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Nihon Rinsho. Japanese Journal of... Aug 1999
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Isozymes 1982
Review
Topics: 2,3-Diphosphoglycerate; Adenosine Triphosphate; Animals; Antibodies, Monoclonal; Chromosome Mapping; Chromosomes, Human, 21-22 and Y; Diphosphoglyceric Acids; Genetic Code; Glycogen Storage Disease Type VII; Hemolysis; Humans; Isoenzymes; Macromolecular Substances; Muscular Diseases; Neoplasms; Phosphofructokinase-1; Trisomy
PubMed: 6219967
DOI: No ID Found -
Biophysical Journal Apr 2021Although much is known about the biochemical regulation of glycolytic enzymes, less is understood about how they are organized inside cells. We systematically examine...
Although much is known about the biochemical regulation of glycolytic enzymes, less is understood about how they are organized inside cells. We systematically examine the dynamic subcellular localization of glycolytic protein phosphofructokinase-1/PFK-1.1 in Caenorhabditis elegans. We determine that endogenous PFK-1.1 localizes to subcellular compartments in vivo. In neurons, PFK-1.1 forms phase-separated condensates near synapses in response to energy stress from transient hypoxia. Restoring animals to normoxic conditions results in cytosolic dispersion of PFK-1.1. PFK-1.1 condensates exhibit liquid-like properties, including spheroid shapes due to surface tension, fluidity due to deformations, and fast internal molecular rearrangements. Heterologous self-association domain cryptochrome 2 promotes formation of PFK-1.1 condensates and recruitment of aldolase/ALDO-1. PFK-1.1 condensates do not correspond to stress granules and might represent novel metabolic subcompartments. Our studies indicate that glycolytic protein PFK-1.1 can dynamically form condensates in vivo.
Topics: Animals; Caenorhabditis elegans; Glycolysis; Organelles; Phosphofructokinase-1; Phosphofructokinases; Phosphorylation
PubMed: 32853565
DOI: 10.1016/j.bpj.2020.08.002 -
Cell Reports Nov 2023Aerobic glycolysis is critical for cancer progression and can be exploited in cancer therapy. Here, we report that the human carboxymethylenebutenolidase homolog...
Aerobic glycolysis is critical for cancer progression and can be exploited in cancer therapy. Here, we report that the human carboxymethylenebutenolidase homolog (carboxymethylenebutenolidase-like [CMBL]) acts as a tumor suppressor by reprogramming glycolysis in colorectal cancer (CRC). The anti-cancer action of CMBL is mediated through its interactions with the E3 ubiquitin ligase TRIM25 and the glycolytic enzyme phosphofructokinase-1 platelet type (PFKP). Ectopic CMBL enhances TRIM25 binding to PFKP, leading to the ubiquitination and proteasomal degradation of PFKP. Interestingly, CMBL is transcriptionally activated by p53 in response to genotoxic stress, and p53 activation represses glycolysis by promoting PFKP degradation. Remarkably, CMBL deficiency, which impairs p53's ability to inhibit glycolysis, makes tumors more sensitive to a combination therapy involving the glycolysis inhibitor 2-deoxyglucose. Taken together, our study demonstrates that CMBL suppresses CRC growth by inhibiting glycolysis and suggests a potential combination strategy for the treatment of CMBL-deficient CRC.
Topics: Humans; Cell Line, Tumor; Glucose; Glycolysis; Neoplasms; Phosphofructokinase-1; Phosphofructokinase-1, Type C; Phosphofructokinases; Tumor Suppressor Protein p53
PubMed: 37967006
DOI: 10.1016/j.celrep.2023.113426 -
Chembiochem : a European Journal of... Sep 2022Detection of pyrophosphate is important in quantifying enzyme activity, particularly adenylation domain activity during non-ribosomal peptide synthesis. The previous...
Detection of pyrophosphate is important in quantifying enzyme activity, particularly adenylation domain activity during non-ribosomal peptide synthesis. The previous development of an enzyme coupled PP /NADH assay allowed the measurement of such activity in an online fashion using commercially available components. Now, with a key enzyme - 6-phosphofructokinase - no longer available, we have screened and identified viable replacement enzymes that can be expressed in high yield and that are far superior in activity to the now discontinued commercial product. This will support the ability of groups to continue to use this established online assay for pyrophosphate detection.
Topics: Diphosphates; NAD; Peptides; Phosphofructokinase-1; Phosphofructokinases
PubMed: 35876398
DOI: 10.1002/cbic.202200325 -
Nihon Rinsho. Japanese Journal of... Feb 1995
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The Journal of Veterinary Medical... Oct 2019In healthy individuals, plasma glucose levels are maintained within a normal range. During fasting, endogenous glucose is released either through glycogenolysis or...
In healthy individuals, plasma glucose levels are maintained within a normal range. During fasting, endogenous glucose is released either through glycogenolysis or gluconeogenesis. Gluconeogenesis involves the formation of glucose-6-phosphate from a variety of precursors followed by its subsequent hydrolysis to glucose. Gluconeogenesis occurs in the liver and the kidney. In order to compare gluconeogenesis in canine liver and kidney, the activity and expression of the rate limiting enzymes that catalyze the fructose-6-phosphate and fructose 1,6-bisphosphate steps, namely, phosphofructokinase-1 (PFK-1) (glycolysis) and fructose bisphosphatase-1 (FBP-1) (gluconeogenesis), were examined. Healthy male and female beagle dogs aged 1-2 years were euthanized humanely, and samples of their liver and kidney were obtained for analysis. The levels of PFK-1 and FBP-1 in canine liver and kidney were assessed by enzymatic assays, Western blotting, and RT-qPCR. Enzyme assays showed that, in dogs, the kidney had higher specific activity of PFK-1 and FBP-1 than the liver. Western blotting and RT-qPCR data demonstrated that of the three different subunits (PFK-M, PFK-L, and PFK-P) the PFK-1 in canine liver mainly comprised PFK-L, whereas the PFK-1 in the canine kidney comprised all three subunits. As a result of these differences in the subunit composition of PFK-1, glucose metabolism might be regulated differently in the liver and kidney.
Topics: Animals; Dogs; Female; Fructose-Bisphosphatase; Gluconeogenesis; Glycolysis; Kidney; Liver; Male; Phosphofructokinase-1
PubMed: 31474665
DOI: 10.1292/jvms.19-0361 -
Methods in Enzymology 1982
Topics: Adenosine Monophosphate; Allosteric Regulation; Kinetics; Macromolecular Substances; Molecular Weight; NAD; Phosphofructokinase-1; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet
PubMed: 6218374
DOI: 10.1016/s0076-6879(82)90106-9 -
Methods in Enzymology 1975
Topics: Acetone; Ammonium Sulfate; Chemical Phenomena; Chemistry, Physical; Chromatography; Chromatography, DEAE-Cellulose; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Fractional Precipitation; Methods; Phosphofructokinase-1; Protamines; Saccharomyces cerevisiae; Spectrophotometry
PubMed: 124388
DOI: 10.1016/0076-6879(75)42097-3 -
Journal of Cellular Biochemistry May 2017It is known that interfering with glycolysis leads to profound modification of cancer cell proliferation. However, energy production is not the major reason for this...
It is known that interfering with glycolysis leads to profound modification of cancer cell proliferation. However, energy production is not the major reason for this correlation. Here, using HeLa cells as a model for cancer, we demonstrate that phosphofructokinase-P (PFK-P), which is overexpressed in diverse types of cancer including HeLa cells, modulates expression of P44/42 mitogen-activated protein kinase (MAPK). Silencing of PFK-P did not alter HeLa cell viability or energy production, including the glycolytic rate. On the other hand, silencing of PFK-P induced the downregulation of p44/42 MAPK, augmenting the sensitivity of HeLa cells to different drugs. Conversely, overexpression of PFK-P promotes the upregulation of p44/42 MAPK, making the cells more resistant to the drugs. These results indicate that overexpression of PFK-P by cancer cells is related to activation of survival pathways via upregulation of MAPK and suggest PFK-P as a promising target for cancer therapy. J. Cell. Biochem. 118: 1216-1226, 2017. © 2016 Wiley Periodicals, Inc.
Topics: Cell Proliferation; Cell Survival; Gene Silencing; Glycolysis; HeLa Cells; Humans; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinase 3; Phosphofructokinase-1; Signal Transduction
PubMed: 27791266
DOI: 10.1002/jcb.25774