis, R. J. (2008) · Genetics in Medicine · doi:10.1097/gim.0b013e31818b0d9b · Cited by 217 · see citing works
Fructose-1,6-bisphosphate couples glycolytic flux to activation of Ras
Peeters, K., Van Leemputte, F., Fischer, B., Bonini, B. M., Quezada, H., Tsytlonok, M., Haesen, D., Vanthienen, W., Bernardes, N., Gonzalez-Blas, C. B., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01019-z · Cited by 203 · see citing works
Addiction to Coupling of the Warburg Effect with Glutamine Catabolism in Cancer Cells
Smith, B., Schafer, X., Ambeskovic, A., Spencer, C. M., Land, H., & Munger, J. C. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.045 · Cited by 168 · see citing works
“It is also clear that specific oncogenic mutations, for example, those activating the Ras-Akt-mTOR pathways, are critical for activation of common cancer-associated metabolic activities (Deprez et al., 1997; Elstrom et al., 2004; Gaglio et al., 2011; Guo et al., 2011; Kole et al., 1991; Ramanathan et al., 2005; Telang…”
BackgroundRas transformation requires metabolic control by 6-phosphofructo-2-kinase
Telang, S., Yalçın, A., Clem, A. L., Bucala, R., Lane, A. N., Eaton, J. W., & Chesney, J. A. (2006) · Oncogene · doi:10.1038/sj.onc.1209709 · Cited by 166 · see citing works
“Stable transfection of oncogenic H-rasV12 into Rat-1 immortalized fibroblasts causes increased glucose uptake and lactate production (Racker et al., 1985; Kole et al., 1991).”
BackgroundTargeting the Metabolic Microenvironment of Tumors
Bailey, K. M., Wojtkowiak, J. W., Hashim, A. I., & Gillies, R. J. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-397927-8.00004-x · Cited by 154 · see citing works
“Phosphofructokinase-1 (PFK-1) catalyzes the phosphorylation of fructose- 6-phosphate to fructose-1,6-bisphosphate in a rate-limiting step in the glycolytic pathway.”
BackgroundInfluentialRecent developments in the regulation of the angiogenic switch by cellular stress factors in tumors
North, S., Moenner, M., & Bikfalvi, A. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.08.007 · Cited by 136 · see citing works
Fructose 2,6-Bisphosphate in Cancer Cell Metabolism
Bartrons, R., Simon‐Molas, H., Rodríguez‐García, A., Castaño, E., Navarro‐Sabaté, À., Manzano, À., & Martinez‐Outschoorn, U. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00331 · Cited by 134 · see citing works
“PFK1 activity is induced by HIF-1α (57) or the overexpression of the oncogenes RAS and SRC (58).”
BackgroundInfluential6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase and tumor cell glycolysis
Chesney, J. A. (2006) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000241661.15514.fb · Cited by 128 · see citing works
Current State and Future Challenges for PI3K Inhibitors in Cancer Therapy
Sirico, M., D’Angelo, A., Gianni, C., Casadei, C., Merloni, F., & De Giorgi, U. (2023) · Cancers · doi:10.3390/cancers15030703 · Cited by 121 · see citing works
Mazurek, S., Zwerschke, W., Jansen‐Dürr, P., & EIGENBRODT, E. (2001) · Oncogene · doi:10.1038/sj.onc.1204792 · Cited by 107 · see citing works
“Metabolic consequences of ras-induced tetramerization of M2-PK As in other cell lines, in NRK cells oncogenic ras led to an overproportional increase of glycolytic enzymes, especially in 6-phosphofructo 1-kinase (PFK 1) (Gregory et al., 1976; Kole et al., 1991).”
BackgroundSpoden, G. A., Rostek, U., Lechner, S. G., Mitterberger, M. C., Mazurek, S., & Zwerschke, W. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.06.024 · Cited by 96 · see citing works
The potential utility of PFKFB3 as a therapeutic target
Bartrons, R., Rodríguez‐García, A., Simon‐Molas, H., Castaño, E., Manzano, À., & Navarro‐Sabaté, À. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1498082 · Cited by 90 · see citing works
“In addition, transformed cell lines and tumors present increased PFK-1 activity, which is activated by Ras and Src oncogenes [77,78], leading to increased levels of glycolysis in transformed cell lines [79].”
BackgroundTargeting small GTPases: emerging grasps on previously untamable targets, pioneered by KRAS
Yin, G., Huang, J., Petela, J., Jiang, H., Zhang, Y., Gong, S., Wu, J., Liu, B., Shi, J., & Gao, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01441-4 · Cited by 87 · see citing works
Ge, X., Lyu, P., Cao, Z., Li, J., Guo, G., Xia, W., & Gu, Y. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.06.068 · Cited by 85 · see citing works
The oncoprotein H-RasV12 increases mitochondrial metabolism
Telang, S., Lane, A. N., Nelson, K. K., Arumugam, S., & Chesney, J. A. (2007) · Molecular Cancer · doi:10.1186/1476-4598-6-77 · Cited by 71 · see citing works
“Ectopic expression of oncogenic Ras in immortalized cells has been found to: (i) increase glucose uptake and lactate production; (ii) increase ribose-5-phosphate, a glucose-derived anabolic precursor of DNA and RNA; and (iii) increase sensitivity to the glycolytic inhibitors, 2-deoxyglucose and oxamate [12-14].”
BackgroundBoehm, J. R., Kutz, S. M., Sage, E. H., Staiano‐Coico, L., & Higgins, P. J. (1999) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199910)181:1 · Cited by 32 · see citing works
Cancer’s craving for sugar: an opportunity for clinical exploitation
Yeluri, S., Madhok, B., Prasad, R. K., Quirke, P., & Jayne, D. G. (2009) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-009-0590-8 · Cited by 57 · see citing works
Structure-based drug design: From nucleic acid to membrane protein targets
Dailey, M. M., Hait, C., Holt, P. A., Maguire, J. M., Meier, J. B., Miller, M. C., Petraccone, L., & Trent, J. O. (2009) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2009.01.011 · Cited by 55 · see citing works
“fructose 2,6 bisphosphate (F2,6BP) (Kole et al., 1991; Mazurek et al., 2001; Ramanathan et al., 2005).”
BackgroundGlycolysis: an emerging regulator of osteoarthritis
Jiang, D., Guo, J., Liu, Y.-Q., Li, W., & Lu, D.-Z. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1327852 · Cited by 63 · see citing works
“In studies related to cancer and aerobic glycolysis, the interaction between HIF-1 a and PFKFB3 gene expression has been found to affect glycolysis progression and cell activity (107).”
BackgroundDíaz‐Moralli, S., Tarrado‐Castellarnau, M., Alenda, C., Castells, A., & Cascante, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025323 · Cited by 53 · see citing works
RAS signalling in energy metabolism and rare human diseases
Dard, L., Bellancé, N., Lacombe, D., & Rossignol, R. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.003 · Cited by 51 · see citing works
Novel Therapeutic Targets of Tumor Metabolism
Kishton, R. J., & Rathmell, J. C. (2015) · The Cancer Journal · doi:10.1097/ppo.0000000000000099 · Cited by 48 · see citing works
“This is the first committed step in glycolysis, and the activity of PFK1 is elevated in many types of cancer, allowing for increased flux of glucose into the glycolytic pathway.(21,22) The mechanism of increased PFK1 activity in cancer relies on the generation of an allosteric activator of PFK1.”
BackgroundMEK1/2 Inhibition Decreases Lactate in BRAF-Driven Human Cancer Cells
Miniotis, M. F., Arunan, V., Eykyn, T. R., Marais, R., Workman, P., Leach, M. O., & Beloueche‐Babari, M. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-1969 · Cited by 49 · see citing works
“RAS activation increases glycolysis in rat fibroblasts (17, 18) and the ERK1/2 transcriptional targets C-MYC and NF-kB (19) upregulate glycolytic enzyme expression (20) and increase glucose transporter expression (21), respectively.”
BackgroundAzole Antimycotics - A Highway to New Drugs or a Dead End?
Musioł, R., & Kowalczyk, W. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712799462621 · Cited by 40 · see citing works
Farsani, S. S. M., & Verma, V. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1175532 · Cited by 31 · see citing works
More Than Meets the Eye Regarding Cancer Metabolism
Kubicka, A., Matczak, K., & Łabieniec-Watała, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179507 · Cited by 30 · see citing works
Canonical and Non-Canonical Roles of PFKFB3 in Brain Tumors
Alvarez, R., Mandal, D., & Chittiboina, P. (2021) · Cells · doi:10.3390/cells10112913 · Cited by 23 · see citing works
“mRNA induction in a hypoxic environment as opposed to wild-type cells [8] Oncogenic signaling via the Ras pathway is a known regulator of cancerous glucose metabolism as well as a key contributor to the HIF-1α hypoxic response [9,49,50].”
BackgroundTelang, S., Nelson, K. K., Siow, D. L., Yalçın, A., Thornburg, J. M., Imbert-Fernandez, Y., Klarer, A. C., Farghaly, H., Clem, B. F., Eaton, J. W., et al. (2012) · Molecular Cancer · doi:10.1186/1476-4598-11-60 · Cited by 22 · see citing works
“Activated GTP-bound Ras family members promote survival and proliferation in part by increasing glucose uptake and flux into the synthesis of ribose-5-phosphate and lactate [2-4].”
BackgroundCasillo, S. M., Gatesman, T. A., Chilukuri, A. S. S., Varadharajan, S., Johnson, B. J., Premkumar, D. R., Jane, E. P., Plute, T. J., Koncar, R. F., Stanton, A.-C. J., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113557 · Cited by 18 · see citing works
Tristetraprolin posttranscriptionally downregulates PFKFB3 in cancer cells
Jang, J. H., Kim, D. J., Ham, S., Vo, M., Jeong, S. Y., Choi, S. H., Park, S. S., Jeon, D. Y., Lee, B. J., Ko, B. K., et al. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.10.128 · Cited by 13 · see citing works
Xia, X., Werner, D., Popanda, O., & Thielmann, H. W. (1994) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/bf01191798 · Cited by 11 · see citing works
Uncharged tRNA-phosphofructokinase interaction in amino acid deficiency
RABINOVITZ, M. (1996) · Amino Acids · doi:10.1007/bf00806583 · Cited by 9 · see citing works
RAS: Circuitry and therapeutic targeting
Singh, G., Thakur, N., & Kumar, U. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110505 · Cited by 5 · see citing works
Glycolytic Pathway as a Target for Tumor Inhibition
Lu, W., & Huang, P. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6615-5_5 · Cited by 4 · see citing works
Wolfe, H., Hannigan, C., O’Sullivan, M., Barry-Carroll, L., Brennan, S., LAWLOR, B. A., Robertson, I. H., & Lynch, M. A. (2018) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2018.02.007 · Cited by 4 · see citing works
Ogura, M., Shikano, N., Nakajima, S., Sagara, J., Yamaguchi, N., Kusanagi, K., Okui, Y., Mizutani, A., Kobayashi, M., & Kawai, K. (2015) · Nuclear Medicine and Biology · doi:10.1016/j.nucmedbio.2014.12.017 · Cited by 1 · see citing works
“PFK-1 mediates the phosphorylation of D-Fru-6-P to D-Fru1,6-P2 using ATP, and is regulated allosterically by the level of D-fructose 2,6-bisphosphate (D-Fru-2,6-P2) [34].”
BackgroundPorquet, M. Z. (2010) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Caracterització i regulació transcripcional del gen "pfkfb3"
Obach, M. (2007) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)
Resnick, R. J., Kole, H. K., & Racker, E. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90083-u
Self-citationHereditary cancer syndromes linked to oxidative phosphorylation insufficiency
Kaplan, B., Duraj, T., Lee, D. C., & Seyfried, T. N. (2025) · ONCOLOGIE · doi:10.1515/oncologie-2025-0301
Manipulating the Tumor Microenvironment for Therapeutic Benefit
Bailey, K. M. (2014) · Digital Commons - University of South Florida (University of South Florida)
- Authors
- Kole, H. K., Resnick, R. J., Van Doren, M., & Racker, E.
- Affiliations
- Cornell University (US)
- Corresponding author
- Racker, Efraim
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1991-05
- Volume
- 286
- Issue
- 2
- Pages
- 586-590
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W1973601236
- Cited by
- 57
- References
- 20
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 1 · 2015: 4 · 2014: 1 · 2013: 1 · 2012: 3
- FWCI
- 0.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ca008964-26)
- National Cancer Institute (CA-08964)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- 6-phosphofructokinase, fructose-2,6-bisphosphate, oncogenic Ras, ras-transformed fibroblasts, Rat-1 fibroblasts, glycolysis regulation, ATP inhibition, NAD+, NADPH, cyclic AMP, lactic acid production, enzyme regulation
- MeSH terms
- Animals, Cell Line, Cell Transformation, Neoplastic, Cell-Free System, Fibroblasts, Fructose, Fructosediphosphates, Glycolysis, Kinetics, Lactates, Phosphates, Phosphofructokinase-1, Genes, ras, Rats
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