Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The increase in both glucose 6-phosphatase and hexokinase activities in brown adipose tissues of cold-exposed mice probably relates to thermogenesis by the substrate cycle between glucose 6-phosphate and glucose (Watanabe et al.: Anatomical Record 219:39-44, 1987). To clarify the factors causing the simultaneous increase, we examined biochemically the effects of uni- or bilateral surgical denervation of brown adipose tissues, of adrenalectomy, or of streptozotocin injection on the increase in the two activities in the tissues of cold-exposed mice. Further, the effects of denervation on the increase were also examined histochemically. The simultaneous increase in the two activities was inhibited in the denervated tissues of cold-exposed animals in biochemical and histochemical experiments. However, the increase in the activities was not inhibited in the tissues of animals exposed to cold after adrenalectomy or streptozotocin injection. The results suggest strongly that the activation of the substrate cycle in brown adipose tissues of cold-exposed mice is caused by a transmitter released from sympathetic nerve endings, probably norepinephrine.
Anat Rec 1990 Mar
PMID:Neuronal regulation of substrate cycle between glucose 6-phosphate and glucose in brown adipose tissues of cold-exposed mice. 215 53

Cytochemical and biochemical glucose 6-phosphatase (G6Pase) activity was examined in brown adipose tissues of normal, cold-exposed, or starved mice. In addition, G6Pase activity in white adipose tissue and hexokinase activity in brown and white adipose tissues were biochemically measured. In normal animals, the reaction product for G6Pase activity was localized in the endoplasmic reticulum and nuclear envelope of brown adipose cells. The amount of the reaction product increased in cold-exposed or starved animals. Biochemical G6Pase activity (259.7 +/- 48.5 ng Pi/min/mg protein) in brown adipose tissues of normal animals was higher when the value was compared with values of other organs. Biochemical G6Pase and hexokinase activities increased rapidly in brown adipose tissues of cold-exposed animals, and a close relation was found between activities of the two enzymes. In brown adipose tissues of animals starved for 3 days, biochemical G6Pase activity increased, but hexokinase activity did not change. In white adipose tissues of normal, cold-exposed, or starved animals, G6Pase activity was very low, although the enzyme activity increased slightly in animals starved for 3 days. The results show that the high G6Pase activity in brown adipose cells probably relates to thermogenesis in cold-exposed animals and may be concerned with glucose release into the blood in starved animals.
Anat Rec 1987 Sep
PMID:Significance of increase in glucose 6-phosphatase activity in brown adipose cells of cold-exposed and starved mice. 282 61

Glucose-6-phosphatase (G6Pase) activity was examined cytochemically in the metaphysis of femurs of 3- and 7-day-old rats. G6Pase and hexokinase activities were also examined biochemically in the femur and tibia of 3-day-old animals. The reaction product for G6Pase activity was seen in the endoplasmic reticulum and nuclear envelope of all cell types composing the metaphysis. The amount of the reaction product was abundant in osteoblasts, moderate in osteocytes, and moderate to scarce in osteoclasts and capillary endothelial cells. Biochemical G6Pase activity in the bones was higher than that in the brain, submandibular gland, or pancreas of the animals. Hexokinase activity in the bones was not different from that in the submandibular gland, pancreas, or kidney. The activity ratio of G6Pase and hexokinase in the bones (0.603) was greater than that in the submandibular gland, pancreas, or brain and smaller than that in the kidney. Possible physiological significances of the higher G6Pase activity in osteoblasts are discussed.
Anat Rec 1988 Mar
PMID:High glucose-6-phosphatase activity in osteoblasts in the metaphysis of femur of growing rats. 283 86

Penfluridol, a commonly used antipsychotic agent in a clinical setting, exhibits potential anticancer properties against various human malignancies. Here, we investigated the effect of penfluridol on the biological behavior of colorectal cancer (CRC) cells. Cell viability and clonogenic potential were detected by the cell counting kit-8 and colony formation assay. The cell apoptosis and cell cycle distribution were quantified through flow cytometry. Caspase-3 activity, glucose consumption, lactate production, and intracellular ATP levels were evaluated using the corresponding commercial detection kits. The protein levels of related genes were detected through western blotting. Mitochondrial membrane potential was detected using JC-1 staining. A CRC xenograft tumor model was used to validate the antitumor activity of penfluridol in vivo. Penfluridol reduced cell survival and promoted apoptotic cell death effectively through the mitochondria-mediated intrinsic pathway in a dose-dependent manner. Furthermore, the process of glycolysis in HCT-116 and HT-29 cells was inhibited upon penfluridol treatment, as evidenced by the decrease in glucose consumption, lactate production, and intracellular ATP levels. Further mechanistic studies revealed that penfluridol influenced cell apoptosis and glycolysis in CRC cells by downregulating hexokinase-2 (HK-2). The proapoptotic effect and glycolytic inhibition-induced by penfluridol were effectively reversed by HK-2 overexpression. Consistent with in vitro results, penfluridol could also suppress tumor growth and trigger apoptosis in vivo. Penfluridol triggers mitochondrial-mediated apoptosis and induces glycolysis inhibition via modulating HK-2 in CRC and provides a theoretical basis to support penfluridol as a repurposed drug for CRC patients.
Anat Rec (Hoboken) 2020 May 29
PMID:Penfluridol triggers mitochondrial-mediated apoptosis and suppresses glycolysis in colorectal cancer cells through down-regulating hexokinase-2. 3247 Feb