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PubMed1989

Assignment of human aldolase C gene to chromosome 17, region cen----q21.1.

The mapping of the gene coding for human aldolase C has been studied using a specific cDNA probe and genomic blots from a panel of human-hamster somatic cell hybrids. The results show that the aldolase C gene is on chromosome 17. In situ experiments have restricted the mapping to the region 17cen----q21.1. Using the same panel of human-hamster somatic cell hybrids, we have confirmed the localization of aldolase A and B on chromosomes 16 and 9, respectively.

Animals↗
PubMed1985

An immunohistochemical study of aldolase C in normal and neoplastic nervous tissues.

Cellular localization of aldolase C isozyme was examined in the normal human brain and in nervous tissue tumors by the indirect immunoperoxidase method using an antibody to aldolase C. In normal brain tissues, staining was most prominent in astrocytes and Purkinje cells, although faint staining was also occasionally observed in some other neurons. Oligodendroglia and ependymal cells showed no distinct staining. The nervous tissue tumors we examined included 34 gliomas (ten astrocytomas and 24 anaplastic gliomas), 30 medulloblastomas, and seven neuronal tumors. Positive staining was observed in some gliomas, but not in the medulloblastomas and neuronal tumors examined. In gliomas, nine of ten astrocytomas and six of 24 anaplastic gliomas showed positive staining in their main constituent cells. In the remaining gliomas, most constituent cells were unstained or positive cells were only sporadically present. These findings indicated that aldolase C was expressed in some of astrocytic glioma cells as in the normal counterpart, more frequently in more differentiated form.

Brain↗
PubMed1983

Aldolase and adenosine deaminase activity in lymphocytes of patients with glomerulonephritis.

Studies on the adenosine deaminase (ADA) and aldolase activities in lymphocytes were performed in 67 patients with glomerulonephritis (gn) and in 20 healthy individuals from the control group to get an insight into the lymphocyte metabolism. Statistically significant decrease of ADA activity was found in the groups of patients with chronic proliferative gn, membranoproliferative gn, membranous gn and lupus nephritis in comparison with the healthy individuals from the control group. As far as decrease of aldolase activity is concerned it has reached statistical significance in patients with mesangial gn, membranoproliferative gn, membranous gn and lupus nephritis. The lymphocyte metabolism did not show any abnormalities in the enzymatic indicators only in patients with acute proliferative gn and submicroscopic gn. The activity comparison between both enzymes in the lymphocytes, contrasted on the basis of high and low clinical dynamics of gn, revealed a tendency to lower ADA and aldolase activities in patients with high clinical dynamics. However, this difference was at the limit of statistical significance (p less than or equal to 0.10).

Adenosine Deaminase↗
PubMed1995

The promoter from the rice nuclear gene encoding chloroplast aldolase confers mesophyll-specific and light-regulated expression in transgenic tobacco.

The rice genome contains at least four separate loci that encode aldolase isozymes. Among these, the aldolase P (AldP) gene, a nuclear gene coding for chloroplast aldolase, is expressed predominantly in the leaf blade mesophyll cells in rice. To dissect promoter elements that regulate such tissue- or cell type-specific expression, we constructed various AldP promoter-beta-glucuronidase (GUS) fusion genes and transferred them into Nicotiana tabacum (tobacco) plants. Analysis of GUS activities in the transgenic tobacco revealed the presence of at least two elements within 2.0 kb AldP promoter region. One is located within the segment from position -2.0 kb to -1.2 kb and acts as a negative element. The other is a positive element located between -1.2 kb and -0.31 kb that confers developmentally regulated, mesophyll cell-specific expression. In addition, the 1.2 kb rice promoter segment flanking the transcription start site contains an element(s) that serves as target for light induction in tobacco. The results suggest that the AldP gene promoter of rice, a monocot promoter, can function in an essentially physiological manner in the dicot tobacco plant.

Blotting, Northern↗
PubMed1985

Characterization and comparison of soluble and immobilized pig muscle aldolases.

Pig muscle aldolase was insolubilized by covalent attachment to a polyacrylamide matrix containing carboxylic functional groups. The catalytic activity of the Akrilex C-aldolase was 2014 units/g solid, i.e., an activity loss of only about 5% relative to the initial activity. The pH optimum for catalytic activity shifted form 7.25 to 7.5 and the apparent temperature optimum from 313 to 318 K. The Michaelis constant of the insolubilized enzyme was significantly higher than that of the soluble aldolase. Heat- and urea-inactivation experiments revealed that the immobilization increased the stability of the enzyme.

Animals↗
PubMed1989

Immobilization of pig muscle aldolase on a silica-based support.

Pig muscle aldolase was covalently attached to a silica-based support possessing aldehyde functional groups. The activity of the immobilized enzyme was 37 U/g solid, and the specific activity calculated on a bound protein basis was 1.9 U/mg protein. The optimum pH for the catalytic activity was pH 7.5. The apparent optimum temperature was found to be 45 degrees C. The Km app value of the immobilized aldolase with D-fructose 1,6-diphosphate as substrate was 1.25 X 10(-4) M. The conformational stability was improved by the immobilization. The immobilized aldolase was used for the continuous splitting of D-fructose 1,6-diphosphate.

Animals↗
PubMed2003

A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning.

A novel enzyme, D-3-hydroxyaspartate aldolase (D-HAA), catalyzing the conversion of D-3-hydroxyaspartate to glyoxylate plus glycine, was purified to homogeneity from Paracoccus denitrificans IFO 13301. D-HAA is strictly D-specific as to the alpha-position, whereas the enzyme does not distinguish between threo and erythro forms at the beta-position. In addition to D-3-hydroxyaspartate, the enzyme also acts on d-threonine, D-3-3,4-dihydroxyphenylserine, D-3-3,4-methylenedioxyphenylserine, and D-3-phenylserine. The D-HAA gene was cloned and sequenced. The gene contains an open reading frame consisting of 1,161 nucleotides corresponding to 387 amino acid residues. The predicted amino acid sequence displayed 35% and 22% identity with that of the D-threonine aldolase of Arthrobacter sp. DK-38 and Alcaligenes xylosoxidan IFO 12669, respectively. This is the first paper reporting both a purified enzyme with D-3-hydroxyaspartate aldolase activity and also its gene cloning.

Amino Acid Sequence↗
PubMed2003

Identification of the high-virulence clone of group B streptococci by using a probe containing a putative aldolase gene.

A high-virulence clone (HVC) was proposed as causing much of the morbidity and mortality when a collection of group B Streptococcus (GBS) isolates was examined by multi-locus enzyme electrophoresis. HVC isolates could be further distinguished by their inability to grow at 40 degrees C, and a temperature-sensitive aldolase was identified as responsible for this characteristic. In the present study, the HVC was sought in a collection of 57 GBS isolates by hybridization with a probe containing a putative aldolase gene on genomic DNA restriction enzyme digests. Isolates were initially classified as HVC or non-HVC by their inability to grow at 40 degrees C. Three serotype III invasive isolates had the HVC control restriction/hybridization pattern. They were also unable to grow at 40 degrees C. The remaining 11 invasive and all carrier isolates showed a pattern identical to that of the non-HVC control. These results provide additional support for the existence of a highly virulent clonal group among serotype III isolates and suggest that hybridization with a probe containing the aldolase gene on DNA restriction enzyme digests can be an alternative method for identifying highly virulent isolates.

Bacterial Typing Techniques↗
PubMed2005

F-actin, beta-tubulin, aldolase, and fructose-1,6-bisphosphatase in heteropteran ovarioles--I. Immunocytochemical investigations of whole-mounted ovarioles.

The distribution of F-actin, beta-tubulin, aldolase, and fructose-1,6-bisphosphatase (FBPase) in ovarioles of four heteropteran species (Ilyocoris cimicoides, Coreus marginatus, Lygus pratensis, and Notostira elongata) was investigated biochemically and immunocytochemically. Aldolase was found to be uniformly distributed in the cytoplasm of trophocytes and follicular cells, with the highest concentration in prefollicular cells. Its concentration in follicular cells increased during differentiation and reached a peak in ovarian follicles at the stage of late choriogenesis. FBPase was observed in the cytoplasm (weak reaction) and on cell borders (strong reaction) of both germ line and somatic cells. No FBPase or aldolase signal was observed on the F-actin trophic core mesh or on stress fibers.

Actins↗
PubMed1987

Dietary regulation of aldolase isozyme expression in rat intestinal mucosa.

Changes of aldolase A and B protein levels and their mRNA levels due to starvation for 48 h in mucosae of the jejunum, ileum, and colon were determined by Western and Northern blot analyses. In fed rats, B protein and B mRNA were predominant in the jejunum. In the ileum, both A protein and A mRNA, as much as B protein and B mRNA, were present in significant amounts. In the colon, A protein and A mRNA were predominant. The enzyme activity levels in those segments of fed rat intestine were in parallel to total enzyme protein levels (A + B) and also to total mRNA levels (A + B), thus suggesting that aldolase isozyme expression in fed rat intestine is determined mainly at the level of transcription. Starvation for 48 h caused about 30% reduction of both B protein level and B mRNA level in jejunum. In the ileum, both A and B mRNA levels were lowered 30-40% from those of fed rats, while A and B protein levels were reduced slightly (A, 0%; B, 12%). In the colon, starvation caused about 50% increase of A mRNA level and about 10% reduction of A protein level. By measuring the synthetic rate of the enzyme proteins from in vivo [35S]methionine incorporation, the accumulation of A mRNA in this tissue was suggested to be due to the significant fall of the translation rate of A mRNA. The translational and post-translational controls of aldolase isozyme expressions in rat intestines are discussed.

Animals↗
PubMed1979

Interaction of rabbit muscle aldolase with phospholipid liposomes.

The interaction between rabbit muscle fructose diphosphate aldolase and phospholipid model membranes (liposomes) was studied by measurement of the tryptophan fluorescence of the enzyme. Interaction with liposomes decreases intrinsic fluorescence intensity of the enzyme and shifts the emission wavelength maximum to higher values. The effects appear to be strongly dependent on the nature of the phospholipid polar group and on ionic strength. Also, a reversible modification of specific activity of aldolase upon interaction with liposomes was found. It is postulated that aldolase binds to liposomes mainly by electrostatic interactions and that the binding causes a change in the conformation of the enzyme.

Animals↗
PubMed1984

Quantitative characterization of the interactions of aldolase and glyceraldehyde-3-phosphate dehydrogenase with erythrocyte membranes.

Results of studies on the interactions of aldolase and glyceraldehyde-3-phosphate dehydrogenase with erythrocyte ghosts have been reinterpreted by making allowance for possible multivalency of the enzymes in regard to their interactions with matrix sites. It is shown that the curvilinearity of the experimental Scatchard plots may be attributed fully to the formation of enzyme-membrane complexes in which tetravalent enzyme may form crosslinks between several membrane sites. This interpretation of the results is preferable to earlier analyses based on heterogeneity of membrane sites in that (a) it takes into account the tetrameric nature of aldolase and glyceraldehyde-3-phosphate dehydrogenase, and (b) it is consistent with experimental demonstrations that band 3 protein is the sole site for enzyme interaction with the erythrocyte matrix. The dependence on ionic strength of the intrinsic association constant for either interaction is such that the binding of neither aldolase nor glyceraldehyde-3-phosphate dehydrogenase could be detected at ionic strengths in excess of 0.08 I. This finding is discussed in relation to the claims and counterclaims concerning the physiological significance of these interactions between glycolytic enzymes and erythrocyte membranes.

Anion Exchange Protein 1, Erythrocyte↗
PubMed1981

Reversible microsomal binding of hepatic aldolase.

Fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13) partitions between the microsomes and the cytosol when a rat liver homogenate is fractionated by differential centrifugation. Gel electrophoresis and immunodiffusion indicate that the one isozyme present in the liver of the young adult rat is found in both fractions. The association of the aldolase with membranes is differentially sensitive to a variety of metabolites and inorganic salts. In the absence of cellular salts, 1 mM fructose 1,6-bisphosphate or glucose 1,6-bisphosphate elutes 50% of the enzyme from the microsomes. About 9 mM Pi or citrate is necessary to produce the same effect. With other metabolites or inorganic salts higher concentrations are required. The fraction of total enzyme which partitions with the microsomes when a homogenate is submitted to high speed centrifugation, correlates inversely with the level of fructose 1,6-bisphosphate in the supernatant solution and this concentration is higher when the tissue concentration in the homogenate is greater. The Km for fructose 1,6-bisphosphate of 3 . 10(-4) for aldolase bound to microsomes is decreased to 6 . 10(-6) M when the enzyme is dissociated from the membranes with salt. These observations appear relevant to the ongoing discussion regarding the physiological relevance of the subcellular localization of glycolytic enzymes.

Animals↗
PubMed1983

Nucleotide sequence of a cDNA clone for human aldolase B.

Two specific clones for human aldolase B were isolated from a human liver cDNA library using a rat aldolase B cDNA probe. The clones were identified by positive hybridization-selection and one of them was sequenced. The 127 C-terminal residues of the human protein were deduced from this nucleotide sequence analysis. They showed 92% homology with the corresponding previously published amino-acid sequence of rat liver aldolase B.

Amino Acid Sequence↗
PubMed1985

Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver.

Nearly complete cDNA clones for human aldolase A mRNA were isolated from human liver cDNA library and the nucleotide sequence determined. Using the cDNA clone as a probe the length of human aldolase A mRNAs, isolated from the skeletal muscle, liver and placenta tissues, was measured by RNA blotting and estimated to be 1,600 nucleotides for skeletal muscle mRNA and 1,700 nucleotides for both the liver and placenta mRNAs, indicating that different species of mRNA coding for human aldolase A were expressed in the different tissues.

Amino Acid Sequence↗
PubMed1977

Isoelectrofocusing of aldolase B from normal human livers and from livers with hereditary fructose intolerance.

By isoelectrofocusing in thin-layer acrylamide-ampholine gel, normal human aldolase B has been resolved into 5 bands. Moreover we were able to specifically stain (after isoelectrofocusing) the mutated aldolase B in livers with hereditary fructose intolerance, and to show that only the 3 most anodic bands are seen. Some different hypotheses are discussed to account for the microheterogeneity of the normal aldolase B, and for the different isoelectrofocusing pattern found in livers with hereditary fructose intolerance.

Carbohydrate Metabolism, Inborn Errors↗
PubMed1987

Serum aldolase isoenzymes in benign and malignant liver disease.

Using a radio-immunoassay, aldolase A and B isoenzyme concentrations have been measured in the sera of patients in order to assess their specificity and sensitivity in a variety of hepatic disorders. Serum aldolase A has been confirmed to be elevated in some patients with malignant infiltration of the liver, but its sensitivity is not sufficient to be of clinical value. Aldolase B is a sensitive marker of liver cell damage which correlates closely with conventional biochemical markers of inflammation. It appears to distinguish successfully between hepatic and cardiac damage.

Fructose-Bisphosphate Aldolase↗
PubMed1988

Alternative promoter usage by aldolase A during in vitro myogenesis.

Aldolase A in the mouse, as in human and rat, shows tissue-specific variability of message size. In addition, in muscle tissue the mRNA size is also developmentally regulated. In order to determine whether this muscle-specific regulatory mechanism can be reproduced in vitro, we have examined the mRNA species of aldolase A isolated from mouse C2C12 myoblasts and myotubes on Northern blots and by primer extension. We show that aldolase A mRNA increases during in vitro myogenesis; that this induction is accompanied by a change in the message population; and that this change is due to activation of a muscle-specific alternative promoter.

Actins↗