Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.1.1 (
hexokinase
)
5,274
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The accumulations by axoplasmic transport of selected enzyme activities proximal and distal to a ligature placed on the sciatic nerve were monitored in rats exposed in utero to maternal antibodies to nerve growth factor (NGF) and in control rats. Littermates of the animals exposed to anti-NGF were shown elsewhere to have had a 70% reduction in the number of sensory neurons in dorsal root ganglia and a 90% reduction in number of neurons in superior cervical (sympathetic) ganglion. The accumulation of F(-)-sensitive acid phosphatase activity was depressed 75% both proximal and distal to the tie. Accumulation of F(-)-resistant acid phosphatase activity was depressed nearly 50% proximal to the tie. Distal accumulation of this activity did not occur in either group of rats. Accumulation of
acetylcholinesterase
activity was depressed 30%. Distal accumulation of the activities of beta-glucuronidase and
hexokinase
was depressed 50%. In the lumbar dorsal root ganglia, dry weight was reduced 40%, and the activities of peroxide-sensitive, F(-)-resistant acid phosphatase and of the mitochondrial enzymes
hexokinase
, glutamic dehydrogenase, glutamic-oxalacetic transaminase, and NAD-dependent isocitric dehydrogenase were all reduced a little more, 45--50% per ganglion. However, the activities of the lysosomal enzymes, F(-)-sensitive acid phosphatase and beta-glucuronidase, of the peroxide-resistant, F(-)-resistant acid phosphatase, and of the mitochondrial enzyme glutaminase were all reduced about 60% per ganglion. The results of these measurements were interpreted to suggest that much, and perhaps all, of the F(-)-sensitive acid phosphatase activity in motion in peripheral nerve in rat is confined to sensory axons.
...
PMID:Transported enzymes in sciatic nerve and sensory ganglia of rats exposed to maternal antibodies against nerve growth factor. 616 7
The effect of tris-(2-chloroethyl)-amine (HN-3) on RNA and DNA was investigated spectrophotometrically. The shift in the absorbance spectrum caused by the addition of HN-3 was used to test a variety of compounds for their ability to inhibit RNA alkylation. The effect of HN-3 on the activity of several enzymes was also investigated. The activities of ribonuclease A, desoxyribonuclease I,
acetylcholinesterase
, diaphorase, glutathione reductase, adenosine desaminase, glyoxalase I, 3-hydroxyacyl-CoA-dehydrogenase, xanthine oxidase, glucose-6-phosphate dehydrogenase,
hexokinase
and the microsomal N-oxygenation of aniline were not changed by HN-3, whereas the activity of cytochrome-c-reductase exhibited a dose dependent diminution in the presence HN-3. Of 105 compounds tested only 14, namely, sodium thiosulfate, dithioxanthine, thiosalicylic acid, 1,2,4-triazole-5-thiol, 2-thiocytosine, 2-thiohistadine, 2,3-dithiosuccinic acid, thioglycolic acid, 3-mercapto-D-valine,6-amino-2-thiouracil, thionicotine amide, dithiothreitol, sodium sulfite, and ergothioneine prevented the alkylation of RNA. All of them also reacted with HN-3 in absence of RNA. No correlation was found between the reaction constant of the reaction compound:HN-3 in the absence of RNA and the concentration of the compound which inhibited RNA alkylation by 50%. The compounds which were effective in vitro were also tested in mice for their ability to reduce HN-3 toxicity in vivo. Only sodium thiosulfate, d-penicillamine, and dithiosuccinic acid were effective. A 3.9fold increase in the LD50 of HN-3 was achieved in mice treated with sodium thiosulfate 3330 mg/kg i.p., a 1.7fold with 2125 mg dithiosuccinic acid/kg, and a 2fold increase with 2500 mg/kg d-penicillamine. The compound tested was injected i.p. 0.5 to 1 min after the s.c. injection of HN-3.
...
PMID:Effect of various compounds on the reaction of tris-(2-chloroethyl)amine with ribonucleic acid in vitro and on its toxicity in mice. 617 33
The distribution of
hexokinase
, a general glycolytic enzyme, was compared to that of cytochrome oxidase and
acetylcholinesterase
(
AChE
) in the somatosensory cortex and the superior colliculus of the rat. The vibrissal barrel fields of the adult rat contain high
hexokinase
and cytochrome oxidase activity and low
AChE
activity. In the superior colliculus,
hexokinase
activity was highest in cell layers and discrete foci of intense activity were observed in the deep grey layer. This distribution was different from that of both cytochrome oxidase and
AChE
in this structure.
...
PMID:The distribution of hexokinase compared to cytochrome oxidase and acetylcholinesterase in the somatosensory cortex and the superior colliculus of the rat. 631 13
The regional enzyme activities of glucose metabolism in the rat brain were investigated. Hexokinase (
EC 2.7.1.1
) and pyruvate dehydrogenase (EC 1.2.4.1), key enzymes for glucose metabolism, showed no changes in activity in all the regions studied of the aging brain as compared with the adult brain. However, the activity of D-3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is low throughout the adult brain and, in contrast with
hexokinase
and pyruvate dehydrogenase, its activity decreases significantly during aging. Other enzymes that showed significant decreases during aging are aldolase (EC 4.1.2.13), lactate dehydrogenase (EC 1.1.1.27), citrate synthase (EC 4.1.3.7), and NAD+-linked isocitrate dehydrogenase (EC 1.1.1.41). The catabolic enzyme in cholinergic metabolism,
acetylcholinesterase
(
EC 3.1.1.7
), selected as an example of a non-energy-metabolising enzyme, also showed significant decreases in all regions of the brain in aging, although its highest activity remained in the striatum. These results are discussed with respect to the energy metabolism in various brain regions and their status with aging.
...
PMID:Energy-metabolizing enzymes in brain regions of adult and aging rats. 646 Aug 51
When studying enzymic activities in successively chosen portions of solutions of pyruvatekinase,
hexokinase
, lactatedehydrogenase, alkaline phosphatase,
acetylcholinesterase
and trypsin fast macroscopic fluctuations were revealed. These fluctuations were found earlier in protein preparations of the actomyosin complex and creatinkinase and described as "conformation fluctuations". Similar macroscopic fluctuations were also revealed when measuring the rate of reaction between ascorbic acid and dichlorphenolindophenol (DCAPI). The spectra of macroscopic fluctuations in solutions of different proteins and ascorbic acid+DCAPI are similar to each other in principle. This gives grounds to consider the ability towards macroscopic fluctuations to be a common property of solutions of different substances.
...
PMID:[Macroscopic fluctuations--a general property of aqueous solutions of different proteins and other substances. Statistical spectral analysis of macroscopic fluctuations]. 739 55
Erythrocyte aspartate aminotransferase (AST) and alanine aminotransferase (ALT) activities are often used as indices of vitamin B-6 nutritional status; however, results using a mixed population of erythrocytes can be quite variable. Erythrocytes from two strains of mice (Mus domesticus), A/Ibg and DBA/Ibg, were separated according to age by centrifugation through discontinuous Percoll density gradients into three fractions: top (least dense, youngest), middle and bottom (most dense, oldest). A sufficient yield of age-fractionated erythrocytes was obtained from a single mouse for all of the enzyme measurements. The activities of AST, ALT and three age-marker enzymes, pyruvate kinase,
acetylcholinesterase
and
hexokinase
, were found to be significantly higher in the youngest cell fractions, and declined in the older, more dense fractions. A mice had significantly lower AST and ALT activities in the age separated fractions than did DBA mice. The measurement of enzyme activities in low density, young cells may be especially useful in studies involving conditions in which the proportion of young erythrocytes may be elevated with respect to the entire erythrocyte mass.
...
PMID:Aminotransferase activities in mouse, Mus domesticus, erythrocytes separated according to age. 755 57
The maximal rates (Vmax) of some enzyme activities related to synaptosomal energy metabolism were studied in different types of synaptosomes from cerebellar cortex of Macaca Fascicularis (Cynomolgus monkey). Different synaptosomal populations, namely "large" and "small" synaptosomes, were isolated from the anterior lobule of the cerebellar cortex of monkeys treated p.o. with dihydroergocriptine at the dose of 12 mg/kg/day before and during the induction of a Parkinson's-like syndrome by MPTP administration (i.v., 0.3 mg/kg/day for 5 days). The enzymes were chosen according to their regulatory role and as markers of the following metabolic pathways: (a) glycolysis ((
hexokinase
, phosphofructokinase, lactate dehydrogenase), (b) Krebs' (TCA) cycle (citrate synthase, malate dehydrogenase), (c) amino acid, glutamate metabolism (glutamate dehydrogenase, glutamate-pyruvate- and glutamate-oxaloacetate-transaminases), (d) acetylcholine catabolism (
acetylcholinesterase
) and (e) ATPases, i.e. Na(+)-K(+)-ATPase, Mg(2+)-ATP synthetase, Mg(2+)-ATPase, Ca(2+)-Mg(2+)-ATPase and Ca(2+)-ATPase Low and High affinity for Ca2+. The MPTP administration modified the activities of citrate synthase, malate dehydrogenase, Na(+)-K(+)-ATPase,
acetylcholinesterase
and glutamate-oxaloacetate transaminase only on selected types of synaptosomes. Pharmacological treatment by dihydroergocriptine was able to recovery at the steady-state levels the activities of these enzymes, thus demonstrating a partial protective effect on these biochemical parameters.
...
PMID:Parkinson-like disease by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) toxicity in Macaca fascicularis: synaptosomal metabolism and action of dihydroergocriptine. 817 63
We show here that carbamylcholine (acetylcholine agonist) or pyridostigmine (
acetylcholinesterase
inhibitor), drugs which are widely used in medical treatments, exerted a rapid reduction in mitochondrial-bound
hexokinase
. This reduction was inversely proportional to the changes in glucose-6-phosphate levels in skeletal and heart muscle. Increased concentration of acetylcholine, occurring in various diseases or induced by
acetylcholinesterase
inhibitors, was reported to cause deterioration of mitochondrial function, resulting in heart and muscle damage. The present experiments suggest that the reduction in mitochondrial-bound
hexokinase
, which is closely linked to intramitochondrial oxidative metabolism, may play an important role in the mechanism which leads to tissue damage.
...
PMID:Effects of carbamylcholine and pyridostigmine on mitochondrial-bound hexokinase in skeletal muscle and heart. 881 28
Rasagiline (N-propargyl-1-(R)-aminoindan) is a selective, irreversible monoamine oxidase B (MAO B) inhibitor which has been developed as an anti-Parkinson drug. In controlled monotherapy and as adjunct to L-dopa it has shown anti-Parkinson activity. In cell culture (PC-12 and neuroblastoma SH-SY5Y cells) it exhibits neuroprotective and anti-apoptotic activity against several neurotoxins (SIN-1, MPTP, 6-hydroxydopamine and N-methyl-(R)-salsolinol) and ischemia. In vivo, it reduces the sequelae of traumatic brain injury in mice and speeds their recovery. The neuroprotective activity of rasagaline does not result from MAO B inhibition, since its S-enantiomer, TVP1022, which has 1000-fold weaker MAO inhibitory activity, exhibits similar neuroprotective properties. Introduction of a carbamate moiety into the rasagiline molecule to confer
cholinesterase
inhibitory activity for the treatment of Alzheimer's disease, resulted in compounds TV3326 [(N-Propargyl-(3R)Aminoindan-5-YL)-Ethyl Methyl Carbamate] and its S-enantiomer TV3279 [(N-Propargyl-(3S)Aminoindan-5-YL)-Ethyl Methyl Carbamate], which retain the neuroprotective activities of rasagiline and TVP1022. They also antagonize scopolamine-induced impairments in spatial memory. In addition, TV3326 exhibits brain-selective MAO A and B inhibitory activity after chronic administration and has antidepressant-like activity in the forced swim test. This is associated with an increase in brain levels of serotonin. The anti-apoptotic activity of these propargylamine-containing derivatives may be related to their ability to delay the opening of voltage-dependent anion channels (VDAC), which are part of the mitochondrial permeability transition pore. The propargylamine moiety is responsible for the increase in the mitochondrial family of Bcl-2 proteins, prevention in the fall in mitochondrial membrane potential, prevention of the activation of caspase 3, and of translocation of glyceraldehyde-3-phosphate dehydrogenase from the cytoplasm to the nucleus. The latter processes are closely associated with neurotoxin-induced apoptosis. Rasagiline interacts with and prevents the binding of PKI 1195 to the pro-apoptotic peripheral benzodiazepine receptor, which together with Bcl-2,
hexokinase
, porin, and adenine nucleotide translocator constitutes part of the VDAC. Furthermore, rasagiline, TV3326 and TV3279 are able to influence the processing of amyloid precursor protein by activation of alpha-secretase and increasing the release of soluble alpha APP in rat PC-12 and human neuroblastoma SH-SY5Y cells and in rat and mice cortex and hippocampus. This process has been shown to involve the upregulation of PKC and MAP kinase. It is quite likely that the induction of Bcl-2 and activation of PKC by rasagiline and TV3326 is closely linked to the anti-apoptotic action of these drugs and their ability to process APP by activation of alpha-secretase.
...
PMID:Molecular basis of neuroprotective activities of rasagiline and the anti-Alzheimer drug TV3326 [(N-propargyl-(3R)aminoindan-5-YL)-ethyl methyl carbamate]. 1204 33
Determination of erythrocyte number and their indices and enzymatic activity of: glucose-6-phosphate dehydrogenase (G-6PD), superoxide dismutase (SOD),
acetylcholinesterase
(AchE), glutathione reductase (GR) and
hexokinase
(Hx) in peripheral blood erythrocytes of workers chronically exposed to mercury vapours during the production of chloride (the mercuric electrolysis method). The studied workers were equipment operators, electricians and electrolysis maintenance men at the chloride production department using the mercuric electrolysis method. The study involved 46 men, aged 21 to 56, (x = 39 +/- 10.4) exposed to mercury vapours for the period from 7 months to 32 years (x = 14.7+/-10.8), working in a three shift system, for 8 hours a day. Smokers constituted 50% of the studied group (23 men). Urine mercury concentrations of workers exposed to mercury vapours were in the range from 10 to 215 microg/dm3 (x = 81,4 +/- 72,9) and in blood in range 4 do 72 microg/dm3 (x=16.3 +/- 15,0). Controls were 46 men aged 20-54, (x=33.6 +/- 9.8), workers and voluntary blood donors, who never experienced occupational exposure to mercury vapours or other chemicals, and to physical agents. The percentage of smokers in the control group was 34.7% (16 men). Basic haematological determinations (hematocrit - Hct, Hb concentration, erythrocyte number in mm3 of blood, mean red cell hemoglobin concentration (MCHC), mean red cell volume (MCV) and enzymatic studies (activity of G-6PD, SOD, AchE, GR, Hx) in peripheral blood samples obtained from workers and controls were performed. Hematological parameters of the peripheral blood were determined using AVL 808 hematological counter, following the manufacturer's instructions. Activity of the studied enzymes was estimated by the spectrophotometric method described by Beutler, following the recommendations of the International Committee for Standardisation in Hematology. Values of Ht were higher in all the subgroups exposed to Hg workers (divided according to duration of exposure or urine mercury concentrations) in comparison to the control group. The erythrocyte number in mm3 of peripheral blood was also higher in the exposed workers group than in controls. MCHC in the total group exposed to mercury vapours was lower than in the controls. In the subgroup exposed to mercury vapours for < 10 years, the value of this parameter was lower than in the control group; whereas in the subgroups separated in respect to mercury concentration in the urine, it was lower only in workers showing the highest urine concentration of this metal. In workers exposed to mercury vapours, MCV index values were lower than in the controls. In the subgroups of workers who smoked and those who did not smoke, they were also lower than in the controls; whereas in the group of the longest exposed workers from 21 to 35 years, it was found to be higher than in controls. The activity of G6PD was lower in the group of subjects occupationally exposed to mercury vapours than in the control group - 5.60 +/- 1.60 and 7.41 +/- 0.43 IU/gHb respectively. When comparing the subgroups of smokers and non-smokers with the controls, workers showed lower G6PD activity than in the matching control subgroups - 6.24 +/- 1.97 and 7.44 +/-0.22 IU/gHb in the subgroups of smokers and 4.97 +/- 0.72 and 7.38 +/- 0.18 IU/gHb in non-smokers respectively. Erythrocyte G6PD activity was lower in all studied groups separated in respect to exposure time - 5.54 +/- 1.75, 6.02 +/- 2.05 and 5.54 +/- 1.05 IU/gHb respectively. The same pattern of changes was observed in the subgroups separated in respect to mercury concentration in the urine compared to the controls. The lowest enzyme activity was found in the subgroups showing the highest mercury concentration in the urine wnen compared with the subgroup with the lowest urine concentration of this metal - 5.19 +/- 1.50 and 6.00 +/- 1.84 IU/gHb respectively SOD activity in the group of workers exposed to mercury was lower compared to the controls - 2289.97 +/- 122.31 and 2418.03 +/- 60.28 IU/gHb respectively. The smoking and non-smoking workers showed respective SOD activities on - 2305.43 +/- 102.75 and 2274.50 +/- 124.5 IU/gHb; whereas in the matching subgroup of controls - 2452.11 +/- 88.72 and 2382.09 +/- 91.22 IU/gHb, respectively. The activity of this enzyme in all investigated groups selected in respect to length of employment, revealed lower values when compared with the controls - 2271.20 +/- 115.23 in the group with under 10 years of exposure, 2335.11 +/-167.71 IU/gHb in those exposed for 11-20 years, and 2290.40 +/- 26.12 IU/gHb in the subgroup exposed for the longest period of time. Similar changes were observed in the activity of this enzyme in the subgroups separated in respect to mercury concentration in the urine when SOD activity was compared with the controls. The AchE activity was higher in the group exposed to mercury vapours compared to the controls and the respective values were - 50.22 +/- 14.44 and 36.87 +/- 2.92 IU/gHb. In the subgroups separated in respect to length of exposure, the activity of this enzyme was statistically significantly higher than in the control group. The GR activity levels were lower in the exposed group - 8.01 +/-2.54 IU/gHb, compared to the controls - 10.24 +/- 1.24 IU/gHb. In the subgroups of smokers and non-smokers, GR activity was lower, 8.48 +/- 2.37 and 7.54 +/- 2.68 IU/gHb, compared to smokers and non-smokers in the control group, 10.26 +/- 1.01 and 10.16 +/- 1.03 IU/gHb, respectively. The GR activity was also statistically significantly lower in all groups separated in respect to duration of exposure, with the values of 8.56 +/-2.39, 8.26 +/- 2.38, 7.06 +/- 2.75 IU/gHb, respectively in subject groups and 10.24 +/- 1.35 in the control group. Similar changes were noticed in the subgroup separated in respect to mercury concentration in the urine. The Hx activity was lower in the group exposed to mercury vapours - 1.08 +/-0.11. compared with the controls - 1.21 +/- 0.16 IU/gHb. The enzyme activity showed a similar pattern in the subgroups separated in respect to duration of exposure when they were compared with the control group. Exposure to mercury vapours present changes in the red blood cells, manifested by increased (when compared with the control group), number of erythrocytes in peripheral and decreased mean cell volume and mean cell hemoglobin concentration values, as well as changes in the metabolic processes occurring in the erythrocytes. In subjects exposed to mercury vapours some metabolic processes may be additionally modified by addiction to cigarette smoking.
...
PMID:[Red cell system and selected red cell enzymes in men occupationally exposed to mercury vapours]. 1778 49
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