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)

Subunit specific radioimmunoassay for aldolase isozymes were developed for the quantification of human aldolase A and B. Aldolase B immunoreactivities were predominantly high in adult normal liver, while aldolase A was distinctly low. Aldolase A was high, while aldolase B was low in neonatal liver compared with the adult liver. Aldolase A immunoreactivities were almost the same as those of aldolase B in fetal liver (28 weeks). Aldolase A was predominantly found in human hepatoma tissues, whereas aldolase B was distinctly low in the same hepatoma tissues. With regard to human hepatoma cell lines, aldolase A was also predominantly found in HepG2 and PLC/PRF/5 cell lines, whereas aldolase B levels were extremely low. Almost the same results were obtained from mRNA expression of aldolase A and B in human hepatoma cell lines by the method of northern hybridization. Effects of various reagents on differentiation of hepatoma cell lines were investigated. Neither Dimethyl Sulfoxide (DMSO) and 12-O-Tetradecanoylphorbol-13-acetate (TPA), which are known to be the inducers of differentiation of human leukemia cell lines such as HL-60, nor Transforming Growth Factor-beta 1 (TGF-beta 1) and Hepatocyte Growth Factor (HGF), which are known to be growth inhibitors, could cause the differentiation of hepatoma cell lines in the alteration of aldolase isozymes. The same data were shown in mRNA expression of aldolase isozymes. These results suggest that aldolase A immunoreactivities and mRNA expression are both predominantly high in hepatoma cell lines, and the reagents such as DMSO, TPA, TGF-beta 1 and HGF which tried to differentiate the hepatoma cell lines used in this study were not effective in the alteration of aldolase isozymes.
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PMID:[Immunoreactivities and messenger RNA expression of aldolase A and B in human hepatoma cell lines]. 786 61

Evidence for the presence of the enzymes of the Entner-Doudoroff pathway in Helicobacter pylori was obtained using 1H and 31P nuclear magnetic resonance spectroscopy. Bacterial lysates generated 6-phosphogluconate and NADH or NADPH in incubations with glucose-6-phosphate and NAD+ or NADP+, indicating the presence of glucose-6-phosphate dehydrogenase activities. Formation of pyruvate was observed in time courses of incubations of bacterial lysates with 6-phosphogluconate as the only substrate, suggesting the presence of 6-phosphogluconate dehydratase and 2-keto-3-deoxy-6-phosphogluconate aldolase activities. The existence of these enzymes and of triose phosphate isomerase was confirmed by observing the appearance of dihydroxyacetone phosphate in time courses of bacterial lysates incubated with 6-phosphogluconate. Aldolase activity was measured by the production of pyruvate and dihydroxyacetone phosphate in lysates incubated with 2-keto-3-deoxy-6-phosphogluconate as the sole substrate. Dehydrogenase, dehydratase and aldolase activities were observed in several bacterial strains including wild types from fresh isolates. Kinetic parameters were measured for the three activities. The cellular location of the enzymes was investigated by comparing the activities measured in the pellet and supernatant fractions obtained by centrifugation of lysate suspensions. The concentration of compounds causing 50% inhibition of enzyme activity was determined from dose-response curves. The data suggested the presence of two glucose-6-phosphate dehydrogenases linked to NAD+ and NADP+ activities. Using inhibitors differences between the H. pylori and mammalian KDPG aldolases were detected. The presence of these enzyme activities in H. pylori provided evidence for the existence of the Entner-Douderoff pathway in the bacterium.
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PMID:The Entner-Doudoroff pathway in Helicobacter pylori. 803 47

We studied the alteration of aldolase isozymes in the serum and tissues of patients with cancer and other diseases using radioimmunoassays specific for aldolase A, B, and C subunits. Aldolase B was predominantly found in adult liver, where aldolase A and C were distinctly low. Aldolase A and B showed almost the same concentration in fetal liver, while in neonatal liver aldolase B protein concentrations were much higher than aldolase A. In contrast, aldolase A was the predominant isozyme found in hepatoma and gastric cancer tissues, whereas aldolase B was distinctly low in hepatoma tissues, and extremely low in gastric cancer tissues. These results suggest that the aldolase A is a more fetal type of liver isozyme than the aldolase B and C, and aldolase B is a more differentiated type of liver isozyme than aldolase A and C. Serum FDP aldolase activities were elevated in half of patients with liver diseases, all patients with muscle diseases and a few patients with cancer. Serum aldolase A levels were elevated in patients with muscle diseases and cancer, but not elevated in patients with liver diseases. In contrast, serum aldolase B levels were elevated in patients with liver disease, but not elevated in patients with muscle diseases and other diseases without liver injury. Serum aldolase B levels showed a trend to decrease in cancer patients with normal GPT levels. Serum aldolase A/B ratios were significantly increased in cancer patients with normal GPT levels, whereas they showed the decreased levels in patients with liver diseases.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Alteration of aldolase isozymes in serum and tissues of patients with cancer and other diseases. 804 42

Aldolase copelleted with taxol stabilized microtubules with a Bmax = 0.74 moles of aldolase per mole of tubulin dimer. Removal of the carboxy terminals from microtubules with limited subtilisin digestion, decreased binding to 0.16 moles of aldolase per mole of tubulin dimer. Aldolase inhibited subtilisin cleavage of the C-terminals while triose phosphate isomerase, an enzyme that does not interact with microtubules, did not affect subtilisin activity. These data indicate that the carboxy terminals are involved in tubulin-aldolase interactions.
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PMID:Aldolase-tubulin interactions: removal of tubulin C-terminals impairs interactions. 810 23

Seven mares were infected with 20,000 Trichinella spiralis larvae; 2 of them were reinfected 22 wk later with the same amount of larvae. The course of infection in horses was assessed by serology (ELISA), biochemistry (aldolase activity), parasitology and histopathology. In each animal, infection was followed by a significant rise in specific antibody titers culminating at 5-10 wk post-infection (pi) and decreasing thereafter. Reinfection was followed by a slight rise in antibody levels. Aldolase activity increased during the first infection, but was not modified by reinfection. The parasite burden was maximum 20 wk pi (24-145 larvae/g according to localisation) and was very low at 52 wk pi (0.4-5 larvae/g). Compared to mares infected only once, the number of parasites in the reinfected animals was similar 28 wk pi but much lower 40 wk pi. Moreover, 6 wk post-reinfection, the larvae were surrounded by a large inflammatory granuloma which could have been caused by larvae from the reinfection batch. These experiments confirm the susceptibility of horses to Trichinella spiralis and the rapid disappearance of specific antibodies which prevents usual serological methods from being used in the diagnosis of infected animals. Reinfection could help the horse to eliminate the larvae more rapidly.
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PMID:[Biological and parasitic variations in horses infested and reinfested by Trichinella spiralis]. 831 6

Aldolase and glyceraldehyde-3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis are stable only in high concentrations of KCl present within the physiological environment. Data concerning the structural changes in the two enzymes as a result of lowering of salt concentration and changes in pH were obtained by monitoring the intrinsic protein fluorescence in the presence of quenchers. When the KCl concentrations were lowered below 2 M or in the presence of 6 M guanidine hydrochloride, the emission maximum shifted to a longer wavelength, indicating enhanced exposure of tryptophyl residues to the solvent. The spectral characteristics of the two proteins in guanidine hydrochloride and 0.4 M KCl were identical. However, these denatured states appear to be different than those observed after acid denaturation. Further perturbation of fluorescence was observed due to I-, and application of the Stern-Volmer law showed that the total fluorescence was available to the quenchers only in 0.4 M KCl solutions. The unfolding of proteins in 0.4 M KCl was a gradual process which was accompanied by a time-dependent loss in enzyme activity. The activity loss was complete within 30 min for aldolase whereas in the case of GAPDH nearly 3 h was required for the destruction of activity. For both enzymes, inactivation and protein denaturation were strongly correlated. The data on activity and thermostability measurements of the two enzymes in varying concentrations of KCl and potassium phosphate revealed that though both proteins are halophilic, the forces in the maintenance of their stability could be different.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Halophilic class I aldolase and glyceraldehyde-3-phosphate dehydrogenase: some salt-dependent structural features. 842 83

Oxidation of enzyme-substrate carbanion intermediates by extrinsic oxidants may result in irreversible paracatalytic inactivation of certain enzymes. In paracatalytically modified fructose-1,6-bisphosphate aldolase from rabbit muscle the polypeptide chain had been found to be crosslinked at active-site Lys229 (Schiff base forming with substrate) and Lys146 by a phosphorylated three-carbon moiety [Lubini, D. G. E. and Christen, P. (1979) Proc. Natl Acad. Sci. USA 76, 2527-2531]. In the present study, the structure of this crosslink was elucidated by instrumental analysis. Aldolase was paracatalytically modified in the presence of fructose 1,6-bisphosphate and hexacyanoferrate(III). The completely inactivated enzyme was digested with pronase. The crosslinked peptide was isolated by gel filtration and reverse-phase HPLC. Mass spectroscopy, 1H- and 13C-NMR showed that a derivative of dihydroxyacetone phosphate forms an amidine with the epsilon-amino groups of the two lysine residues: [formula: see text]
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PMID:Paracatalytic self-inactivation of fructose-1,6-bisphosphate aldolase. Structure of the crosslink formed at the active site. 851 1

Aldolase deficiency of red blood cell is a rare cause of hereditary hemolytic anemia and now there exists only three patients in the world. We had a 24-year-old man operated on for gallbladder stone secondary to this uncommon disease. He underwent a cholecystectomy under general anesthesia combined with thoracic epidural block, using isoflurane, fentanyl, vecuronium, midazolam and lidocaine. During the surgery serum concentrations of bilirubin, free hemoglobin and LDH showed no change, suggesting a lower incidence of drug-induced hemolysis in the case of aldolase deficiency than in other enzyme deficiency. This fact also provides a useful guide to the choice of anesthetics and related agents. In the postoperative period, however, we found a hemolytic response to fever with a drop in hemoglobin level to 2.5 g.dl-1. Aldolase activity of his red cell is heat labile and an increase in body temperature may aggravate a disturbance in the glycolytic pathway leading to hemolytic crisis. It is thus important to prevent the body temperature from rising when a patient is suffering from hemolytic anemia due to red cell aldolase deficiency.
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PMID:[Anesthesia for a patient with red cell aldolase deficiency]. 851 55

Amide hydrogen exchange has been measured in short segments of intact rabbit muscle aldolase at temperatures of 14-50 degrees C by the protein fragmentation/mass spectrometry method (Zhang Z, Smith DL, 1993, Protein Sci 2:522-531). Deuterium levels in some segments did not change over the temperature range of the measurements, whereas deuterium levels in other segments increased rapidly with temperature. These results demonstrate that the equilibrium constant for local unfolding, Kunf, of some segments increases with temperature in the low temperature range (14-30 degrees C) of this study. Aldolase begins to lose activity at temperatures above 40 degrees C. In the 40-50 degrees C temperature range, Kunf is greater than 10(-4) in some regions and less than 10(-6) in other regions. This wide range of regional stability in the temperature range where aldolase begins to denature is interpreted in terms of cooperative unfolding/folding domains. Regions of highest stability were located along the hydrophobic subunit binding surface. It is proposed that hydrogen exchange might be used to identify unfolding domains in multidomain proteins whose thermodynamic properties have been determined by differential scanning calorimetry.
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PMID:Thermal-induced unfolding domains in aldolase identified by amide hydrogen exchange and mass spectrometry. 881 61

Nine monoclonal mouse anti-human aldolase C antibodies, mAbs A4, A8, B4, B7, B8, C1, D9, E10, and H1, were isolated and characterized. These mAbs fall substantially into four groups according to their reactivity with antigens. (i) Human aldolase C-specific mAbs (B8, D9, and H1). (ii) Type C aldolase-specific mAbs (B4 and E10). (iii) Ubiquitous mAbs, which react with vertebrate aldolases irrespective of type of isozyme and species (A4 and B7). (iv) Sub-ubiquitous mAbs, which are closely similar to the ubiquitous mAbs but differ slightly in terms of antigenic specificity (A8 and C1). Aldolase C-specific mAbs B8, H1, B4, and E10, but not D9, have their epitopes on a region within amino acid positions 79-193 of antigens, where the type-C isozyme group-specific sequence-3 (IGS-3) is situated. In contrast, ubiquitous mAbs A4 and B7 and sub-ubiquitous mAb A8 may have their epitopes on the commonly conserved regions of the three isozyme groups. The epitope of sub-ubiquitous mAb C1 appears to be on the IGS-2/3 but this is yet to be resolved. These nine mAbs can be classified into two groups based on the mode of epitope recognition, which was determined by ELISA, immunoblotting, and immunoprecipitation assays: (i) primary sequence-epitope mAbs such as B4, E10, and B7; and (ii) conformation-epitope mAbs (B8, D9, H1, A4, A8, and C1). Among these mAbs, aldolase C-specific mAbs H1 and E10 appear to be useful as probes for detection of conformational change around the type-C IGS-3 motif of human aldolase C because, when assessed by immunoprecipitation assay, mAb H1 reacts only with human aldolase C but not with CA250 and CA306, while mAb E10 reacts with CA250 and CA306 but not with aldolase C, even though these antigens have a common type-C IGS-3 motif. Similarly, the ubiquitous mAb B7 should serve as a probe for general use to detect vertebrate aldolases irrespective of isozyme groups and species.
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PMID:Monoclonal anti-human aldolase C antibodies that react to the isozyme group-specific sequences and generally conserved sequences of human aldolase C1. 888 19


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