The phosphorylation state of phosphofructokinase from the mantle tissue of the facultative anaerobe mollusk Mytilus galloprovincialis was determined by a back-phosphorylation technique. The incubation of intact mantle tissue with 8-bromoadenosine 3':5'-cyclic monophosphate increased significantly the phosphate content of phosphofructokinase, which indicates that the enzyme can be phosphorylated in vivo by endogenous cAMP-dependent protein kinase. The phosphate content of mussel phosphofructokinase changes significantly during the year, in agreement with the kinetic data that show a more active enzyme form in earlier autumn. These results suggest that cAMP-dependent phosphorylation of phosphofructokinase can be partially responsible for the observed glycolytic changes associated with the annual gametogenic cycle that takes place in the mantle tissue of the mollusk. On the contrary, no differences were observed between aerobic and 24-h hypoxic mussels with regard to the phosphorylation state and the kinetic constants of phosphofructokinase. This result is inconsistent with the hypothesis that phosphorylation of phosphofructokinase is involved in the glycolytic depression that takes place during the long-term environmental hypoxia that the mollusk can undergo.
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http://dx.doi.org/10.1006/abbi.1998.0631 | DOI Listing |
Nat Struct Mol Biol
January 2025
Zhejiang Provincial Key Laboratory of Pancreatic Disease, Department of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Thymidine kinase 1 (TK1), a crucial enzyme in DNA synthesis, is highly expressed in various cancers. However, the mechanisms underlying its elevated expression and the implications for tumor metabolism remain unclear. Here we demonstrate that activation of growth factor receptors enhances TK1 expression.
View Article and Find Full Text PDFACS Med Chem Lett
January 2025
Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35 Yamate-cho, Suita, Osaka 564-8680, Japan.
Inhibiting phosphofructokinase-1 (PFK1) is a promising approach for treating lactic acidosis and mitochondrial dysfunction by activating oxidative phosphorylation. Tryptolinamide (TLAM) has been shown as a PFK1 inhibitor, but its complex stereochemistry, with 16 possible isomers complicates further development. We conducted an asymmetric synthesis, determined the absolute configurations, and evaluated the PFK1 inhibitory activity of the TLAM isomers.
View Article and Find Full Text PDFJ Insect Physiol
December 2024
State Key Laboratory of Wheat and Maize Crop Science/Henan International Laboratory for Green Pest Control/College of Plant Protection, Henan Agricultural University, Zhengzhou, China. Electronic address:
The enzyme 6-phosphofructokinase-1 (PFK1) acts as the primary rate-limiting enzyme in glycolysis, catalyzing the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. This glycolytic process provides essential substrates for the synthesis of sex pheromones. However, the specific function of PFK1 in sex pheromone biosynthesis remains unidentified.
View Article and Find Full Text PDFInt J Biol Sci
December 2024
Department of Human Cell Biology and Genetics, Joint Laboratory of Guangdong-Hong Kong Universities for Vascular Homeostasis and Diseases, School of Medicine, Southern University of Science and Technology, Shenzhen, Guangdong 518055, China.
PFKP Phosphofructokinase, Platelet Type isoform), as an essential metabolic enzyme, contributes to the high glycolysis rates seen in cancers while its role in oncogenic pathways, especially from a non-metabolic aspect, is not fully understood. We found that PFKP was highly expressed in NSCLC and was related to poor patient survival. Knockdown of PFKP significantly inhibited cell proliferation, colony formation, invasion, and migration of NSCLC cells.
View Article and Find Full Text PDFExp Biol Med (Maywood)
November 2024
Department of Veterinary Integrative Biosciences, Texas A&M University, College Station, TX, United States.
Fructose and lactate are present in high concentrations in uterine luminal fluid, fetal fluids and fetal blood of ungulates and cetaceans, but their roles have been ignored and they have been considered waste products of pregnancy. This review provides evidence for key roles of both fructose and lactate in support of key metabolic pathways required for growth and development of fetal-placental tissues, implantation and placentation. The uterus and placenta of ungulates convert glucose to fructose via the polyol pathway.
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