Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The three structural genes rhaA, rhaB and rhaD, that specify the enzymes rhamnose isomerase, rhamnulose kinase and rhamnulose 1-phosphate aldolase respectively, have been cloned from Escherichia coli K-12. The precise location of the genes has been determined by gene complementation analysis and by enzymatic assays of strains transformed with recombinant plasmids containing different parts of the cloned region. The corresponding gene products have been studied by their expression in maxicells. Protein products of 47 kDa, 52-54 kDa and 32 kDa have been assigned to rhamnose isomerase, rhamnulose kinase and rhamnulose 1-phosphate aldolase respectively.
FEMS Microbiol Lett 1989 Dec
PMID:Identification of the rhaA, rhaB and rhaD gene products from Escherichia coli K-12. 255 52

A patient with Graves' disease associated with severe muscle weakness who was finally diagnosed as polymyositis by pathological examination of the muscle is reported. A 28-year-old women was incidentally found to have hyperthyroidism when she consulted a hospital for the evaluation and treatment of anemia in 1979. She was treated with methimazole for approximately a month when she stopped the medication by herself. Approximately two yr later (Nov. 4, 1981) she consulted another hospital with complaints of palpitation and muscle weakness. Diagnosis of hyperthyroidism due to Graves' disease and thyrotoxic myopathy were made, followed by the treatment with radioiodine (4 mCi of 131I). She was further treated with propylthiouracil (PTU). Four yr after the treatment, serum thyroid hormone concentration declined to the lower level than normal and serum TSH concentration increased. She was subsequently treated with synthetic I-T4. Despite the fact she became euthyroid with the treatment, muscle weakness as well as elevated concentrations of muscle enzymes were not improved. Muscle biopsy was made in July 1983, and she was diagnosed as immune polymyositis and treatment with prednisolone and cyclophosphamide in addition to PTU or I-T4, was started. With the treatment, serum LDH decreased to the normal range. However she still has muscle weakness and serum concentrations of CPK and aldolase are still in higher levels than normal range.
J Endocrinol Invest 1989 Dec
PMID:A case of Graves' disease associated with polymyositis. 209 Jun 76

Brass splinters weighing 28 mg were implanted in the center of the vitreous of rabbit eyes. After a few days the well-known infiltration and liquefaction of the vitreous body were observed, together with retinal necrosis. Cellular and lysosomal enzymes usually found only in very low concentrations in the vitreous body increased more than a hundredfold during the inflammatory process and the increasing opacification. The enzymes assayed were lactic dehydrogenase (LDH), phosphofructose aldolase (ALD), glycerinaldehyde phosphate dehydrogenase (GAPDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G-6-PDH), glutathione reductase (GR), beta-N-acetylglucose aminidase (NAcGA), and cathepsin-D. The kinetics of enzyme reproduction in the vitreous suggested that the cellular enzymes of the energy producing metabolism might originate both from the invading leukocytes as well as from the degrading retina. It seems likely that the cathepsin-D occurring in the vitreous originates mainly from the retina, and the beta-N-acetylglucose aminidase mainly from the pigment epithelium. The pathologically increased enzyme activity might well permit diagnostic conclusions concerning the intensity and stage of destruction of the retina by brass poisoning.
Klin Monbl Augenheilkd 1989 Dec
PMID:[Enzyme activities of the retina and vitreous body following experimental implantation of a brass splinter]. 262 23

The proteins of soybean roots undergoing anaerobiosis can be grouped into three classes. Class 1 proteins are induced severalfold and at least 28 of these were identified by in vivo labeling. These proteins include the enzymes alcohol dehydrogenase (ADH), fructose aldolase, pyruvate decarboxylase, phosphoglucomutase, and lactate dehydrogenase. Class 2 proteins include such enzymes as glucose phosphate isomerase, sucrase, and malate dehydrogenase; their specific activity remains constant in aerobiosis or anaerobiosis. The third class of proteins includes those enzymes such as peroxidase whose activity decreases more than 90% after just 1 day in anaerobiosis. Immunoblotting coupled with two-dimensional chromatography of in vitro translated plant extracts demonstrated that ADH level during anaerobiosis is controlled by its mRNA concentration. Little or no mRNA for ADH was detected in aerobically grown roots. This suggests that the increased level of ADH activity is due to de novo synthesis of the mRNA rather than activation of a sequestered mRNA or superactivation of the protein.
Biochem Genet 1989 Dec
PMID:Gene regulation during anaerobiosis in soya roots. 262 97

ATPase activity of uterus and ovary was markedly elevated in presence of gossypol and decreased in presence of lactic acid indicating activation and inhibition of energy metabolism by gossypol and lactic acid respectively. The elevated levels of glycogen in uterus indicate inhibition of glycogenolysis as supported by phosphorylase activity. Whereas in ovary the glycogen depletion indicates activation of glycogenolysis supported by phosphorylase activity. The activity levels of aldolase and G-6-PDH decreased in the uterus in presence of gossypol and increased in presence of lactic acid. The same were elevated in ovary indicating the activation of hexose mono and diphosphate pathways. Lactic acid accumulated in presence of both gossypol and lactic acid with a depletion in level of pyruvic acid in both the tissues. This situation in the uterus indicates the condition of anti-implantation in presence of both gossypol and lactic acid. The NAD-LDH activity was inhibited in presence of gossypol and activated in presence of lactic acid in both tissues.
Indian J Exp Biol 1989 Dec
PMID:In vitro effects of gossypol and lactic acid on rat uterus and ovary during implantation and antiimplantation. 263 59

At pH 7.5, in the presence of 0.1 M KCl, 2 mM MgCl2 and 15 mM phosphate, the binding of 1 molecule of alfa-actinin for each strand of 1000 actin monomers doubles the apparent viscosity of an F-actin solution (12 microM as the monomer). Further binding of one molecule of aldolase for each strand of 280 actin monomers halves the apparent viscosity of the alfa-actinin-F-actin system without any desorption of alfa-actinin. The effect of aldolase is not hindered by the addition of 0.1 mM fructose 1,6-bisphosphate. It is shown that orthophosphate acts as a damper of the regulatory effect of fructose bisphosphate on the interaction between aldolase and microfilaments.
Biochem Int 1989 Dec
PMID:Opposite effects of alfa-actinin and of fructose 1,6-bisphosphate aldolase on the microfilament network. The role of orthophosphate revisited. 263 65

Since the discovery of glucose-6-phosphate dehydrogenase (G6PD) deficiency and pyruvate kinase deficiency, erythroenzymopathies associated with hereditary hemolytic anemia have been extensively investigated. Kinetic and electrophoretic studies have shown that most erythroenzymopathies are caused by the production of a mutant enzyme. Single amino acid substitutions have been determined in G6PD and phosphoglycerate kinase variants by studies of the enzyme. Except for these two enzymes, it has been difficult to purify and to characterize the patient's enzyme because of the low protein contents in red blood cells. Recent advance in recombinant DNA technology has made possible the isolation of normal genomic DNA or cDNA for several enzymes. These results permit us to study the molecular basis of erythroenzymopathies at the nucleotide level. Single base substitutions have been identified in aldolase, triosephosphate isomerase, G6PD and adenylate kinase variants by the cloning and nucleotide sequence of the patients' genes. To date, all of the enzyme-deficient variants which have been investigated are caused by point mutations. An exception is a hemolytic anemia secondary to increased adenosine deaminase (ADA) activity. Red cell ADA activity increases on the order of a hundred-fold in affected individuals. The basic abnormality appears to result from overproduction of structurally normal enzyme due to abnormal translational efficiency.
Rinsho Byori 1989 Dec
PMID:[Pathophysiology and laboratory tests of hemolytic anemia: with special reference to erythroenzymopathies]. 269 73

Fructose-1,6-bisphosphate aldolase A (fructose-bisphosphate aldolase; EC 4.1.2.13) deficiency is an autosomal recessive disorder associated with hereditary hemolytic anemia. To clarify the molecular mechanism of the deficiency at the nucleotide level, we have cloned aldolase A cDNA from a patient's poly(A)+ RNA that was expressed in cultured lymphoblastoid cells. Nucleotide analysis of the patient's aldolase A cDNA showed a substitution of a single nucleotide (adenine to guanine) at position 386 in a coding region. As a result, the 128th amino acid, aspartic acid, was replaced with glycine (GAT to GGT). Furthermore, change of the second letter of the aspartic acid codon extinguished a F ok I restriction site (GGATG to GGGTG). Southern blot analysis of the genomic DNA showed the patient carried a homozygous mutation inherited from his parents. When compared with normal human aldolase A, the patient's enzyme from erythrocytes and from cultured lymphoblastoid cells was found to be highly thermolabile, suggesting that this mutation causes a functional defect of the enzyme. To further examine this possibility, the thermal stability of aldolase A of the patient and of a normal control, expressed in Escherichia coli using expression plasmids, was determined. The results of E. coli expression of the mutated aldolase A enzyme confirmed the thermolabile nature of the abnormal enzyme. The Asp-128 is conserved in aldolase A, B, and C of eukaryotes, including an insect, Drosophila, suggesting that the Asp-128 of the aldolase A protein is likely to be an amino acid residue with a crucial role in maintaining the correct spatial structure or in performing the catalytic function of the enzyme.
Proc Natl Acad Sci U S A 1987 Dec
PMID:Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation. 282 99

The effect of oral administration of endosulfan (12.5 mg/kg body weight), daily, for 4 days was investigated in female rats of 4 different age groups, i.e., 15, 30, 70, and 365 days old. Maximum hyperglycemia, maximum depletion of liver glycogen and maximum inhibition of brain acetylcholine esterase activity were observed in 365-day-old (adult) animals whereas these changes were found to be negligible in 15-day-old animals. A decrease in the activity of liver aldolase was observed in rats of all age groups but maximum decrease was observed in adult rats. In contrast to these changes, erythrocyte (Na+, K+)-ATPase was maximally inhibited in 15-day-old rats. These studies indicated that the toxic effects of endosulfan are age-dependent.
Toxicol Lett 1988 Dec
PMID:Biochemical studies on endosulfan toxicity in different age groups of rats. 285 Nov 97

Daily administration of 2g/kg/day di(2-ethylhexyl)phthalate (DEHP) to immature rats was found to cause testicular atrophy and reduce zinc concentration. Specific activities of testicular enzymes associated with postmeiotic spermatogenic cells, such as lactate dehydrogenase isozyme-X, hyaluronidase and sorbitol dehydrogenase, were lower than those of control by day 10, coincident with degeneration of spermatogenic cells. The specific activities of enzymes associated with premeiotic spermatogenic cells, Sertoli cells or interstitial cells (beta-glucuronidase, gamma-glutamyl transpeptidase and malate dehydrogenase) were higher than those of control by day 10. The specific activities of alcohol dehydrogenase and aldolase, zinc containing enzymes, increased after DEHP treatment in spite of the decrease in zinc concentration in the testis. In conclusion, changes in several testicular cell-specific enzymes appear to be useful biochemical markers of testicular injury induced by testicular toxicants such as DEHP. However, these changes occurred after or simultaneous with massive histological or morphological changes rather than prior to such changes.
Arch Toxicol 1986 Dec
PMID:Testicular atrophy induced by di(2-ethylhexyl)phthalate: changes in histology, cell specific enzyme activities and zinc concentrations in rat testis. 288 30


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>