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

The level of expression of the genes for hexokinase, aldose reductase and sorbitol dehydrogenase was investigated in lenses of mice and rats. These genes represent two separate but interrelated pathways for the metabolism of glucose in the cell. It is hypothesized that the extent of expression of the hexokinase gene may play an important role in the regulation of the levels of glucose in the lens. It is known that if there occurs a build up of intracellular glucose, such as in diabetes mellitus, activation of the aldose reductase/sorbitol dehydrogenase pathway may lead to various diabetic complications, including a lessening of lens clarity. We have therefore determined the levels of expression of the genes for these three enzymes in the lens of both mice and rats. Mice are known to be more resistant than rats to the development of lens opacification during hyperglycemia. By Northern blot hybridization analysis, and by quantitation of the resulting hexokinase, aldose reductase and sorbitol dehydrogenase mRNA hybrids, we found that in the mouse lens the expression of the hexokinase gene exceeded that of the aldose reductase gene by a factor of three, while in the rat it only approached about 1/4 that of the aldose reductase gene. The extent of expression of the SDH gene, however, was equal between the mouse and rat lenses. These results were calculated relative to the level of expression of the alpha A-crystallin gene in those two types of lenses, in order to account for the generally higher genetic expression found in the rat relative to the mouse lens due to its higher content of DNA, henceforth larger mass. The presence of high levels of hexokinase mRNAs relative to aldose reductase mRNAs in the lens would be expected to favor metabolism of glucose via the glycolytic pathway rather than the sorbitol pathway, leading to retardation of development of sugar cataracts in the mouse lens; while the opposite is true for the rat lens.
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PMID:Levels of expression of hexokinase, aldose reductase and sorbitol dehydrogenase genes in lens of mouse and rat. 831 91

Royal College of Surgeons (RCS) rats have hereditary retinal degeneration in association with posterior subcapsular opacities. Cataract formation is thought to be correlated with an increase in lipid peroxidation products in the vitreous (Zigler and Hess, 1985). In order to examine the possibility that parallel changes in enzyme activity are occurring within the lens, we analysed the activity of four key enzymes and the crystallin protein profile. We compared RCS rat lenses at three different stages of cataract formation to clear lenses of the nonpigmented RCS rat, lenses from pigmented RCS rat and to normal (Fisher) rat. Our data shows that concomitant with the appearance of the RCS cataract, the ratio of the crystallins beta 1, beta H and gamma to the total lens protein was reduced. The crystallin profile of a clear RCS lens was similar to that of a normal (Fisher) lens. No significant difference in the activity of the enzymes hexokinase and glucose-6-phosphate dehydrogenase (G6PD) was found among the lenses, however the activity of glutathione reductase and aldolase was reduced in the cataractous lenses.
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PMID:Enzyme activities and crystallin profiles of clear and cataractous lenses of the RCS rat. 840 88

We compared the metabolism of [1-13C]glucose by wild type cells of Neurospora crassa at normal growth temperature and at heat shock temperatures, using nuclear magnetic resonance analysis of cell extracts. High temperature led to increased incorporation of 13C into trehalose, relative to all other metabolites, and there was undetectable synthesis of glycerol, which was a prominent metabolite of glucose at normal temperature (30 degrees C). Heat shock strongly reduced formation of tricarboxylic acid cycle intermediates, approximately 10-fold, and mannitol synthesis was severely depressed at 46 degrees C, but only moderately reduced at 45 degrees C. A mutant strain of N. crassa that lacks the small alpha-crystallin-related heat shock protein, Hsp30, shows poor survival during heat shock on a nutrient medium with restricted glucose. An analysis of glucose metabolism of this strain showed that, unlike the wild type strain, Hsp30-deficient cells may accumulate unphosphorylated glucose at high temperature. This suggestion that glucose-phosphorylating hexokinase activity might be depressed in mutant cells led us to compare hexokinase activity in the two strains at high temperature. Hexokinase was reduced more than 35% in the mutant cell extracts, relative to wild type extracts. alpha-Crystallin and an Hsp30-enriched preparation protected purified hexokinase from thermal inactivation in vitro, supporting the proposal that Hsp30 may directly stabilize hexokinase in vivo during heat shock.
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PMID:Glucose metabolism in Neurospora is altered by heat shock and by disruption of HSP30. 1007 52