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PubMed1993

Isoenzyme shift from glucokinase to hexokinase is not an early but a late event in hepatocarcinogenesis.

The appearance of hepatocellular adenomas and carcinomas induced in rat liver with N-nitrosomorpholine is preceded by different types of preneoplastic foci consisting of phenotypically altered hepatocytes. The altered cells show changes in the activities of various enzymes including those of carbohydrate metabolism. Glucokinase is a type of hexokinase that is specific for hepatocytes. The enzyme plays a key role in glucose homeostasis in normal liver parenchyma and is replaced in the dedifferentiated hepatocytes of carcinomas by a low Km hexokinase. To determine the time course of the shift from glucokinase to this isoenzyme in the development of carcinomas, focal hepatic lesions were dissected from freeze-dried serial tissue sections by the laser-dissection method and studied by microbiochemical tests. In early clear and acidophilic cell foci that excessively stored glycogen (glycogenotic foci) a nearly normal glucokinase activity comparable with that of the surrounding hepatocytes was observed, whereas in the later appearing mixed cell foci a reduction in the activity of this enzyme without a compensatory increase in the hexokinase activity was found. A pronounced activity of hexokinase was only measurable in fully developed carcinomas. Since glucokinase is not modified at the post-transcriptional level, a gradual decrease in its mRNA during hepatocarcinogenesis can be assumed. A shift in gene expression from glucokinase to the isoenzyme hexokinase occurs only at the mixed cell foci/carcinoma transition step of the carcinogenic process.

Adenoma, Liver Cell↗
PubMed2004

Effect of different thyroid states on mitochondrial porin synthesis and hexokinase activity in developing rabbit brain.

Voltage-dependent anion-selective channel proteins (VDACs) are pore-forming proteins found in the outer mitochondrial membrane of all eukaryotes and in brain postsynaptic membranes. VDACs regulate anion fluxes of a series of metabolites including ATP, thus regulating mitochondrial metabolic functions. Hexokinase binds to porin. The mitochondrially bound hexokinase can greatly increase the rate of aerobic glycolysis. The activities of hexokinase and protein levels of mitochondrial porin were determined in brains of hypothyroid rabbits and in hypothyroid rabbits administered with thyroxine. Proteins were separated by electrophoresis, and the proteins of interest were quantified. Western blotting analysis revealed a significant decrease (approximately 50%) in the relative amount of porin in the hypothyroid compared with euthyroid rabbits. The changes in the developmental pattern of hexokinase activity in the brain of hypothyroid rabbits and the effect of T(4) on this enzyme activity have been investigated. Hypothyroid rabbits showed lower activity than their corresponding age-matched normal neonates. Administration of thyroxine to the hypothyroid neonates at birth abolished the effects of methimazole [1-methyl-2-mercaptoimidazole (MMI)]. These findings apparently indicate that the synthesis of the pore-forming protein and the hexokinase enzymes are under thyroid control during the fetal and the early postnatal period.

Animals↗
PubMed1994

Hexokinase activity in mouse embryos developed in vivo and in vitro.

Micro-determination methods were used for quantitative examination of possible differences in energy metabolism in mouse embryos arising after spontaneous ovulation or after gonadotrophin stimulation. Comparisons of embryonic development in vivo and in vitro were also made. The relevance of the results to human development and their clinical significance are discussed. The enzymatic activity of hexokinase, phosphofructokinase, glucose 6-phosphate dehydrogenase, malate dehydrogenase and lactate dehydrogenase in individual mouse embryos throughout preimplantation development was evaluated. Hexokinase activity in 1-cell embryos was the lowest by far of the five enzymes measured, and the 0.035 +/- 0.010 pmol of nicotinamide adenine dinucleotide phosphate hydrogenase formed/embryo/min was also lower than in any of the somatic organs examined. Hexokinase activity, unlike the other enzymes, progressively increased in the morulae and blastocyst stages in embryos obtained either by spontaneous ovulation or via gonadotrophin stimulation. Although there is a significant delay, this increase was also observed when 2-cell embryos developed in vitro. Increases in hexokinase activity were observed 68-75 h after human chorionic gonadotrophin administration in vivo, but after 80-86 h in vitro. These increases in vitro were inhibited by the administration of actinomycin D added to the medium. The results suggest that hexokinase may be a key enzyme synthesized as the zygotic genome is expressed in preimplantation embryos, and its measurement may help to assess the quality of embryos developed in vitro.

Animals↗
PubMed1996

Functional interaction of hexokinase with ATP requires participation by both small and large lobes of the enzyme: implications for other proteins using the actin fold as a nucleotide binding motif.

The actin fold is a structural motif involved in binding of ATP to an otherwise diverse family of proteins that includes hexokinase, actin, and the 70 kDa heat shock protein. Previous analyses have focused attention on a hydrophobic pocket within the large lobe of hexokinase (and analogous regions in other proteins possessing the actin fold motif) as the-site for binding of the adenine moiety. However, there is reason to believe that binding of the adenine moiety also involves a beta-sheet region located in the small lobe of hexokinase. It is postulated that functional interaction with ATP, required for catalysis, involves interactions with both regions. The expected structural consequences provide a basis for explaining the kinetic mechanism suggested for this enzyme, i.e., although both substrates can bind independently, the preferred kinetic pathway is not random but ordered, with glucose binding first. The structural features postulated to be involved in binding of ATP to hexokinase are also found in other proteins possessing the actin fold motif. Interaction of the nucleotide with the beta-sheet region, analogous to that found in the "small lobe" of hexokinase, may induce functionally important conformational changes in other proteins employing the actin fold as a nucleotide binding motif.

Actins↗
PubMed1988

Autophosphorylation of yeast hexokinase PII.

Autophosphorylation of hexokinase PII was studied using an enzyme purified from Saccharomyces cerevisiae. Incubation of this enzyme preparation with [gamma-32P]ATP and Mn2+ or Mg2+ gave a phosphoprotein of molecular mass 58,000 which corresponded to hexokinase PII. D-Xylose stimulated autophosphorylation of hexokinase PII. Dilution of hexokinase PII over a 10-fold concentration range did not change the specific activity of hexokinase PII autophosphorylation suggesting that it may occur by an intramolecular mechanism.

Hexokinase↗
PubMed2001

Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase.

The serine/threonine kinase Akt/PKB is a major downstream effector of growth factor-mediated cell survival. Activated Akt, like Bcl-2 and Bcl-xL, prevents closure of a PT pore component, the voltage-dependent anion channel (VDAC); intracellular acidification; mitochondrial hyperpolarization; and the decline in oxidative phosphorylation that precedes cytochrome c release. However, unlike Bcl-2 and Bcl-xL, the ability of activated Akt to preserve mitochondrial integrity, and thereby inhibit apoptosis, requires glucose availability and is coupled to its metabolism. Hexokinases are known to bind to VDAC and directly couple intramitochondrial ATP synthesis to glucose metabolism. We provide evidence that such coupling serves as a downstream effector function for Akt. First, Akt increases mitochondria-associated hexokinase activity. Second, the antiapoptotic activity of Akt requires only the first committed step of glucose metabolism catalyzed by hexokinase. Finally, ectopic hexokinase expression mimics the ability of Akt to inhibit cytochrome c release and apoptosis. We therefore propose that Akt increases coupling of glucose metabolism to oxidative phosphorylation and regulates PT pore opening via the promotion of hexokinase-VDAC interaction at the outer mitochondrial membrane.

Animals↗
PubMed1979

Turnover rates of hexokinase I, phosphofructokinase, pyruvate kinase and creatine kinase in slow-twitch soleus muscle and heart of the rabbit.

Hexokinase I was purified from rabbit heart to a specific activity of 70 U/mg protein. The purified enzyme was electrophoretically homogeneous with an apparent molecular weight of 102,000. Purified immunoglobulins from sheep were used to titrate the percentage of hexokinase I in various tissues of the rabbit. Precipitating antibodies from sheep were also prepared against rabbit muscle MM-creatine kinase, phosphofructokinase and pyruvate kinase. Apparent turnover rates of these phosphotransferases and of hexokinase I were determined in rabbit heart and soleus muscle by means of the immunoprecipitation technique after single pulse labelling with [U-14Cl]leucine in vivo. Apparent half-lives of phosphofructokinase, pyruvate kinase and hexokinase I were 0.56 d, 0.73 d and 0.93 d in rabbit heart. In slow-twitch soleus muscle half-lives of phosphofructokinase, pyruvate kinase, hexokinase II and creatine kinase were 0.63 d, 0.72 d, 0.85 d and 0.82 d. The similarity of the rate constants of degradation of these enzymes is interpreted as an indication that different tissue concentrations result primarily from different rates of synthesis.

Animals↗
PubMed1979

Enzyme memory. Effect of glucose 6-phosphate and temperature on the molecular transition of wheat-germ hexokinase LI.

A theory is presented that associates burst (orlag) kinetics with the respective concentrations of enzyme initial states X1 and X6 and with the cooperation of a mnemonical enzyme. The theory predicts that for an enzyme with a negative cooperation, decreasing the initial concentration of X1 (or increasing that of X6) tends to increase the induction time. This increase may correspond to a reversal of a burst in a lag. Similarly, if the enzyme has a positive cooperation, decreasing the initial concentration of X6 (or increasing that of X1) increases the induction time. The first case above is expected to apply to wheat germ hexokinase LI, X1 being the form that binds glucose preferentially, and X6 the one that binds glucose 6-phosphate. By changing solely the respective concentrations of the two initial forms, one may expect to modify the pre-steady-state phase but not the steady-state kinetics of the reaction. By jumping the temperature of the enzyme solution from 4 degrees C to 30 degrees C and letting the transconformation ewuilibrium relax for various periods of time before mixing enzyme with the substrates, one can analyse the effect of the relative concentrations of X1 and X6 on the induction time. One can estimate in that way one of the rate constants of the transconformation between the two free enzyme forms. The shorter the incubation time at 30 degrees C then the smaller is the negative induction time (in absolute values). Another possibility of controlling the ratio between the two initial concentrations of the enzyme, is to pre-mix hexokinase with glucose 6-phosphate and to arrange that glucose-6-phosphate concentration, after mixing enzyme and substrates, is held constant whatever the pre-mixing conditions. When wheat germ hexokinase LI is pre-mixed 30 min at 30 degrees C with glucose 6-phosphate before the reaction starts, the burst does not disappear. If, on the other hand, pre-mixing is effected at 4 degrees C the burst is reversed into lag. This result is taken to mean that the equilibrium constant between the two free enzyme forms (the 'circle' and the 'rhombus') is strongly dependent on temperature. A direct study of the effect of glucose 6-phosphate on the conformational equilibrium of wheat germ hexokinase, gives support to this interpretation. If hexokinase is mixed at 4 degrees C with glucose 6-phosphate a slow increase in fluorescence of tryptophanyl residues is observed, which indicates that the 'rhombus' conformation accumulates under these conditions. On the other hand, at 30 degrees C, glucose 6-phosphate does not produce any significant change in the fluorescence of the protein. As expected, these results imply that the equilibrium between the two free enzymes species is freely reversible a 4 degrees C and nearly irreversible at 30 degrees C. The equations derived from the mnemonical model allow fitting or simulation of the experimental results.

Enzyme Induction↗
PubMed1983

Metal-nucleotide structure at the active sites of the mammalian hexokinases.

The diastereomers of adenosine 5'-O-(2-thiotriphosphate) (ATP beta S) in the presence of Mg2+, Co2+ and Cd2+ have been used to determine the stereospecificity of the metal-nucleotide binding site of rat muscle hexokinase type II and rat liver glucokinase by the method developed by Jaffe and Cohn [J. Biol. Chem. 254, 10839-10845 (1979)]. The kinetic parameters, Km and V, for the mammalian hexokinase reaction have been determined for ATP beta S in the presence of the three divalent metal ions. In the presence of Mg2+, both enzymes exhibit a preference for the B diastereomer of ATP beta S (V ratio, B/A approximately equal to 20). With Cd+, the stereospecificity is reversed and the A diastereomer is the preferred substrate, suggesting direct coordination of S on the beta-P to this metal ion. Co2+ exhibits a decreased specificity for the B diastereomer over Mg2+. This decreasing order of stereo-specificity for the B isomer reflects primarily the decreasing ratios of nucleotide complexes coordinated to O rather than S on the beta-P as the metal ion is changed from Mg2+ to Co2+ to Cd2+. The kinetic parameters for the hexokinases have also been determined for adenosine 5'-O-(1-thiotriphosphate) (ATP alpha S) using the same three metal ions as activators. The A diastereomer is the preferred substrate regardless of the metal ion. This absence of reversal of stereospecificity for metal-ATP alpha S suggests that the alpha-P is not involved in coordinating the metal on the enzyme, unlike the beta-P. That is, the structural constraints of the ATP-binding site on the enzyme overcome the preferred coordination of Cd2+ to S. Given the greater stability of bidentate metal-ATP complexes over monodentate, these data are interpreted as indicating that MgATP binds to the mammalian hexokinases as the beta gamma-bidentate complex in the A screw sense geometry, as has been found for the yeast hexokinase (Jaffe and Cohn, reference cited above).

Animals↗
PubMed1986

Hexokinase PII from Saccharomyces cerevisiae is regulated by changes in the cytosolic Mg2+-free ATP concentration.

Hexokinase PII is not inhibited by high Mg-ATP concentrations if the Mg2+-free ATP is kept at low levels (0.01 mM) in the assay mixture. Hexokinase PI activity is not affected either by Mg2+-free ATP nor by free Mg2+ in the assay mixture. Thus, hexokinase PI and PII activities appear not to be regulated by substrate inhibition as proposed previously [Kopetzki, E. & Entian, K. D. (1985) Eur. J. Biochem. 146, 657-662]. However, the level of Mg2+-free ATP in the hexokinase PII assay mixture strongly affects the enzyme activity by decreasing the Vmax and increasing the Km value for Mg-ATP from 0.15 mM to 5.0 mM. The physiological role of this inhibition, which has not been described previously, was investigated by determining the cytosolic ATP and Mg2+ concentrations in yeast cells grown under derepressing and repressing conditions. Derepression is accompanied by an important loss of Mg2+ from the cells, maintaining the ATP concentration constant. This produces an increase of Mg2+-free ATP in the cytosol from 0.01 mM to 0.1 mM. This free ATP concentration would lead to a maximal inhibition of hexokinase PII.

Adenosine Triphosphate↗
PubMed1994

Low-frequency stimulation of rat fast-twitch muscle enhances the expression of hexokinase II and both the translocation and expression of glucose transporter 4 (GLUT-4).

This study followed changes in the capacities of uptake and phosphorylation of glucose in response to contractile activity in low-frequency stimulated (10Hz, 24 h/d) rat fast-twitch muscle. We investigated the intracellular distribution of GLUT-4, the major glucose transporter isoform in muscle, changes in the amounts of its specific mRNA and total cellular protein, as well as changes in its relative synthesis rate. These analyses were complemented by measurements of total hexokinase activity and hexokinase II (HKII) expression at the levels of mRNA content and protein synthesis. Changes in protein synthesis were determined by in vivo labeling with [35S]methionine. Translocation of GLUT-4 into the sarcolemma was an immediate response to contractile activity, whereas changes in its total amount were observed only with ongoing stimulation (5 d and longer). A twofold increase in GLUT-4 content after 5 d and longer stimulation periods was preceded by elevations of its mRNA and by enhanced [35S]methionine incorporation. Conversely, increases in HKII expression with a rise in total hexokinase activity occurred soon after the onset of stimulation (30-fold elevations of HKII mRNA after 12 h and 20-fold increases in [35S]methionine incorporation after 24 h). With ongoing stimulation, HKII mRNA and synthesis returned to lower levels (fivefold elevations). Nevertheless, hexokinase activity continued to rise, stabilizing at fivefold-elevated levels after 3 d. These observation suggested that posttranscriptional mechanisms contributed to the upregulation of HKII, e.g. stabilization by elevated intracellular glucose and mitochondrial binding of the enzyme. This suggestion was supported by experiments with cessation after 24 h where hexokinase activity continued to increase, although the mRNA content and, especially, the [35S]methionine incorporation decayed steeply. The increase in HKII prior to GLUT-4 suggests that phosphorylation may be rate limiting in glucose utilization of glycolytic fibers under conditions of sustained contractile activity. Taken together, the changes in distribution and content of GLUT-4, as well as in HKII represent early metabolic adaptations. In addition, they are related to the overall process of stimulation-induced fiber type transformation.

Acetylcholinesterase↗
PubMed1996

The inactivation of hexokinase activity does not prevent glucose repression in Candida utilis.

High hexokinase activity was not related to glucose repression in Candida utilis IGC 3092. The addition of Cibacron Blue 3G-A to growing cells in batch culture led to a permanent in vivo hexokinase inactivation, decreased growth rate and inhibited alcohol dehydrogenase. Hexokinase inactivation up to 90% did not alleviate glucose repression of alpha-glucosidase, as has been described for Saccharomyces cerevisiae and other yeasts. Moreover, when cells were physiologically derepressed by growing them in a chemostat at low glucose concentrations, the highest hexokinase activity was shown by the derepressed cells, and decreased as repression increased. Thus, in our strain of C. utilis, hexokinase activity was inversely proportional to glucose repression.

Candida↗
PubMed1996

Molecular analysis of the promoter region of the hexokinase 2 gene of Saccharomyces cerevisiae.

lacZ fusions of the hexokinase 2 gene promoter were constructed and a deletion analysis was performed in order to identify the cis-acting regulatory elements of the promoter that controls hexokinase 2 gene expression. Expression of the hexokinase 2 gene is induced by glucose and around 40-fold repressed by ethanol. This repression seems to be mediated mainly by a repression element located within the coding region of the hexokinase 2 gene, between +39 and +404 bp from the ATG start codon. A second repressing element for ethanol growing cells was located between -455 bp and -254 bp. A synergistic effect on repression of transcription, when ethanol is the carbon source used for growth, was demonstrated by experiments in which both repressing elements were simultaneously removed. The finding of regulatory sequences in the coding region of the hexokinase 2 gene stimulates a search for regulatory elements in the coding region of other yeast genes.

Cloning, Molecular↗
PubMed1999

Mutations that confer resistance to 2-deoxyglucose reduce the specific activity of hexokinase from Myxococcus xanthus.

The glucose analog 2-deoxyglucose (2dGlc) inhibits the growth and multicellular development of Myxococcus xanthus. Mutants of M. xanthus resistant to 2dGlc, designated hex mutants, arise at a low spontaneous frequency. Expression of the Escherichia coli glk (glucokinase) gene in M. xanthus hex mutants restores 2dGlc sensitivity, suggesting that these mutants arise upon the loss of a soluble hexokinase function that phosphorylates 2dGlc to form the toxic intermediate, 2-deoxyglucose-6-phosphate. Enzyme assays of M. xanthus extracts reveal a soluble hexokinase (ATP:D-hexose-6-phosphotransferase; EC 2.7.1.1) activity but no phosphotransferase system activities. The hex mutants have lower levels of hexokinase activities than the wild type, and the levels of hexokinase activity exhibited by the hex mutants are inversely correlated with the ability of 2dGlc to inhibit their growth and sporulation. Both 2dGlc and N-acetylglucosamine act as inhibitors of glucose turnover by the M. xanthus hexokinase in vitro, consistent with the finding that glucose and N-acetylglucosamine can antagonize the toxic effects of 2dGlc in vivo.

Acetylglucosamine↗
PubMed1993

The hexokinase gene is required for transcriptional regulation of the glucose transporter gene RAG1 in Kluyveromyces lactis.

The RAG1 gene of Kluyveromyces lactis encodes a low-affinity glucose/fructose transporter. Its transcription is induced by glucose, fructose, and several other sugars. The RAG4, RAG5, and RAG8 genes are trans-acting genes controlling the expression of the RAG1 gene. We report here the characterization of one of these genes, RAG5. The nucleotide sequence of the cloned RAG5 gene indicated that it encodes a protein that is homologous to hexokinases of Saccharomyces cerevisiae. rag5 mutants showed no detectable hexokinase or glucokinase activity, suggesting that the sugar kinase activity encoded by this gene is the only hexokinase in K. lactis. Both high- and low-affinity transport systems of glucose were affected in rag5 mutants. The defect of the low-affinity component was found to be due to a block of transcription of the RAG1 gene by the hexokinase mutation. In vivo complementation of the rag5 mutation by the HXK2 gene of S. cerevisiae and complementation of hxk1 hxk2 mutations of S. cerevisiae by the RAG5 gene showed that RAG5 and HXK2 were equivalent for sugar-phosphorylating activity but that RAG5 could not restore glucose repression in the S. cerevisiae hexokinase mutants.

Amino Acid Sequence↗
PubMed2004

Akt inhibits apoptosis downstream of BID cleavage via a glucose-dependent mechanism involving mitochondrial hexokinases.

The serine/threonine kinase Akt/protein kinase B inhibits apoptosis induced by a variety of stimuli, including overexpression or activation of proapoptotic Bcl-2 family members. The precise mechanisms by which Akt prevents apoptosis are not completely understood, but Akt may function to maintain mitochondrial integrity, thereby preventing cytochrome c release following an apoptotic insult. This effect may be mediated, in part, via promotion of physical and functional interactions between mitochondria and hexokinases. Here we show that growth factor deprivation induced proteolytic cleavage of the proapoptotic Bcl-2 family member BID to yield its active truncated form, tBID. Activated Akt inhibited mitochondrial cytochrome c release and apoptosis following BID cleavage. Akt also antagonized tBID-mediated BAX activation and mitochondrial BAK oligomerization, two downstream events thought to be critical for tBID-induced apoptosis. Glucose deprivation, which impaired the ability of Akt to maintain mitochondrion-hexokinase association, prevented Akt from inhibiting BID-mediated apoptosis. Interestingly, tBID independently elicited dissociation of hexokinases from mitochondria, an effect that was antagonized by activated Akt. Ectopic expression of the amino-terminal half of hexokinase II, which is catalytically active and contains the mitochondrion-binding domain, consistently antagonized tBID-induced apoptosis. These results suggest that Akt inhibits BID-mediated apoptosis downstream of BID cleavage via promotion of mitochondrial hexokinase association and antagonism of tBID-mediated BAX and BAK activation at the mitochondria.

Animals↗
PubMed1998

Purification and kinetic characterization of hexokinase and glucose-6-phosphate dehydrogenase from Schizosaccharomyces pombe.

Hexokinase and D-glucose-6-phosphate dehydrogenase (G6PDH) from Schizosaccharomyces pmbe have been purified 250-fold by an identical three-step. Both enzymes are dimeric with a molecular mass of 88 kDa for the kinase and 112 kDa for the dehydrogenase. Steady-state kinetic studies were performed on hexokinase and G6PDH, which form the glucose phosphate branch of the oxidative pentose phosphate pathway of S. pombe (fission yeast). Hexokinase promotes Mg(2+)-activated phosphorylation of D-glucose by the equilibrium random Bi Bi mechanism with formation of the abortive enzyme-ADP-glucose complex. ADP inhibits the kinase competitively versus ATP and noncompetitively versus D-glucose. The Mg2+ activation of hexokinase is associated with an increase in the maximal velocity by its interaction with the ternary complex to facilitate the transfer of the phosphoryl group. G6PDH catalyzes NADP(+)-linked oxidation of D-glucose-6-phosphate by the ordered Bi Bi mechanism with NADP+ as the leading reactant. High NADP+ concentration inhibits the dehydrogenase by forming the dead-end ternary complex. In addition, G6PDH is also subjected to product inhibition by NADPH and noncompetitive inhibition by A(G)TP. Thus, the oxidative pentose phosphate pathway in S. pombe may be regulated via inhibition of hexokinase by ADP in conjunction with inhibition of G6PDH by NADPH and ATP.

Glucosephosphate Dehydrogenase↗
PubMed1982

Solubilization of hexokinase activity by an effect of thiopental on the mitochondrial membrane.

In thiopental anesthesia of rats cerebral mitochondrial hexokinase activity was solubilized. This solubilization was also observed when the period necessary for the removal of the rat brain was shortened to 15 s by brain blowing. The influence of the drug on the binding of hexokinase activity to mitochondria of brain, liver and neuroblastoma cells was studied in vitro. Solubilization of hexokinase activity was achieved in all systems at therapeutically relevant thiopental concentrations. On the other hand, chlorpromazine as a highly lipophilic drug only solubilized hexokinase activity at concentrations being already lytic to the membrane. Thus, it is concluded that thiopental solubilize hexokinase activity by affecting the mitochondrial membrane, and that this effect is not only dependent on the lipophilic character of a drug.

Anesthesia↗