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

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Query: EC:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Analysis of slow axonal transport in sciatic and primary visual systems of BB rats with spontaneous diabetes of 2.5-3.5 months duration revealed a delay in transport of the neurofilament (NF) subunits, tubulin, actin, and the 60, 52, and 30 kDa polypeptides in both systems. The polypeptides examined were not affected uniformly. Rather, the transport of the 60, 52, and 30 kDa polypeptides and the rapidly moving component of tubulin, all constituents of the slow component b (SCb) of axonal transport, appeared to be more severely delayed than the transport of polypeptide constituents of the slow component a (SCa), such as NF and the slow-moving tubulin. Transport was not impaired in diabetic BB rats maintained normoglycemic with optimal doses of insulin. A 52 kDa polypeptide constituent of SCb was identified as neuron-specific enolase, and the 30 and 60 kDa polypeptides are likely to be aldolase and pyruvate kinase; all 3 are glycolytic enzymes. Morphometric analysis revealed that the cross-sectional area of sciatic axons was increased proximally at the level of the motor roots and decreased distally at the level of the tibial nerve. The changes in slow transport and caliber observed in central and peripheral axonal systems of diabetic BB rats are virtually identical to those previously described in rats with streptozotocin-induced diabetes, another model of insulin-dependent diabetes. In both models, the alterations of axonal caliber are likely to be secondary to the impairment of axonal transport.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Experimental diabetic neuropathy: similar changes of slow axonal transport and axonal size in different animal models. 336 21

Eight enzymes, e.g. lactate dehydrogenase, malate dehydrogenase, fructose-diphosphate aldolase, sorbitol dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphofructokinase and pyruvate kinase were estimated quantitatively in the rat lens from 37 to 1,211 days of age, by spectrophotometric methods. The activity was expressed as mU/g LWW. All enzymes measured showed declining activities, but LDH, ALD, SDH, G-6-PDH, HK and PFK gave a significant decrease during ageing when plotted semi-logarithmically from 37 to 1,211 days. SDH and G-6-PDH showed a statistically significant difference between the enzymes from the male and the female lenses. The female lens always had a lower activity than the male lens. Of all enzymes the specific activity, expressed as mU/l mg protein, was calculated. This specific activity appeared to be rather constant during ageing, except for ALD. In the female lenses, the specific activity of 7 enzymes was lower than in the male lenses. For ALD the specific activity decreased significantly in the male lens from 5.32 at 37 days to 0.88 at 1,211 days. In the female lens this significant decrease was from 4.97 to 0.81.
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PMID:The quantification of eight enzymes from the ageing rat lens, with respect to sex differences and special reference to aldolase. 340 13

The activities of hexokinase, phosphofructokinase, aldolase, enolase and pyruvate kinase were studied in breast cancer tissues, in comparison to benign breast disease and normal breast tissues. The enzyme activities in breast cancer were significantly increased compared to normal and benign breast tissues (p less than 0.001). Also the increase in activity in benign disease compared to normal was statistically significant (p less than 0.001). Within the group of benign diseases, fibroadenomas could be distinguished from fibrocystic disease, the former generally showing higher activities compared to the latter (p less than or equal to 0.05). Carcinoma subgroups, classified according to their histology, could not be recognized enzymologically. In addition, isozyme composition of pyruvate kinase and enolase was studied. We did not find a significant shift towards K type pyruvate kinase expression in benign disease compared to normal breast tissues. Also fibroadenomas did not differ from fibrocystic disease. However, the amount of K type pyruvate kinase in carcinomas proved to be significantly higher in comparison to benign disease and normal breast tissues (p less than 0.001). Expression of alpha gamma-enolase in normal breast tissue was virtually absent. In benign disease only a minority of specimens did show the hybrid alpha gamma-enolase. Nearly all carcinomas had alpha gamma-enolase expression and in 20% of the carcinomas gamma gamma-enolase could be detected (so-called neuron-specific enolase). By discriminant analysis, the function giving the best discrimination compared to the histological data was based on natural logarithm aldolase and the total of gamma-enolase subunits. Contrary to expectation, the regulator enzymes of glycolysis; i.e., hexokinase, phosphofructokinase and pyruvate kinase were not included in this discriminant function. The best fit produced a 90% correct classification in both benign and malignant disease. If these findings are confirmed to a larger series, the discrimination is sufficiently strong to form the basis of a clinically useful tool.
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PMID:Glycolytic enzymes in breast cancer, benign breast disease and normal breast tissue. 344 71

The molecular architecture of the rabbit skeletal muscle aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) tetramer has been determined to 2.7-A resolution. Solution of the three-dimensional structure of rabbit muscle aldolase utilized phase information from a single isomorphous Pt(CN)4(2-) derivative, which was combined with iterative-phase refinement based upon the noncrystallographic 222-fold symmetry exhibited by the tetramer subunits. The electron-density map calculated from the refined phases (mf = 0.72) was interpreted on the basis of the known amino acid sequence (363 amino acids per subunit). The molecular architecture of the aldolase subunit corresponds to a singly wound beta-barrel of the parallel alpha/beta class structures as has been observed in triose phosphate isomerase, pyruvate kinase, phosphogluconate aldolase, as well as others. Close contacts between tetramer subunits are virtually all between regions of hydrophobic residues. Contrary to other beta-barrel structures, the known active-site residues are located in the center of the beta-barrel and are accessible to substrate from the COOH side of the beta-barrel. Biochemical and crystallographic data suggest that the COOH-terminal region of aldolase covers the active-site pocket from the COOH side of the beta-barrel and mediates access to the active site. On the basis of sequence studies, active-site residues as well as residues lining the active-site pocket have been totally conserved throughout evolution. By comparison, homology in the COOH-terminal region is minimal. It is suggested that the amino acid sequence of the COOH-terminal region may be, in part, the basis for the variable specific activities aldolases exhibit toward their substrates.
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PMID:Molecular architecture of rabbit skeletal muscle aldolase at 2.7-A resolution. 347 68

Neurone-specific enolase (NSE) and the brain form of creatine phosphokinase (CPK-BB) were previously found to be present in rat synaptosomal plasma membranes (SPM) using two-dimensional gel (2-D gel) and peptide analysis; enzymatic activities of these and of pyruvate kinase (PK), all involved in ATP generation, were shown to be "cryptic" unless the SPM were treated with Triton X-100. We now show that enzymatic activation also occurs when the SPM are treated with trifluoperazine (TFP). TFP activation occurred even when the enzymes were membrane associated, showing that solubilization was not responsible for "unmasking" the enzyme activities. When TFP treatment was performed at alkaline instead of neutral pH, NSE and CPK-BB were released as well as PK, nonneuronal enolase, and aldolase which were identified by 2-D gel and tryptic peptide analysis. Other proteins released included calmodulin, actin, and the 70-kilodalton heat-shock cognate protein. Tubulin, synapsin I, and a 35-kilodalton basic protein were largely unaffected. The latter was identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase on the basis of 2-D gel and peptide analyses and subsequent partial sequencing of a rat brain cDNA coding for the same protein. TFP treatment is thus useful for activating latent enzymes as well as for distinguishing enzymes that have a different disposition on the membrane.
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PMID:Trifluoperazine activates and releases latent ATP-generating enzymes associated with the synaptic plasma membrane. 358 33

The enzyme level profiles of some regulatory enzymes and the isozyme patterns of some marker enzymes in bovine adult specialized, adult ordinary and fetal ordinary heart muscles were examined in order to biochemically characterize specialized heart muscle. The activities of hexokinase, phosphofructokinase and glucose-6-phosphate dehydrogenase in adult specialized heart muscle were significantly higher than those in adult ordinary heart muscle, but were similar to those in fetal ordinary heart muscle. The carnitine content and carnitine acetyltransferase activity in adult specialized heart muscle were lower than those in adult ordinary heart muscle. The isozyme patterns of creatine kinase, fructose-bisphosphate aldolase and pyruvate kinase in adult specialized heart muscle resembled those in fetal ordinary heart muscle. These results indicate that adult specialized heart muscle has the biochemical characteristics of fetal ordinary heart muscle.
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PMID:Biochemical characterization of the conduction system of the bovine heart. 359 6

A gel electrophoretic technique was used to demonstrate an interaction with the soluble enzymes aldolase, glyceraldehydephosphate dehydrogenase, pyruvate kinase and muscle type lactate dehydrogenase to the cytoskeletal protein tubulin. It is suggested that tubulin, like actin, is a key cytoskeletal structure with which soluble proteins may associate.
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PMID:Demonstration of tubulin-glycolytic enzyme interactions using a novel electrophoretic approach. 361 4

Cytoplasmic beta-actin and five glycolytic enzyme cDNAs were isolated from a rat skeletal muscle cDNA library and together with a genomic clone of rat cytochrome c were used as probes to quantitate the respective RNA transcription rates in isolated nuclei run off transcription assays from stationary cells cultured under normal or 2% oxygen. The transcription rates of lactate dehydrogenase, pyruvate kinase, triosephosphate isomerase and aldolase increased by 2-5 fold during the 72 hr exposure to 2% oxygen. There was a small increase in actin RNA transcription while both cytochrome c and glyceraldehyde-3-phosphate dehydrogenase RNA transcription rates decreased. Since previous studies demonstrated an increase in steady state glyceraldehyde-3-phosphate dehydrogenase RNA during low O2 exposure it is concluded that the level of this RNA is regulated post transcriptionally whereas the other four glycolytic enzyme RNAs are regulated at least partially at the level of transcription by oxygen availability. The relative transcriptional rates of the RNAs in this study are related to their cellular RNA and protein concentrations.
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PMID:Regulation of glycolytic enzyme RNA transcriptional rates by oxygen availability in skeletal muscle cells. 369 61

The activity and amount of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in muscle of young dystrophic hamsters was reduced to approximately half the level found in control animals. No changes in brain or liver enzyme activity were found. Several other glycolytic enzyme activities and creatine kinase activity in muscle were unchanged, except for modest decreases in aldolase and pyruvate kinase. To assess the synthesis of glyceraldehyde-3-phosphate dehydrogenase, the poly(A)+ RNA was isolated from muscle polysomes of dystrophic and control animals and its activity was assessed in an mRNA-dependent translation system. The translatability of the mRNA for GAPDH found in the dystrophic muscle preparations also was half of that found in the control muscle preparations. Decreases were also found in the translatability of mRNA for tropomyosin.
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PMID:Glyceraldehyde-3-phosphate dehydrogenase mRNA. Activity and amount in dystrophic hamster muscle. 370 72

In three groups of healthy young subjects (n = 33; mean ages 6.4, 13.5, 17.1 years), muscle enzyme activities (creatine kinase, hexose phosphate isomerase, aldolase, pyruvate kinase, lactate dehydrogenase, citrate synthase, fumarase) of the vastus lateralis muscle were investigated to show age-dependent variations. A significant age-dependent increase in aldolase (P less than 0.05) and pyruvate kinase (P less than 0.01) activity and a decrease in fumarase activity (P less than 0.01) were computed. In relation to the age-dependent variation, maximum LDH activities could be measured at an age of 12-14 years; significantly decreased activities of the glycolytic enzymes could only be found in the youngest group.
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PMID:Skeletal muscle enzyme activities in healthy young subjects. 375 6


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