Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ALDOLASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 847 records · Page 47Linked to original sources
PubMed2004

Genes encoding Pir51, Beclin 1, RbAp48 and aldolase b are up or down-regulated in human primary hepatocellular carcinoma.

AIM: To reveal new tumor markers and target genes from differentially expressed genes of primary tumor samples using cDNA microarray. METHODS: The (33 )P labeled cDNAs were synthesized by reverse transcription of message RNA from the liver cancerous tissue and adjacent non-cancerous liver tissue from the same patient and used to hybridize to LifeGrid 1.0 cDNA microarray blot containing 8400 known and unique human cDNA gene targets, and an expression profile of genes was produced in one paired human liver tumor tissue. After a global analysis of gene expression of 8400 genes, we selected some genes to confirm the differential expression using Northern blot and RT-PCR. RESULTS: Parallel analysis of the hybridized signals enabled us to get an expression profile of genes in which about 500 genes were differentially expressed in the paired liver tumor tissues. We identified 4 genes, the expression of three (Beclin 1, RbAp48 and Pir51) were increased and one (aldolase b) was decreased in liver tumor tissues. In addition, the expression of these genes in 6 hepatoma cell lines was also showed by RT-PCR analysis. CONCLUSION: cDNA microarray permits a high throughput identification of changes in gene expression. The genes encoding Beclin 1, RbAp48, Pir51 and aldolase b are first reported that may be related with hepatocarcinoma.

Apoptosis Regulatory Proteins↗
PubMed2000

[Determination of fructose-1,6-diphosphate with aldolase-DNPH by the colorimetric method].

This paper presents a modified method of enzymatic assay for Fructose-1,6-diphosphate(FDP). FDP is split to dihydroxyacetone phosphate (DAP) and glyceraldehyde-3-phosphate (GAP) by the action of aldolase. DAP is hydrolyzed at room temperature to free triose. Under alkaline conditions, the free triose is reacted with 2,4-dinitrophenylhydrazine (DNPH), yielding a 2,4-dinitrophenylhydrazine derivative which dissolve in alkali forming a purple color mixture, with maximum absorption at 540.nm. It is proportional to the contents of FDP. Because the method depends on the colorimetric determination of triose formed from fructose-1,6-diphosphate only by aldolase, glycerophosphate dehydrogenase/triosephosphate isomerase (GDH/TIM) and reduced nicotinamide adenine dinucleotide (NADH) which usually applied in multienzymatic method, are omitted in the modified method. The method is specific, convenient and accuracy for the determination of FDP.

Colorimetry↗
PubMed2001

Aldolase C/zebrin II expression in the neonatal rat forebrain reveals cellular heterogeneity within the subventricular zone and early astrocyte differentiation.

During late gestational and early postnatal development, proliferating cells in the subventricular zones of the lateral ventricles (SVZ) migrate into the gray and white matter of the forebrain and differentiate into astrocytes and oligodendrocytes. Because the cellular composition and structure of the neonatal SVZ is poorly understood, we performed a differential display PCR screen to identify genes preferentially expressed therein. One highly expressed gene encoded aldolase C. We used a specific monoclonal antibody, aldolase C/zebrin II (ALDC/ZII), in combination with markers of glial lineage and proliferation, to characterize the cells that express this gene. In the neonatal SVZ, ALDC/ZII-positive cells, which are generally polygonal and display several processes, have a nonuniform spatial distribution. They do not express vimentin, GFAP, or NG2. A subset of ALDC/ZII-positive cells incorporates bromodeoxyuridine, but progenitors identified by beta-galactosidase expression after infection with recombinant BAG virus do not show ALDC/ZII immunoreactivity. Outside of the SVZ, beta-galactosidase-positive/ALDC/ZII-positive cells have an astrocytic phenotype, suggesting that immunoreactivity was acquired after exit from the SVZ. These studies demonstrate that the neonatal SVZ is composed of different populations of cells that can be characterized by their antigenic phenotype, their proliferative capacity, and their spatial distributions. Nonrandom distributions of different cell types within the SVZ may permit the formation of microenvironments that stimulate the production of cells with specific potentials at appropriate points in development. Analysis of ALDC/ZII expression by astrocyte lineage cells in the neonatal cerebral cortex and white matter may reveal insights into the phenotype and behavior of undifferentiated astrocyte progenitors.

Animals↗
PubMed1975

Biochemical, immunological and genetic studies in leprosy. I. Changes in serum lactate dehydrogenase isoenzymes, creatine phosphokinase and aldolase activity in different forms of leprosy.

Serum lactate dehydrogenase isoenzymes, creatine phosphokinase and aldolase activity were determined in healthy control subjects and in lepromatous and tuberculoid leprosy patients from Ethiopia. Sera from lepromatous patients showed a higher total LDH activity compared with control subject. The values for tuberculoid leprosy patients were similar to those of controls. Sera from normal healthy controls showed a higher proportion of LDH-H form (72%) while lepromatous leprosy patient's sera exhibited a higher proportion of LDH-M form (55%). Tuberculoid leprosy patients showed a pattern similar to that of healthy controls. A possible significance of these observations is discussed. No significant variations were observed in fructose-1,6-diphosphate aldolase activity within the different types of disease and controls. Although creatine phosphokinase levels in different types of leprosy decreased significantly from those of normal healthy, it falls within the reported variation of the activity in normal sera.

Creatine Kinase↗
PubMedDate not supplied

[Effect of yeast mannans on aldolase of rat blood serum].

The activity of aldolase in rat blood serum was studied in experiments in vitro and in vivo as affected by extracellular mannan of Rhodotorula rubra. It was established that in vitro the polysaccharide has an inhibitory effect in the enzyme and in vivo, vice versa, activates it. The maximal activation is observed against a background of the V increase and Km decrease. By the preparative electrophoresis in 7.5% polyakrylamide gel seven isoenzymes of aldolase are obtained. After introduction of the polysaccharide the activity in the individual isoforms of the enzyme increases.

Animals↗
PubMedDate not supplied

[Study of the incorporation of radioactive zinc in Saccharomyces cerevisiae aldolase].

Saccharomyces cerevisiae aldolase concentrates from the culture medium containing ZnSO4 a large amount of Zn which becomes a component part of the enzyme molecular structure. This was made evident by adding to the culture medium 65ZnSO4 and measuring the radioactivity of the aldolase extracted by a Phillips single channel analyzer.

Fructose-Bisphosphate Aldolase↗
PubMed1975

The anomeric form of D-fructose 1,6-bisphosphate used as substrate in the muscle and yeast aldolase reactions.

From a series of rapid quench kinetic experiments, it has been demonstrated that muscle D-fructose bisphosphate aldolase catalyzes the cleavage of beta-D-fructose 1,6-bisphosphate but not that of the alpha anomer, although the alpha anomer may be tightly bound. Yeast D-fructose bisphosphate aldolase appears to utilize both alpha and beta anomers of the substrate, with yeast apoaldolase catalyzing the interconversion of the alpha and beta forms.

Fructose-Bisphosphatase↗
PubMed1976

Isoenzyme transitions of creatine phosphokinase, aldolase and phosphoglycerate mutase in differentiating mouse cells.

Extracts of embryonic mouse tissues (skeletal, cardiac and smooth muscle, and brain) were analysed by Cellogel electrophoresis for their isoenzymic distributions of three enzymes, creatine phosphokinase, aldolase and phosphoglycerate mutase. Embryonic tissues from the 12th day to the end of gestation were examined for isoenzyme transitions, and it was found that the adult forms of these enzymes appeared during gestation. Extracts from cloned teratocarcinoma cells were similarly examined in order to determine their degree of bio-chemical differentiation. Undifferentiated embryonal carcinoma cells contained only the early embryonic forms of all three enzymes, while differentiated cells formed in vivo, and in some cases in vitro, started to express the adult types of creatine phosphokinase and aldolase. Thus, biochemical parallels have been demonstrated between developing embryonic tissues and teratocarcinoma cells differentiating in vitro.

Animals↗
PubMed1990

Fructose-1,6-bisphosphate aldolase preferentially associates to glyceraldehyde-3-phosphate dehydrogenase in a mixture of cytosolic proteins as revealed by fluorescence energy transfer measurements.

Fluorescence energy transfer measurements were implemented for demonstrating the specific character of the interaction between aldolase and glyceraldehyde-3-phosphate dehydrogenase. The enzymes, labeled with monobromobimane (donor) and fluorescein isothiocyanate (acceptor), respectively, were mixed into a cytosol preparation and energy transfer between the two fluorophores was observed to develop. This observation reflecting a contact between the two enzymes, suggests that despite the presence of a multitude of potential macromolecular partners glyceraldehyde-3-phosphate dehydrogenase and aldolase are capable of recognizing each other in the cytoplasm. The idea that in vivo associations of metabolically sequential enzymes may be of physiological benefits is consistent with this result.

Animals↗
PubMed1975

Intracellular localization of fructose 1,6-bisphosphate aldolase.

Submission of a rat liver homogenate made in 250 mM sucrose-1 mM EDTA to centrifugation between 9,500 times g for 10 min and 105,000 times g for 60 min results in the sedimentation of 60 to 70% of the total cellular fructose 1,6-bisphosphate aldolase (EC 4.1.2.13). Under these conditions only about one-quarter of the total triose phosphate dehydrogenase and phosphoglycerate kinase appears in the microsomal fraction. Ultrastructural immunologic localization techniques have demonstrated that the aldolase is associated with the endoplasmic reticulum, in situ. The binding of this enzyme to the membrane is sensitive to changes in pH with an optimum at 6.0, and to increasing concentrations of NaCl and fructose 1,6-bisphosphate, being about 100-fold more sensitive to the ester than to the inorganic salt.

Animals↗
PubMed1990

Partial aldolase B gene deletions in hereditary fructose intolerance.

Hereditary fructose intolerance (HFI) is an autosomal recessive condition caused by a deficiency of aldolase B. We have recently shown that three point mutations in this gene account for approximately 85% of HFI alleles in Europe and the United States and are thus of diagnostic importance. In this paper we define three new lesions in the aldolase B gene: two are large deletions, one of 1.65 kb and one of 1.4 kb; the third is a small deletion of 4 bp. We have determined the breakpoints of these deletions and have demonstrated that the presence of such lesions may complicate the genotyping of individuals for diagnosis of HFI.

Base Sequence↗
PubMed1989

The interaction of fructose-1,6-biphosphate aldolase with liposome membranes: a spin probe technique study.

Thermotropic properties of liposome membranes prepared of bulk bovine erythrocyte membrane lipids, native, or aldolase-modified, were investigated by the ESR method. Breaks were observed in the log 2T parallel vs 1/T plots for two spin labels: tempopalmitate and 5-doxyl-palmitate methyl ester. These phenomena have been interpreted as reflecting structural changes near the lipid bilayer polar heads region. Upon modification with aldolase, the temperature at which the breaks occurred was decreased for both spin probes.

Animals↗
PubMed1985

Coordinate induction of alcohol dehydrogenase 1, aldolase, and other anaerobic RNAs in maize.

Anaerobiosis results in the selective synthesis of a particular set of polypeptides in the maize root including the two alcohol dehydrogenases (Sachs, M. M., Freeling, M., and Okimoto, R. (1980) Cell 20, 761-768), pyruvate decarboxylase (Wignarajah, K., and Greenway, H. (1976) New Phytol. 77, 575-584; Laszlo, A., and St. Lawrence, P. (1983) Mol. Gen. Genet. 192, 110-117), glucose phosphate isomerase (Kelley, P. M., and Freeling, M. (1984) J. Biol. Chem. 259, 673-677) and aldolase (Kelley, P. M., and Freeling, M. (1984) J. Biol. Chem. 259, 14180-14183). This report describes the identification and characterization of cDNA clones to five different mRNA species induced upon anaerobic shock. Immunoprecipitation of hybrid-selected translation polypeptides has determined the identity of the cDNA clone for fructose-1,6-diphosphate aldolase mRNA. Quantitative hybridization analysis of anaerobic mRNAs using the cDNA clones has shown that there is not a simultaneous accumulation of anaerobic mRNAs. Upon reintroduction of air, the anaerobic mRNAs disappear rapidly and at approximately the same rate. A translocation line that generates progeny that contain 1, 2, and 3 doses of the long arm of chromosome one (1L) allowed us to test for clustering of the anaerobic genes; two of the anaerobic genes tested do not reside with Adh 1 and Phi 1 on the long arm of chromosome 1.

Alcohol Dehydrogenase↗
PubMedDate not supplied

Human aldolase A gene: structural organization and expression in tumor cell lines.

The structural intron/exon organization of the cloned human aldolase A gene is reported. The gene is composed of twelve exons, including the coding and the 5' and 3' non-coding regions. Four mRNAs, different at the 5' non-coding region, are transcribed from this gene in a tissue-specific manner. The study of the expression of aldolase A gene in normal liver and neoplastic cell lines demonstrated the resurgence of foetal pattern of expression in all tumor liver cell lines and HeLa cells, thus supporting the foetalism theory for this gene system.

Carcinoma, Hepatocellular↗
PubMed1979

[Clinical and experimental studies on aldolase and its isoenzymes in leukemia and allied hematological disorders (author's transl)].

Relations between clinical course and change in aldolase (ALD) isoenzyme pattern were investigated on the peripheral and bone marrow blood of normal subjects and patients suffering from leukemia, multiple myeloma, hypoplastic anemia and other hematological disorders. Similar examination was performed on human leukemia cells and on sera and leukocytes from Donryu rats inoculated with rat leukemia cells (DBLA-6), induced by NBU. In addition to the enzyme activity, isoenzyme pattern was analyzed electrophoretically. The results obtained were as follows: 1) FDP/F1P ratios of the peripheral and marrow blood were high in untreated leukemia. After the induction therapy, the ratio in the marrow blood was high, but decreased in peripheral blood. 2) In complete remission, both ratios were decreased to normal level. 3) In the early relapse of leukemia, the marrow blood showed a high ratio in spite of normal value in the peripheral blood. During full relapse or reinduction therapy, FDP/F1P ratio remained high in both the peripheral and marrow blood. 4) Atypical hypoplastic leukemia showed a significantly high ratio in the marrow, but a low ratio in the periphery. No difference in either ratio was detected between hypoplastic anemia and normal subjects. 5) Zymogram of leukemia cells from leukemia patients showed that ALD-A was predominant more clearly than in normal leukocytes. ALD in normal leukocytes was composed mainly of ALD-A and its hybrids with ALD-B and ALD-C. 6) The ratio in sera and leukocytes from rats inoculated with DBLA-6 cells was increased with exacerbation of leukemia. ALD-A was predominant in rat leukemia cells on the zymogram. It is concluded that aldolase isoenzymes, especially the FDP/F1P ratio, are useful in estimating clinical course of leukemia, particularly in deciding early relapse of leukemia in bone marrow. These laboratory findings are also useful in differentiating atypical leukemia from hypoplastic anemia.

Adolescent↗
PubMedDate not supplied

[Interaction of aldolase A with lecithin liposomes].

The aldolase A binding to the lecithin liposomes (Kd = 2.4 +/- 0.1 X 10(-3) M) has been shown by the fluorescence and tryptophan phosphorescence at the room temperature. The interaction is accompanied by an increase in the phospholipid bilayer microviscosity, and some conformational changes in the hydrophobic part of the enzyme, pronouncing themselves in Trp-147 environment rigidity, decrease. The observation of membrane viscosity vs. incubation time revealed practically instant enzyme-membrane interaction and no gradual incorporation. The accessibility of the NAD-binding domain of aldolase for NADH in the liposome presence remains unaltered.

Fructose-Bisphosphate Aldolase↗