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PubMed1997

Fructose-3-phosphate production and polyol pathway metabolism in diabetic rat hearts.

Previous studies have suggested that polyol-pathway and nonenzymatic glycation may be involved in the development of cardiac myopathy, a well-known manifestation of diabetes. Although the exact etiology of this complication is not fully understood, it is likely to be multifactorial. In this study, we investigated the metabolic consequences of diabetes and the effect of aldose reductase inhibitor (ARI) treatment on cardiac tissues of Sprague-Dawley rats. Perchloric acid (PCA) extracts of hearts from the animals were examined using 31P-nuclear magnetic resonance (NMR), gas chromatography/mass spectrometry (GC/MS), and high-performance liquid chromatography (HPLC). In 31P-NMR spectra of diabetic animals, a peak resonating at the chemical shift of 5.8 ppm with a coupling constant of 10 Hz was identified as fructose-3-phosphate (F3P). Undetectable in controls (< approximately 20 nmol/g), this metabolite was present at a concentration of 81.3 +/- 16.3 nmol/g wet weight (n = 4) in diabetic rat hearts. GC/MS analysis of these extracts from diabetics also identified a decomposition product of F3P, 3-deoxyglucosone (3DG), at a concentration of 9.4 +/- 3.5 nmol/g (n = 3), compared with 0.98 +/- 0.43 nmol/g (n = 3) in controls. No evidence was found for the expected detoxification products of 3-DG, 3-deoxyfructose and 2-keto 3-deoxygluconate. Concomitant with the elevation of F3P and 3DG, fructose and sorbitol levels were also elevated in diabetic animals. Surprisingly, ARI treatment was found to have no effect on the levels of these metabolites. These data suggest that either the heart may be unique in its production of fructose or it may not readily transport the ARI sorbinil. Production of the potent glycating agents F3P and 3DG in diabetics suggests that these compounds may be contributing factors in the glycation of cardiac proteins in the diabetic rat heart.

Administration, Oral↗
PubMed1997

Charge interactions in sperm-egg recognition.

A novel method using derivatized agarose beads for investigating the types of molecules, when isolated from all others, that can form stable adhesive bonds, was recently described by Roque et al. (1996). The findings from this study were extended to living sea urchin cell systems. Both the bead results and the experiments with sea urchin cells suggested that phosphorylated amino acids can form stable adhesive bonds with positively charged peptides (Roque et al., 1996). As these experiments only examined phosphorylated amino acids, the validity of the hypotheses developed in the earlier study was dependent on extending the experiments to additional phosphorylated molecules. In this study, effects of D-mannose, D-mannose-1-phosphate, D-fructose, D-fructose-1-phosphate, maltose and maltose-1-phosphate on embryo cell reaggregation and sperm-egg interaction using untreated, jelly coat-free and vitelline layer disrupted Strongylocentrotus purpuratus sea urchin eggs were examined. The phosphorylated sugars (50 mM), and not their non-phosphorylated counterparts, strongly inhibited fertilization of the 3 types of eggs. ATP, at concentrations as low as 0.8 mM also completely inhibited fertilization. The phosphorylated sugars had little or no effect on reaggregating sea urchin blastula cells. A likely explanation of these results is that sperm-egg interaction in the sea urchin involves positively and negatively charged receptors; the positively charged receptors are blocked by exogenously added phosphorylated molecules. These and earlier studies indicate that by extending results from bead modeling studies to living systems, interesting information can be obtained regarding bonding mechanisms that may modulate adhesive interactions.

Adenosine Triphosphate↗
PubMed1987

Study of hereditary fructose intolerance by use of 31P magnetic resonance spectroscopy.

The effect of fructose on liver metabolism in patients with hereditary fructose intolerance (HFI) and in heterozygotes for HFI was studied by 31P magnetic resonance spectroscopy (31P-MRS). In patients with HFI (n = 5) ingestion of small amounts of fructose was followed by an increase in sugar phosphates and decrease in inorganic phosphate (Pi) in the liver that could be detected by 31P-MRS. 31P-MRS could be used to diagnose fructose intolerance and to monitor the patients' compliance with a fructose-restricted diet. In heterozygotes (n = 8) 50 g fructose given orally led to accumulation of sugar phosphates and depletion of Pi in the liver. Fructose also induced a larger increase in plasma urate in heterozygotes than in control subjects. The effect of fructose on liver Pi and plasma urate was most pronounced in heterozygotes with gout (n = 3). Heterozygosity for HFI may predispose to hyperuricaemia.

Carbohydrate Metabolism, Inborn Errors↗
PubMed1999

Phosphofructokinase-1 from Saccharomyces cerevisiae: analysis of molecular structure and function by electron microscopy and self-catalysed affinity labelling.

Conventional and cryoelectron microscopy portray native octameric yeast phosphofructokinase-1 (PFK) as consisting of two identical heterotetrameric tetrahedron-like moieties being rotated relative to each other. Immunoelectron microscopy employing subunit-specific IgG identifies alpha-type subunits in the contact zone of the two tetrahedrons, while beta-chains are recognized exclusively at the tips of the octamer. The chemical reaction of phosphofructokinase with analogues of fructose 6-phosphate followed by autocatalytic phosphoryl transfer from [gamma-32P]-ATP results in a specific labelling of the alpha-subunit. AMP and fructose 2,6-bisphosphate affect labelling by stimulating the binding of substrate analogue; AMP additionally promotes phosphoryl transfer. No stimulation of labelling is observed with proteolytically modified tetrameric 12-S phosphofructokinase.

Adenosine Monophosphate↗
PubMed1981

Lithium inhibition of phosphofructokinase.

The mode of action of lithium in prophylaxis of recurrent affective disorder is unknown although it has been suggested that lithium might compete with magnesium in magnesium dependent processes. We have previously shown pyruvate kinase to be inhibited by lithium and the present study demonstrates a small inhibition by lithium of phosphofructokinase that is also a major regulatory step in glycolysis. Inhibition of PFK was competitive with respect to ATP and magnesium and noncompetitive with respect to potassium and fructose-6-phosphate. Inhibition was enhanced at reduced concentrations of magnesium.

Adenosine Triphosphate↗
PubMed2002

A radioassay for phosphofructokinase-1 activity in cell extracts and purified enzyme.

Phosphofructokinase-1 plays a key role in the regulation of carbohydrate metabolism. Its activity can be used as an indicator of the glycolytic flux in a tissue sample. The method most commonly employed to determine phosphofructokinase-1 activity is based on oxidation of NADH by the use of aldolase, triosephosphate isomerase, and alpha-glycerophosphate dehydrogenase. This method suffers from several disadvantages, including interactions of the auxiliary enzymes with phosphofructokinase-1. Other methods that have been used also require auxiliary enzymes or are less sensitive than a coupled assay. Here, we propose a direct method to determine phosphofructokinase-1 activity, without the use of auxiliary enzymes. This method employs fructose-6-phosphate and ATP labeled with 32P in the gamma position ([gamma-32P]ATP), and leads to the formation of ADP and fructose-1,6-bisphosphate labeled with 32P ([1-32P]fructose-1,6-bisphosphate). Activated charcoal is used to adsorb unreacted [gamma-32P]ATP, and the radioactive product in the supernatant, [1-32P]fructose-1,6-bisphosphate, is analyzed on a liquid scintillation counter. The proposed method is precise and relatively inexpensive, and can be applied to determine phosphofructokinase-1 activity in cellular extracts as well as in the purified enzyme.

Adenosine Triphosphate↗
PubMed1998

Essential histidyl residues at the active site(s) of sucrose-phosphate synthase from Prosopis juliflora.

Chemical modification of sucrose-phosphate synthase (EC 2.4.1.14) from Prosopis juliflora by diethyl pyrocarbonate (DEP) and photo-oxidation in the presence of rose bengal (RB) which modify the histidyl residues of the protein resulted in the inactivation of the enzyme activity. This inactivation was dependent on the concentration of the modifying reagent and the time of incubation and followed pseudo-first order kinetics. For both the reagents, the inactivation was maximum at pH 7.5, which is consistent with the involvement and presence of histidine residues at the active site of the enzyme. Substrates, UDPG and F6P protected the enzyme against the inactivation by the modifying reagents suggesting that the histidine residues may be involved in the binding of these substrates and are essential for the catalytic activity. Specificity of DEP was indicated by an increase in absorbance at 240 nm along with concomitant inactivation of the enzyme and reactivation of the modified enzyme by hydroxylamine. These results strongly suggest the presence of histidine residue(s) at or near the active site of the enzyme.

Amino Acid Sequence↗
PubMed1975

Effects of calcium ions on pyruvate kinase from human erythrocytes.

Ca2+ ions have a biphasic effect on the allosteric pyruvate kinase (EC 2.7.1.40) from human erythrocytes: Ca2+ is an activator at low phosphoenolpyruvate (PEP) concentrations: at increased PEP concentrations Ca2+ behaves as an inhibitor. In the presence of ATP the same effect was observed and at low PEP concentrations Ca2+ ions can completely abolish the ATP inhibitory effect. At high Ca2+ concentrations there is a loss of the cooperativity towards PEP. The enzyme activated by fructose-1,6-diphosphate (FDP) is inhibited by Ca2+ ions at all concentrations of PEP tested. Mg2+ ions are not able to counteract the activation by Ca2+ ions at low PEP concentrations. The results are interpreted on the basis of the model of Monod.

Adenosine Triphosphate↗
PubMed1975

Modification of pyruvate kinase isozymes in prolonged primary cultures of adult rat hepatocytes.

Pyruvate kinase isozymic changes were studied in the adult hepatocyte cultures, by electrophoretic, kinetic and immunological methods. We were able to maintain parenchymal cells from normal adult rat liver in non-proliferating monolayer cultures up to 10 days. Hepatocytes appeared to contain a dominant PK I type up to 4-5 days of culture. After day 5, PK III type was regularly present with PK I and after 7 days PK III type was always the only isozyme detected in culture. It must be pointed out that, by the Ouchterlony method and sometimes by electrophoresis, concentrated extracts from freshly isolated hepatocytes or starting hepatocyte cultures did also contain Pyruvate kinase PK III type. These results suggest that Pyruvate kinase III is present but partly repressed in the adult parenchymal cells and becomes derepressed in culture.

Aging↗
PubMed2000

Regulation of glycolysis during acclimation of scallops (Patinopecten yessoensis Jay) to anaerobiosis.

Some glycolytic metabolites in the adductor muscle were measured after transfer of scallops from aerobic to anaerobic saltwater for 12 h. The level of octopine increased gradually during the initial 3 h incubation, and thereafter the level increased rapidly up to 12 h. The ATP level also did not show any significant change for the initial 3 h, and then decreased rapidly. The fructose 2,6-biphosphate (Fru 2,6-BP) level increased drastically during the initial 3 h incubation, but thereafter the level did not show any significant change up to 12 h. In the short-term effects of anaerobiosis for 90 min, the level of fructose 6-phosphate (Fru 6-P) increased just after transfer to anaerobiosis, and then its level decreased. In contrast, the fructose 1,6-biphosphate (Fru 1,6-BP) level increased greatly, at the time when both glucose 6-phosphate (Glc 6-P) and Fru 6-P decreased. The Fru 2,6-BP level did not any significant change during the initial 15 min incubation, but thereafter the level increased gradually up to 90 min. Scallop 6-phosphofructo 1-kinase (EC 2.7.1.11) (PFK1) was strongly activated by 1 microM Fru 2,6-BP when 0.2 mM Fru 6-P was used as a substrate, but the activity was not affected at 5 mM Fru 6-P. In view of these results, the regulation mechanism of glycolysis is discussed.

Adenosine Triphosphate↗
PubMed1999

Ribose 1,5-bisphosphate regulates rat kidney cortex phosphofructokinase.

Phosphofructokinase (EC 2.7.1.11) is a major enzyme of the glycolytic pathway, catalyzing the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate. In this study, we demonstrated the effect of ribose 1,5-bisphosphate on phosphofructokinase purified from rat kidney cortex. Ribose 1,5-bisphosphate relieved the phosphofructokinase from ATP inhibition and increased the affinity for fructose 6-phosphate at nanomolar concentrations. These activating effects of ribose 1,5-bisphosphate were enhanced in the presence of AMP. Ribose 1,5-bisphosphate reduced the inhibition of the phosphofructokinase induced by citrate. These results suggest that ribose 1,5-bisphosphate is an activator of rat kidney cortex phosphofructokinase and synergistically regulates the enzyme activity with AMP.

Adenosine Monophosphate↗