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)

Lactate dehydrogenase and aldolase activity were reduced in lateral gastrocnemius muscle from two mouse mutants, A2G-adr and 129Re-dy, with abnormal muscle function. The activities of both of these enzymes were significantly reduced in the lateral gastrocnemius muscle from the A2G-adr mice at ages varying from 2 weeks to 32 weeks, whereas the activities in the soleus, heart, liver, and brain were the same as in the control animals. The lactate dehydrogenase isoenzymes in the lateral gastrocnemius and soleus muscles from the A2G mice were quantified, and although those of the soleus were comparable in mutant and control muscle, the lateral gastrocnemius from the adr mutant had reduced activity of LDH 5 and increased activities of the other four isoenzymes. The findings suggest that the adr mutation is expressed in the white (Type II) muscle fibres and not in the red (Type I) fibres or in any of the organs studied. It is suggested that the initiation of differentiation into Type II fibres from the embryonic form is absent or delayed in the A2G mutant. The reduced activities of lactate dehydrogenase and aldolase in 129Re-dy muscle confirm the findings of other workers.
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PMID:Developmental changes in lactate dehydrogenase and aldolase activity of the A2G-adr mouse with abnormal muscle function: further comparison with the 129Re-dy mutant. 673 64

A study was made of the effect of acute treatment of rats with intramuscular chlorophos and trichlorometaphos in a dose of 50 mg/kg on oxidation metabolism. The animals who had received low-grade gluten protein demonstrated, in the course of injections of organophosphorous pesticides, a considerable activation of glycolytic enzymes (aldolase and lactate dehydrogenase--LDH), changes in the spectra of LDH isozymes and an increase in the activity of a non-precipitated fraction of dehydrogenases belonging to the tricarboxylic acid series. This indicates the deterioration of aerobic oxidation and compensatory increase in little effective anaerobic pathway of carbohydrate transformation. In control rats, who had received casein, a full-value protein of animal origin, the administration of pesticides gave rise to insignificant changes, which points to the protective role of balanced nutrition aimed against toxic action of organophosphorous pesticides on oxidation metabolism.
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PMID:[Effect of organophosphate pesticides on oxidative metabolism against a background of a protein-balanced and -imbalanced diet]. 678 41

1. The authors report the results obtained after the action of certain optotoxic substances on several enzyme activities in the retina of the pig. 2. This in vitro study involved enzyme interferences of the following optotoxic agents : ethionamide, d-penicillamine, ethylene diaminotetra-acetic acid (EDTA), disodium and dicobalt salts. The enzyme activities studied involved glycolysis, the enzymes selected being as follows: glucose phosphate isomerase (GPI, E.C. 5.3.1.9), fructose-1,6-diphosphate aldolase (F1-6diPA, E.C. 4.1.2.13), lactate dehydrogenase (LDH, E.C. 1.1.1.27). 3. Following the action of the effectors studied, a marked decrease in the enzyme activities examined was found in the retina. This decrease, of varying rapidity and regularity, went as far in some cases as total inhibition; there was disturbance of glycolysis. 4. These results indicate the existence of interactions with a complex mechanism. It may be noted that all of the effectors studied were chelating agents of divalent metals and the changes which they induced in the enzyme activities examined may be explained by interference of the chelates formed with metal cations, such as Zn++, co-factors or effectors of these glycolysis enzymes (with the exception of GPI). These stable chelates are formed by virtue of the primary amine--NH2, thiol--SH, thionyl-[Formula: see text] groups, i.e. groups belonging to molecules essential to cell metabolism.
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PMID:[Effects of optotoxic substances on several glycolytic enzyme activities in the retina of the pig (author's transl)]. 679 28

In 117 bronchial carcinoma patients hospitalized to receive radiation therapy, the serum levels of aldolase, LDH, alkaline phosphatase, GOT and GPT were checked prior to, during, and following radiation therapy at intervals of 4--6 weeks. Among the enzymes tested, aldolase proved to provide the best screening test for judging prognosis, course of disease and probable occurrence of recurrence or metastases.
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PMID:Enzymatic tests in the prognosis and course controls in bronchial carcinoma patients. 712 55

In rabbits, the right hind limb was immobilized by means of plaster cast for 1, 2, 4 or 6 weeks and the activities of some metabolic enzymes: GOT, GPT, LDH, aldolase and acid phosphatase (in part of lysosomal origin), were examined in the slow m. soleus, and in the fast m. gastrocnemius. The former muscle is known to have mainly an oxidative, while the latter mainly a glycolytic type of metabolism. The activities of enzymes highly involved in the metabolism of the muscle diminished for a certain time during atrophy, then a relative rise occurred. Acid phosphatase activity likewise decreased after an initial relative increase. Reduction of enzymatic activities is explained by the activation of proteolytic enzymes, on the basis of measurements performed in these experiments and of results published by others. The decrease of enzymatic activity was more marked in the muscle which in normal state exhibits higher activity than in the other type of muscle studied. Thus, in the gastrocnemius a high rate of degradation of glycolytic enzymes was observed, while in the soleus degradation of oxidative enzymes prevailed. This phenomenon leads to the dedifferentiation of the muscle cell during immobilization.
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PMID:Experimental studies on hypokinesis of skeletal muscle with different functions. VI. 716 67

The CPK, aldolase, GOT, GPT, and LDH concentrations in the serum and lumbar CSF of 80 patients with neuromuscular diseases and 20 controls were measured. The value obtained in serum was essentially in agreement with the data in the literature. This is the first publications reporting on regular CSF enzyme examinations in different neuromuscular disorders, particularly the results obtained in neurogenic muscular atrophies, which have certain characteristic features. The LDH activity in CSF was decreased in peroneal muscular atrophy, the GPT concentration in CSF was elevated in spinal muscular atrophy, and the mean activity of CSF aldolase was increased in amyotrophic lateral sclerosis. The simultaneous determination of enzymes in serum and CSF can provide valuable information in the research of certain details of pathomechanisms and thus lead to further improvement of diagnosis.
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PMID:Investigations on enzyme activity in the serum and CSF of patients with neuromuscular diseases. 731 27

Authors have treated with allopurinol ten children with progressive muscular dystrophy, whose ages were between 15 months to eleven years. An initial and monthly clinical evaluation of muscular strength, Gowers's sign and pseudohypertrophy was performed. Monthly determinations of CPK, LDH, aldolase, GOT and serum urate; every two months electromyography was also made. In three patients a complete recovery of strength, Gowers's sign was found and at the same time pseudohypertrophy diminished; the age average was three years and four months. In four patients a partial recovery was found; the age average was nine years and four months. In three patients there was no answer to treatment, they were contracted and had deformities, being age average ten years. No variations on monthly controls of CPK, LDH, aldolase and GOT were observed. On these facts their opinion is that allopurinol is an effective drug in the treatment of progressive muscular dystrophy and that its' effectivity is better when treatment is initiated early and, of course, before patients present deformities and contractures.
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PMID:[Allopurinol in progressive muscular dystrophy (author's transl)]. 746 88

A 13-year-old boy with mental retardation developed idiopathic cardiomyopathy and glycogen storage myopathy, but with normal lysosomal enzyme activities, consistent with a syndrome of lysosomal glycogen storage disease with normal acid maltase coined by Danon et al (1981). He was in good health except for WPW syndrome diagnosed at 7 years of age. He had heart murmur with abnormal ECG, elevated serum GOT, GPT, LDH, CK and aldolase levels. An echocardiogram showed obstructive hypertrophic cardiomyopathy. Lysosomal enzyme activities including acid alpha-glucosidase in fibroblasts were within normal limits. In the biopsied biceps brachii muscle, there was a mild variation in fiber size. An approximately 10 percent of myofibers had tiny vacuoles which contained periodic acid Schiff positive granules and were slightly high in acid phosphatase activity. The vacuoles were encircled by membranes with high neuron specific enolase (NSE) and acethylcholin-esterase (AchE) activities. On electron microscopy, numerous autophagic vacuoles scavenging glycogen granules were recognized as seen in acid maltase deficiency. Because the vacuolar membranes were high in NSE and AchE activities, lysosomal membrane formation from the cell membrane may be defective. When one has a patient with mild to moderate mental retardation, idiopathic hypertrophic cardiomyopathy and high serum CK level, muscle biopsy must be performed to rule out the present disorder.
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PMID:[A patient with lysosomal glycogen storage disease with normal acid maltase]. 839 37

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

The ability of glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aldolase, pyruvate kinase (PK), and lactate dehydrogenase muscle-type (LDH(M)), to generate interactive microtubule networks was investigated. Bundles have previously been defined as the parallel alignment of several microtubules and are one form of microtubule networks. Utilizing transmission electron microscopy, interactive networks of microtubules as well as bundles were readily observed in the presence of GAPDH, aldolase, or PK. These networks appear morphologically as cross-linked microtubules, oriented in many different ways. Light scattering indicated that the muscle forms of GAPDH, aldolase, PK and LDH(m) caused formation of the microtubule networks. Triose phosphate isomerase (TPI) and lactate dehydrogenase heart-type (LDH(H)), glycolytic enzymes which do not interact with tubulin or microtubules, did not produce bundles, or interactive networks. Sedimentation experiments confirmed that the enzymes that cross-link also co-pellet with the microtubules. Such cross-linking of microtubules indicate that the enzymes are multivalent with the capability of simultaneous binding to more than one microtubule.
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PMID:Glycolytic enzymes and assembly of microtubule networks. 852 27


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