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PubMed1995

Characterization of a silencer that modulates transcription of the human distal aldolase A promoter.

Transcription from the distal promoter (pL) of the human aldolase A gene is driven by both positive and negative cis-acting elements. With footprinting and gel mobility assays we defined: (i) the position of the negative regulatory cis-element (AldA-NRE), which spans a GA-rich sequence; (ii) the sequence of AldA-NRE, which is critical for protein specific binding and is homologous to other silencer-like motifs. Removal of the negative cis-element fully restores the expression of the distal promoter. Insertion of the AldA-NRE upstream from a heterologous promoter results in a 6-fold decrease in CAT reporter gene expression, suggesting that AldA-NRE might be involved in a more general type of mechanism that mediates repression of gene transcription.

Animals↗
PubMed2000

An overlapping set of DNA elements in the rat aldolase B gene origin/promoter regulates transcription and autonomous replication.

Promoter of the rat aldolase B (AldB) gene is centered on an origin of chromosomal DNA replication in vivo, and it directs autonomous replication upon transfection into cultured cells. Previous studies showed that the 200 bp promoter fragment is necessarily required for the autonomous replication. Here, we identified three cis-elements required for replication within the 200 bp promoter, using autonomously replicating plasmids carrying various mutations and deletions. One is an element that is previously defined as a regulatory element for liver-specific transcription (site C). Other two, purine-rich (site PPu) and A (T)-rich (site A/T) sequences, were those often found in eukaryotic origin regions. Sites C and PPu were found to bind specific nuclear factors in transfected cells, and the results of competitive binding assay implied direct or indirect interaction between sites C and PPu.

Animals↗
PubMed1993

The dual effects of Ca2+ on binding of the glycolytic enzymes, phosphofructokinase and aldolase, to muscle cytoskeleton.

We show here that in rat diaphragm muscle, a short time of incubation with the Ca(2+)-ionophore A23187 induced an increase in cytoskeleton-bound phosphofructokinase (EC 2.7.1.11) and aldolase (EC 4.1.2.13), whereas a longer period of incubation, which causes a pathological rise in intracellular Ca2+, induced a decrease in bound enzymes. Lactate concentration correlated with both phases of Ca2+ action on the binding of the enzymes. The increase in cytoskeleton-bound enzymes could be prevented by treatment with the calmodulin antagonists trifluoperazine or CGS 9343B (a novel, potent, and selective inhibitor of calmodulin activity). These results suggest that calmodulin is involved in the Ca(2+)-induced binding of the enzymes to muscle cytoskeleton.

Animals↗
PubMed1995

Myotube-specific activity of the human aldolase A M-promoter requires an overlapping binding site for NF1 and MEF2 factors in addition to a binding site (M1) for unknown proteins.

The human aldolase A gene is expressed in several tissues through the use of three alternative promoters. The activity of one of the promoters, pM, is restricted to skeletal muscle. We reported previously that a proximal 280 bp pM fragment confers tissue-specific expression to a CAT reporter gene in transgenic mice. This small regulatory region directs expression to muscle composed mainly of fast-twitch fibers. Here we show that a minimal promoter fragment from base-pairs -164 to +45 is sufficient to highly active pM during myoblast differentiation in cell culture and demonstrate that two DNA elements play a major role in this activation. These elements consist of a binding site (M1) for unknown ubiquitous proteins and an overlapping binding site for MEF2 and NF1 families of transcription factors. The NF1 factor constitute the main binding activity on the MEF2/NF1 site and, interestingly, some of the DNA-protein complexes that form with muscle nuclear extracts on the NF1 element differ from those that form with non-muscular extracts.

Animals↗
PubMed1999

Developmental regulation of the aldolase A muscle-specific promoter during in vivo muscle maturation is controlled by a nuclear receptor binding element.

During the post-natal period, skeletal muscles undergo important modifications leading to the appearance of different types of myofibers which exhibit distinct contractile and metabolic properties. This maturation process results from the activation of the expression of different sets of contractile proteins and metabolic enzymes, which are specific to the different types of myofibers. The muscle-specific promoter of the aldolase A gene (pM) is expressed mainly in fast-twitch glycolytic fibers in adult body muscles. We investigate here how pM is regulated during the post-natal development of different types of skeletal muscles (slow or fast-twitch muscles, head or body muscles). We show that pM is expressed preferentially in prospective fast-twitch muscles soon after birth; pM is up-regulated specifically in body muscles only later in development. This activation pattern is mimicked by a transgene which comprises only the 355 most proximal sequences of pM. Within this region, we identify a DNA element which is required for the up-regulation of the transgene during post-natal development in body muscles. Comparison of nuclear M1-binding proteins from young or adult body muscles show no qualitative differences. Distinct M1-binding proteins are present in both young and adult tongue nuclear extracts, compared to that present in gastrocnemius extracts.

Alitretinoin↗
PubMed2000

Detachment of the glycolytic enzymes, phosphofructokinase and aldolase, from cytoskeleton of melanoma cells, induced by local anesthetics.

Cancer cells are characterized by a high rate of glycolysis, which is their primary energy source. An important mechanism that controls glycolysis is the reversible binding of glycolytic enzymes to cytoskeleton. We report here that the local anesthetics, lidocaine and bupivacaine, induced a dose-dependent detachment of the glycolytic enzymes, phosphofructokinase (EC 2.7.1.11) and aldolase (EC 4.1.2.13), from cytoskeleton of B16 melanoma cells. The detachment of glycolytic enzymes from cytoskeleton would reduce the provision of local ATP, in the vicinity of cytoskeleton-membrane and would also affect cytoskeleton structure. We show here that the local anesthetics decreased the viability of melanoma cells. The detachment of the glycolytic enzymes from cytoskeleton, induced by the drugs, preceded melanoma cell death, which indicates that this is an early effect and not a result of cell death. Bupivacaine was more potent than lidocaine both on the glycolytic enzymes and on cell viability. The present results suggest that local anesthetics, and especially bupivacaine, are promising drugs for the treatment of melanoma.

Anesthetics, Local↗
PubMed1993

Saccharomyces cerevisiae phosphoglucose isomerase and fructose bisphosphate aldolase can be replaced functionally by the corresponding enzymes of Escherichia coli and Drosophila melanogaster.

Two glycolytic enzymes, phosphoglucose isomerase and fructose-1,6-bisphosphate aldolase, of Saccharomyces cerevisiae could be replaced by their heterologous counterparts from Escherichia coli and Drosophila melanogaster. Both heterologous enzymes, which show respectively little and no sequence homology to the corresponding yeast enzymes, fully restored wild-type properties when their genes were expressed in yeast deletion mutants. This result does not support notions of an obligatory formation of glycolytic multi-enzyme aggregates in yeast; nor does it support possible regulatory functions of yeast phosphoglucose isomerase.

Animals↗
PubMed1979

Genetic and cytogenetic studies of four glycolytic enzymes in Drosophila melanogaster: aldolase, triosephosphate isomerase, 3-phosphoglycerate kinase, and phosphoglucomutase.

Four glycolytic enzymes in Drosophila melanogaster have been genetically and/or cytogenetically mapped. The structural gene for aldolase (Ald) has been genetically mapped to 3-91.5 and cytogenetically localized to 97A-B. Tpi, the structural gene for triosephosphate isomerase, has been genetically mapped to 3-101.3 and cytogenetically localized to 99B-E. Utilizing closer-flanking markers than the previous mapping, Pgk, the structural gene for 3-phosphoglycerate kinase, has been mapped to 2-5.9; cytogenetically it was found to lie in the interval between 22D and 23E3. The cytogenetic locataion of Pgm, the structural gene for phosphoglucomutase which has been located genetically at 3-43.4, was determined to be in 72D1-5.

Alleles↗
PubMed1977

Kinetics of reactivation of rabbit muscle aldolase after denaturation and dissociation in various solvent media.

The denaturation of aldolase from rabbit muscle in various solvents leads to significant qualitative and quantitative differences with respect to the structural disintegration of the enzyme. The differences refer to the quaternary structure and to the conformation which is changed only slightly in MgCl2 while in guanidine-HCl or urea at pH approximately 2 the molecule is close to the state of the random coil. Using the enzymic activity as a quantitative measure for the refolding process, the reaction order and the rate constants of the processes of structure formation (vi leads to N*) are found to be identical. This observation suggests a common intermediate D in the process of renaturation after denaturation and dissociation in the different solvent media. D may be considered an intermediate state with a defined number of nucleation centers whose rapid formation is predetermined by the aminoacid sequence. As taken from the first order kinetics in the given range of enzyme concentration, transconformation reactions are rate limiting in the obligatory pathway of refolding. At low enzyme concentrations second order steps gain importance which indicates that the enzymic activity is significantly modified by the formation of the native quaternary structure.

Animals↗
PubMed1990

Effect of dietary carbohydrates and ethanol on expression of genes encoding sn-glycerol-3-phosphate dehydrogenase, aldolase, and phosphoglycerate kinase in Drosophila larvae.

The genes encoding glycolytic enzymes in Drosophila form a group of functionally related genes that may be coordinately regulated and thus controlled by common factors. We have examined the effect of dietary carbohydrates and ethanol on expression of the genes encoding glycerol-3-phosphate dehydrogenase (GPDH), aldolase (ALD), and phosphoglycerate kinase (PGK) in D. melanogaster larvae. GPDH activity and transcript abundance increased in response to ethanol and additional amounts of several different carbohydrates. In addition, the levels of two alternatively processed Gpdh transcripts were differentially regulated by the treatments. The nutritional conditions tested had little or no effect on the activities and transcript levels of ALD and PGK. These results indicate that changes in dietary conditions affect expression of specific genes and do not evoke a general response from genes involved in cellular metabolism. The observation that dietary carbohydrates and ethanol increase Gpdh expression without affecting expression of Ald and Pgk reinforces previous suggestions that dietary carbon can be diverted by GPDH from glycolytic catabolism into lipid biosynthesis.

Animals↗
PubMed1985

The histochemical demonstration of fructose diphosphate aldolase activity using a semipermeable membrane technique.

In this communication an enzyme histochemical multistep technique for the demonstration of class 1 fructose-1,6-diphosphate aldolase in heart and skeletal muscle sections is described. With this technique a semipermeable membrane is interposed between the incubating solution and the tissue sections preventing diffusion of the enzyme into the medium during incubation. In the histochemical system the enzyme cleaves the substrate D-fructose-1,6-diphosphate to dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The dihydroxyacetone phosphate is reversibly converted into D-glyceraldehyde-3-phosphate by exogenous and endogenous triose phosphate isomerase. Next the D-glyceraldehyde-3-phosphate is oxidized by exogenous and endogenous glyceraldehyde-3-phosphate dehydrogenase and the electrons are transported concomitantly via NAD+, phenazine methosulphate and menadione to nitro-BT. Sodium azide and amytal are incorporated to block electron transfer to the cytochromes.

Animals↗
PubMed1979

Aldolase and dehydrogenase activities in Spirillum bengal.

Spirillum bengal is unable to grow on sugars, but can utilize different organic acids as carbon sources. Dehydrogenase activities were tested with different substrates and were found highest with lactate, glutamate, acetate, succinate and malate. A low aldolase activity was also detectable.

Cell-Free System↗
PubMed1977

Coupling of fructose-1,6-P2 to aminated agarose by Schiff base reduction. Affinity chromatography of yeast aldolase.

Fructose-1,6-P2 was immobilized by sodium borohydride reduction of the Schiff base formed with aminated agarose (AH-Sepharose 4B). The coupling occurs with high yield (25 mumoles immobilized fructose-1,6-P2 per ml packed gel) at neutral pH and room temperature. Schiff base reduction thus provides a convenient and mild coupling prodecure for sugar phosphates preserving their labile phospho ester bonds. As exemplified by a new isolation procedure for fructose-1,6-P2 aldolase from yeast, sugar phosphates insolubilized in this manner may be used for affinity chromatography of the corresponding enzymes, provided that contaminating unspecific phosphatases are removed in a preceding fractionation step.

Chemical Phenomena↗
PubMed1975

Fructose 1,6-bisphosphate aldolase activity of Rhizobium species.

FDP aldolase was found to be present in the cell-free extracts of Rhizobium leguminosarum, Rhizobium phaseoli, Rhizobium trifolii, Rhizobium meliloti, Rhizobium lupini, Rhizobium japonicum and Rhizobium species from Arachis hypogaea and Sesbania cannabina. The enzyme in 3 representative species has optimal activity at pH 8.4 in 0.2M veronal buffer. The enzyme activity was completely lost by treatment at 60 degrees C for 15 min. The Km values were in the range from 2.38 to 4.55 X 10(-6)M FDP. Metal chelating agents inhibited enzyme activity, but monovalent or bivalent metal ions failed to stimulate the activity. Bivalent metal ions in general were rather inhibitory.

Cell-Free System↗
PubMed1985

Effect of thermodynamic nonideality on the subcellular distribution of enzymes: adsorption of aldolase to muscle myofibrils.

An expression is derived whereby allowance may be made for the effects of thermodynamic nonideality on the biphasic interaction of a macromolecular solute with an immobilized reactant. This quantitative description, written in terms of activity coefficients expressed as virial coefficients on the basis of excluded volume, also takes into account the space-filling effect of an inert macromolecule present in the reaction mixture. Advantage is then taken of the theory to consider the effect of bovine serum albumin on the interaction of aldolase with bovine cardiac muscle myofibrils in I 0.158 imidazole-chloride buffer, pH 6.8. Partition equilibrium studies are used to establish that inclusion of a moderate concentration (14 mg/ml) of serum albumin in reaction mixtures leads to a 35-40% increase in the apparent binding constant written in terms of reactant molarities, and that the enhancement is attributable entirely to nonideality inasmuch as the same thermodynamic binding constant pertains. This investigation of thermodynamic nonideality arising from the space-filling effects of inert macromolecules on enzyme partition reinforces the possibility that some enzymes may be distributed between soluble and adsorbed states in the highly concentrated macromolecular environment of the cell cytoplasm.

Adsorption↗
PubMed1994

Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of the class II fructose-1,6-bisphosphate aldolase gene.

DNA fragment containing Schizosaccharomyces pombe homologue of the class II fructose-1,6-bisphosphate aldolase gene was cloned and sequenced. A long open reading frame, which encodes a polypeptide of 358 amino acid residues, was found in the sequence. Amino acid sequence deduced from the nucleotide sequence is 63% homologous to the amino acid sequence of the enzyme of Saccharomyces cerevisiae. Northern blot analysis revealed that 1.3 kb poly(A)+ RNA is transcribed from this DNA sequence.

Amino Acid Sequence↗